|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-572 |
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: 813.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGRDLLALPE 95
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQ 175
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 256 IFHRGRHPYTRALLSAVPKlgsmkerllparfpiidiktGESQPVADvkdtvsgGRTPILSVKDLTTRFDIRSGLFGRKS 335
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPR--------------------GDPRPVPP-------DAPPLLEARDLKVWFPIKRGLFRRTV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIePTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDPFASL 415
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPFIEHRLG-TKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:COG4172 376 SPRMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 495 LDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVPVPD 572
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-612 |
0e+00 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 727.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGR------DLL 91
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 ALPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSG 171
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 252 TTDDIFHRGRHPYTRALLSAVPKLGSMKERLLPARFPIIDIKTGESQPVADVKDTVSGGRtPILSVKDLTTRFDIRSGLF 331
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGE-PILQVRNLVTRFPLRSGLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 332 GRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDP 411
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 FASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:PRK10261 411 YASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 492 VSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVPVP 571
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA 570
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 549799341 572 DPARRQIKRNMATDEIRSPIRPVDYVPPQRLYREVSAGHLV 612
Cdd:PRK10261 571 DPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYV 611
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-574 |
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: 690.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKkTSRIEGKVMLGGRDLLALPE 95
Cdd:COG1123 2 TPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH-GGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 eemrKVRGKDISMIFQEPMTSLNPIfPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNaknRFDDYPHQFSGGMRQ 175
Cdd:COG1123 79 ----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLER---RLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 256 IFHRGRhpytraLLSAVPKLGSMKERllparfpiidiktgesqpvadvKDTVSGGRTPILSVKDLTTRFDIRsglfgrKS 335
Cdd:COG1123 230 ILAAPQ------ALAAVPRLGAARGR----------------------AAPAAAAAEPLLEVRNLSKRYPVR------GK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDPFASL 415
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:COG1123 356 NPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVPVPDPA 574
Cdd:COG1123 436 DVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-566 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 530.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 14 SVSPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLL-DKKTSRIEGKVMLGGRDLLA 92
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGG 172
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 253 TDDIFHRGRHPYTRALLSAVPklgsmkerllparfpiidikTGESQPVADvkdtvsgGRTPILSVKDLTTRFDIRSGLFG 332
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEP--------------------SGDPVPLPE-------PASPLLDVEQLQVAFPIRKGILK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIePTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDPF 412
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 ASLDPRMSVGTAIMEPF-IEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 492 VSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMS 566
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
308-612 |
6.33e-161 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 463.43 E-value: 6.33e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 308 SGGRTPILSVKDLTTRFDIRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGY 387
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 EVLKLDKTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSG 467
Cdd:COG4608 81 DITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 548 PRAAVFDNPQHPYTKKLMSAVPVPDPARRQiKRNMATDEIRSPIRP-----------------VDYVPPqrlYREVSAGH 610
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDPERRR-ERIVLEGDVPSPLNPpsgcrfhtrcpyaqdrcATEEPP---LREVGPGH 316
|
..
gi 549799341 611 LV 612
Cdd:COG4608 317 QV 318
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-284 |
3.12e-157 |
|
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: 453.74 E-value: 3.12e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKkTSRIEGKVMLGGRDLLALPEEE 97
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPP-PGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQRV 177
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260
....*....|....*....|....*..
gi 549799341 258 HRGRHPYTRALLSAVPKLGSMKERLLP 284
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIP 266
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
314-579 |
1.16e-130 |
|
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: 385.95 E-value: 1.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDIRSGlfgrksgAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP---TSGDVMLDGYEVL 390
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLDKTTLRTMR-RSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSP--DMMRRFPHEFSG 467
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270
....*....|....*....|....*....|..
gi 549799341 548 PRAAVFDNPQHPYTKKLMSAVPVPDPARRQIK 579
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPDGRRLI 265
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
312-593 |
1.45e-112 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 340.02 E-value: 1.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFDIRSGLFgRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITrLIE-PTSGDVMLDGYEVL 390
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLDKTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQR 470
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRA 550
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 549799341 551 AVFDNPQHPYTKKLMSAVPV--PDPARRQIKrnmATDEIRSPIRP 593
Cdd:PRK11308 241 QIFNNPRHPYTQALLSATPRlnPDDRRERIK---LTGELPSPLNP 282
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-251 |
3.62e-112 |
|
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: 334.86 E-value: 3.62e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGRDLLALPEEe 97
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL-KPTS---GSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIrLLEKVRIPNAKNRFDDYPHQFSGGMRQRV 177
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
311-593 |
3.70e-111 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 336.29 E-value: 3.70e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 311 RTPILSVKDLTTRFDIRSG--LFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYE 388
Cdd:PRK15079 5 KKVLLEVADLKVHFDIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 389 VLKLDKTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPF-IEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSG 467
Cdd:PRK15079 85 LLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 549799341 548 PRAAVFDNPQHPYTKKLMSAVPVPDParrQIKRN----MATDEIRSPIRP 593
Cdd:PRK15079 245 TYDEVYHNPLHPYTKALMSAVPIPDP---DLERNktiqLLEGELPSPINP 291
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-283 |
8.47e-107 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 325.14 E-value: 8.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 6 TSMEQTGGSvSPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSRIEGKVML 85
Cdd:PRK09473 1 TVPLAQQQA-DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGGSATF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 86 GGRDLLALPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDY 165
Cdd:PRK09473 79 NGREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 549799341 246 DVVETGTTDDIFHRGRHPYTRALLSAVPKLGSMKERLL 283
Cdd:PRK09473 239 RTMEYGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLL 276
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
314-547 |
3.56e-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: 311.75 E-value: 3.56e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLD 393
Cdd:cd03257 1 LLEVKNLSVSF-------PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAA-DLLEKVGLSPDMMRRFPHEFSGGQRQR 472
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-288 |
4.17e-101 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 310.52 E-value: 4.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDkktsrIEGKVM-----LGGRDLLA 92
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-----YPGRVMaekleFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGG 172
Cdd:PRK11022 78 ISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 549799341 253 TDDIFHRGRHPYTRALLSAVPKLGSMKERL--LPARFP 288
Cdd:PRK11022 238 AHDIFRAPRHPYTQALLRALPEFAQDKARLasLPGVVP 275
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-273 |
1.89e-100 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 308.58 E-value: 1.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGW----KSVVR---NMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKkTSrieGKVMLGGRD 89
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLfgrtVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP-TS---GEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LLALPEEEMRKVRgKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRI-PNAKNRfddYPHQ 168
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
250 260
....*....|....*....|....*
gi 549799341 249 ETGTTDDIFHRGRHPYTRALLSAVP 273
Cdd:COG4608 238 EIAPRDELYARPLHPYTQALLSAVP 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
315-569 |
2.02e-93 |
|
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: 287.47 E-value: 2.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:COG1124 2 LEVRNLSVSY-------GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttlRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGtkqQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIA 474
Cdd:COG1124 75 ---KAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFD 554
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*
gi 549799341 555 NPQHPYTKKLMSAVP 569
Cdd:COG1124 229 GPKHPYTRELLAASL 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
312-574 |
2.57e-90 |
|
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: 289.28 E-value: 2.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP----TSGDVMLDGY 387
Cdd:COG4172 4 MPLLSVEDLSVAF-------GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 EVLKLDKTTLRTMR-RSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLsPD---MMRRFPH 463
Cdd:COG4172 77 DLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDperRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260 270
....*....|....*....|....*....|.
gi 549799341 544 VEIGPRAAVFDNPQHPYTKKLMSAVPVPDPA 574
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-273 |
1.09e-79 |
|
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: 252.03 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLlalpEEEM 98
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKS-TLLRALAGLERPWS---GEVTFDGRPV----TRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHqdiSSSAAKAEVIRLLEKVRIPNA-KNRfddYPHQFSGGMRQRV 177
Cdd:COG1124 74 RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPPSfLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 549799341 258 HRGRHPYTRALLSAVP 273
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-276 |
1.44e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 254.83 E-value: 1.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGRDLLALPEE 96
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISS-----SAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSG 171
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260
....*....|....*....|....*
gi 549799341 252 TTDDIFHRGRHPYTRALLSAVPKLG 276
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMPDFR 266
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-273 |
1.58e-79 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 254.63 E-value: 1.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGG----WK-----SVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTsriEGKVMLGG 87
Cdd:PRK15079 7 VLLEVADLKVHFDIKDGkqwfWQppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV-KAT---DGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 88 RDLLALPEEEMRKVRgKDISMIFQEPMTSLNPIFPIGKQIAEAL-TVHQDISSSAAKAEVIRLLEKVRI-PNAKNRfddY 165
Cdd:PRK15079 83 KDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLINR---Y 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260
....*....|....*....|....*...
gi 549799341 246 DVVETGTTDDIFHRGRHPYTRALLSAVP 273
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
312-567 |
3.89e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 248.60 E-value: 3.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFDIRSGLFGRKSgaVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYevlK 391
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRRQQ--FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFiehRLGTK---QQAREKAADLLEKVGLSPDMMRRFPHEFSGG 468
Cdd:COG4167 77 LEYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPL---RLNTDltaEEREERIFATLRLVGLLPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 469 QRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGP 548
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*....
gi 549799341 549 RAAVFDNPQHPYTKKLMSA 567
Cdd:COG4167 234 TAEVFANPQHEVTKRLIES 252
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
38-271 |
6.77e-78 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 246.51 E-value: 6.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGRDLLALpeeemrKVRGKDISMIFQEPMTSL 117
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPIGKQIAEALTVHQDISSSAaKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTT 197
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSKQA-RALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 198 ALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYTRALLSA 271
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
17-272 |
3.96e-71 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 230.08 E-value: 3.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvDGGWKSVV--RNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKV-----MLGGRD 89
Cdd:COG4107 7 PLLSVRGLSKRY--GPGCGTVVacRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPTSGSVyyrdrDGGPRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LLALPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAknRFDDYPHQF 169
Cdd:COG4107 81 LFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEIPLE--RIDDLPRTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:COG4107 159 SGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVE 238
|
250 260
....*....|....*....|...
gi 549799341 250 TGTTDDIFHRGRHPYTRALLSAV 272
Cdd:COG4107 239 SGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-281 |
1.03e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 231.39 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGW---KSVVR---NMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDL 90
Cdd:PRK11308 4 PLLQAIDLKKHYPVKRGLfkpERLVKaldGVSFTLERGKTLAVVGESGCGKS----TLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 91 LAlPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRI-PNAKNRfddYPHQF 169
Cdd:PRK11308 80 LK-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260 270
....*....|....*....|....*....|..
gi 549799341 250 TGTTDDIFHRGRHPYTRALLSAVPKLGSMKER 281
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLSATPRLNPDDRR 267
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
314-578 |
1.22e-66 |
|
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: 218.52 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFdiRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLD 393
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPfIEHRLGTKQQARE-KAADLLEKVGLSPDMMRRFPHEFSGGQRQR 472
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEP-LRHLTSLDESEQKaRIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250 260
....*....|....*....|....*.
gi 549799341 553 FDNpQHPYTKKLMSAVPVPDPARRQI 578
Cdd:TIGR02769 239 LSF-KHPAGRNLQSAVLPEHPVRRSI 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
308-569 |
6.14e-64 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 213.82 E-value: 6.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 308 SGGRTPILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP---TSGDVML 384
Cdd:PRK09473 6 QQQADALLDVKDLRVTF-------STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 385 DGYEVLKLDKTTLRTMR-RSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLsPDM---MRR 460
Cdd:PRK09473 79 NGREILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEArkrMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 461 FPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYL 540
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 237
|
250 260
....*....|....*....|....*....
gi 549799341 541 GEIVEIGPRAAVFDNPQHPYTKKLMSAVP 569
Cdd:PRK09473 238 GRTMEYGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-273 |
6.74e-62 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 216.26 E-value: 6.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGWKS-------VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRD 89
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ----GGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LLALPEEEMRKVRgKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRI-PNAKNRfddYPHQ 168
Cdd:PRK10261 388 IDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWR---YPHE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
250 260
....*....|....*....|....*
gi 549799341 249 ETGTTDDIFHRGRHPYTRALLSAVP 273
Cdd:PRK10261 544 EIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
312-577 |
2.97e-61 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 204.54 E-value: 2.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdiRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:PRK10419 1 MTLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPfIEHRLGTKQQARE-KAADLLEKVGLSPDMMRRFPHEFSGGQR 470
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREP-LRHLLSLDKAERLaRASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVE---IG 547
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVG 237
|
250 260 270
....*....|....*....|....*....|
gi 549799341 548 PRAAVfdnpQHPYTKKLMSAVPVPDPARRQ 577
Cdd:PRK10419 238 DKLTF----SSPAGRVLQNAVLPAFPVRRR 263
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-271 |
1.11e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 194.67 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 15 VSPVLSVQNLTTSFRVDGGW-----KSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRD 89
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKS----TLAKMLAGIIEPTSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LlalpEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRI-PNAKNrfdDYPHQ 168
Cdd:COG4167 77 L----EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHAN---FYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 549799341 249 ETGTTDDIFHRGRHPYTRALLSA 271
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIES 252
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
314-568 |
2.46e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 190.21 E-value: 2.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLkLD 393
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDpFaSLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRI 473
Cdd:COG1126 69 KKDINKLRRKVGMVFQQ-F-NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 474 AIARSLMLDPKVIVADEAVSALD-----------VSIKAQ----VCnllldlqqnlnlaflfISHDMAVVERVSHRVAVM 538
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDpelvgevldvmRDLAKEgmtmVV----------------VTHEMGFAREVADRVVFM 209
|
250 260 270
....*....|....*....|....*....|
gi 549799341 539 YLGEIVEIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:COG1126 210 DGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
314-567 |
3.17e-56 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 191.16 E-value: 3.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDIRSGLFGRKSgaVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEvLKLD 393
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQT--VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP-LHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRrsVQMIFQDPFASLDPRMSVGTAIMEPFiehRLGTK--QQAREKAADL-LEKVGLSPDMMRRFPHEFSGGQR 470
Cdd:PRK15112 81 DYSYRSQR--IRMIFQDPSTSLNPRQRISQILDFPL---RLNTDlePEQREKQIIEtLRQVGLLPDHASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRA 550
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*..
gi 549799341 551 AVFDNPQHPYTKKLMSA 567
Cdd:PRK15112 236 DVLASPLHELTKRLIAG 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-291 |
4.08e-56 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 192.71 E-value: 4.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLlDKKTSRIEGKVM-LGGRDLLALPE 95
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMrFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTV-------HQDISSSAAKAevIRLLEKVRIPNAKNRFDDYPHQ 168
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGwtykgrwWQRFGWRKRRA--IELLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 549799341 249 ETGTTDDIFHRGRHPYTRALLSAVPKLGSM---KERL--LPARFPIID 291
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLntLPGAIPLLE 286
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
331-569 |
1.51e-55 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 191.11 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEpTSGDVMLDGYEVLKLDKTTLRTMRR------SV 404
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRISEKERrnlvgaEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 405 QMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLsPDMMRR---FPHEFSGGQRQRIAIARSLML 481
Cdd:PRK11022 92 AMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 482 DPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYT 561
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYT 250
|
....*...
gi 549799341 562 KKLMSAVP 569
Cdd:PRK11022 251 QALLRALP 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
312-573 |
1.52e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 196.85 E-value: 1.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfgRKSGAVH-AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRL-----IEPTSGDVMLD 385
Cdd:PRK15134 3 QPLLAIENLSVAF--------RQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 386 GYEVLKLDKTTLRTMR-RSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGL--SPDMMRRFP 462
Cdd:PRK15134 75 GESLLHASEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 463 HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGE 542
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|.
gi 549799341 543 IVEIGPRAAVFDNPQHPYTKKLMSAVPVPDP 573
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQKLLNSEPSGDP 265
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
331-580 |
2.34e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.06 E-value: 2.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQD 410
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 pFASLDPRmsvgTA---IMEPFiEHrLGT-KQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVI 486
Cdd:COG1135 91 -FNLLSSR----TVaenVALPL-EI-AGVpKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 487 VADEAVSALD-------------------VSIkaqvcnllldlqqnlnlafLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:COG1135 163 LCDEATSALDpettrsildllkdinrelgLTI-------------------VLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
250 260 270
....*....|....*....|....*....|...
gi 549799341 548 PRAAVFDNPQHPYTKKLMSAVPVPDPARRQIKR 580
Cdd:COG1135 224 PVLDVFANPQSELTRRFLPTVLNDELPEELLAR 256
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-327 |
2.57e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.06 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEM 98
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLERPTS---GSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQEP--MTSLNpifpIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQR 176
Cdd:COG1135 78 RAAR-RKIGMIFQHFnlLSSRT----VAENVALPLEI-AGVPKAEIRKRVAELLELVGL---SDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 177 VMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 257 FHRGRHPYTRALLSAVPKLGsmkerlLPARFPIIDIKTGESQPVADVKDTVSGGRTPILSvkDLTTRFDIR 327
Cdd:COG1135 229 FANPQSELTRRFLPTVLNDE------LPEELLARLREAAGGGRLVRLTFVGESADEPLLS--ELARRFGVD 291
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-272 |
2.00e-54 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 185.90 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGwksvVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGR-----DLL 91
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLAPDAGEVHYRMRdgqlrDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 ALPEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTV-----HQDISSSAAkaeviRLLEKVRIPnaKNRFDDYP 166
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAvgarhYGDIRATAG-----DWLERVEID--AARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 167 HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGD 246
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|....*.
gi 549799341 247 VVETGTTDDIFHRGRHPYTRALLSAV 272
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
38-271 |
6.38e-54 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 184.52 E-value: 6.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGRDLLAlpeeemRKVRGKDISMIFQEPMTSL 117
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAP------CALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPIGKQIAEALtvhQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTT 197
Cdd:PRK10418 93 NPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 198 ALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYTRALLSA 271
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-249 |
6.59e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 183.32 E-value: 6.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPE 95
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLDRPTS---GEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQEPmtSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQ 175
Cdd:COG1136 78 RELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGL---GDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMgVVAEVSDRTIVMFRGDVVE 249
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
18-272 |
1.81e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 182.50 E-value: 1.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAlPEEE 97
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLEEPDS---GTITVDGEDLTD-SKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRgKDISMIFQE----P-MTSL-NpifpigkqIAEALTVHQDISSSAAKAEVIRLLEKVRIPNaknRFDDYPHQFSG 171
Cdd:COG1126 72 INKLR-RKVGMVFQQfnlfPhLTVLeN--------VTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
250 260
....*....|....*....|.
gi 549799341 252 TTDDIFHRGRHPYTRALLSAV 272
Cdd:COG1126 219 PPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-242 |
1.13e-52 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 179.61 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEM 98
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPTS---GEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEPmtSLNPIFPIGKQIAEALTVHQdISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVM 178
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNH---YPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMgVVAEVSDRTIVM 242
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-552 |
1.56e-51 |
|
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: 185.78 E-value: 1.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSVTsLSIMRLLD------------------------- 73
Cdd:TIGR03269 1 IEVKNLTKKF--DG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDqyeptsgriiyhvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 74 ----KKTSRIEGKVMLGGRDLLALPEEEMRKVRgKDISMIFQEPMtSLNPIFPIGKQIAEALtvhQDISSSAAKAeVIRL 149
Cdd:TIGR03269 76 skvgEPCPVCGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEAL---EEIGYEGKEA-VGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 150 LEKVRIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDM 229
Cdd:TIGR03269 150 VDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 230 GVVAEVSDRTIVMFRGDVVETGTTDDIFHRgrhpytraLLSAVPKLGSMKErllparfpiidIKTGEsqpvadvkdtvsg 309
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVAV--------FMEGVSEVEKECE-----------VEVGE------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 310 grtPILSVKDLTTRFdirsglFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDV-MLDGYE 388
Cdd:TIGR03269 278 ---PIIKVRNVSKRY------ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 389 VLklDKTTLRTMRRS-----VQMIFQDpfASLDPRMSVGTAIMEPfIEHRLgTKQQAREKAADLLEKVGLSPD----MMR 459
Cdd:TIGR03269 349 WV--DMTKPGPDGRGrakryIGILHQE--YDLYPHRTVLDNLTEA-IGLEL-PDELARMKAVITLKMVGFDEEkaeeILD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 460 RFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMY 539
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
570
....*....|...
gi 549799341 540 LGEIVEIGPRAAV 552
Cdd:TIGR03269 503 DGKIVKIGDPEEI 515
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
22-300 |
1.89e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.77 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 22 QNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEMRKV 101
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPTS---GRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 102 RgKDISMIFQE-PMTSLNPIFpigKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIA 180
Cdd:PRK11153 81 R-RQIGMIFQHfNLLSSRTVF---DNVALPLEL-AGTPKAEIKARVTELLELVGLSDKADR---YPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 181 MALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRG 260
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 549799341 261 RHPYTRALLSAV-------PKLGSMKERLLPARFPIIDIK-TGES--QPV 300
Cdd:PRK11153 233 KHPLTREFIQSTlhldlpeDYLARLQAEPTTGSGPLLRLEfTGESvdAPL 282
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
17-272 |
3.11e-51 |
|
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: 177.33 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdGGWKSVvRNMSFEIAPRETVAIVGESGSGKS--VTSLSIMRLLDKKTSRIEGKVMlGGRDLLALP 94
Cdd:TIGR02323 2 PLLQVSGLSKSY---GGGKGC-RDVSFDLYPGEVLGIVGESGSGKStlLGCLAGRLAPDHGTATYIMRSG-AELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPnaKNRFDDYPHQFSGGMR 174
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEID--PTRIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 175 QRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTD 254
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
250
....*....|....*...
gi 549799341 255 DIFHRGRHPYTRALLSAV 272
Cdd:TIGR02323 235 QVLDDPQHPYTQLLVSSI 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-257 |
6.52e-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: 6.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEE 97
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPTS---GSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRgKDISMIFQE--PMTSLNpifpIGKQIAEALTVHQdISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQ 175
Cdd:cd03258 77 LRKAR-RRIGMIFQHfnLLSSRT----VFENVALPLEIAG-VPKAEIEERVLELLELV---GLEDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
..
gi 549799341 256 IF 257
Cdd:cd03258 228 VF 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
331-568 |
1.21e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 178.46 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQD 410
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 pFASLDPRMSVGTAIMEPFIEHRlgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PRK11153 91 -FNLLSSRTVFDNVALPLELAGT--PKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQST 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-269 |
1.98e-50 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 174.40 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGRDLLALPEE 96
Cdd:COG1127 4 PMIEVRNLTKSF---GD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL-RPDS---GEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRgKDISMIFQEP--MTSLNpifpIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMR 174
Cdd:COG1127 76 ELYELR-RRIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 175 QRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTD 254
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|....*
gi 549799341 255 DIFHRGrHPYTRALL 269
Cdd:COG1127 228 ELLASD-DPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
331-557 |
4.31e-50 |
|
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: 173.54 E-value: 4.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQD 410
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 pFASLDPRmSVGTAIMEPFIEHRLGtKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:cd03258 91 -FNLLSSR-TVFENVALPLEIAGVP-KAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
313-569 |
7.38e-50 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 175.86 E-value: 7.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDIRSGLfgrksgaVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPT---SGDVM-LDGYE 388
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGR-------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvTADRFrWNGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 389 VLKLDKTTLRT-MRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEHRLGTK-----QQAREKAADLLEKVGL--SPDMMRR 460
Cdd:COG4170 75 LLKLSPRERRKiIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIkdHKDIMNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 461 FPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYL 540
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYC 234
|
250 260
....*....|....*....|....*....
gi 549799341 541 GEIVEIGPRAAVFDNPQHPYTKKLMSAVP 569
Cdd:COG4170 235 GQTVESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-272 |
9.63e-49 |
|
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: 170.76 E-value: 9.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDG-----GWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLA 92
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKS----TLARLLLGLEKPAQGTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEEEMRKVRgKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNakNRFDDYPHQFSGG 172
Cdd:TIGR02769 78 LDRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
250 260
....*....|....*....|
gi 549799341 253 TDDIFHRgRHPYTRALLSAV 272
Cdd:TIGR02769 235 VAQLLSF-KHPAGRNLQSAV 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-286 |
4.50e-48 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 169.10 E-value: 4.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRVDG-----GWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDL 90
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKS----TLARLLVGLESPSQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 91 LALPEEEMRKVRgKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKnrFDDYPHQFS 170
Cdd:PRK10419 77 AKLNRAQRKAFR-RDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSV--LDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVET 250
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 549799341 251 GTTDDIFHRgRHPYTRALLSAVpklgsmkerlLPAR 286
Cdd:PRK10419 234 QPVGDKLTF-SSPAGRVLQNAV----------LPAF 258
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
311-562 |
7.99e-48 |
|
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: 167.46 E-value: 7.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 311 RTPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVL 390
Cdd:COG1127 2 SEPMIEVRNLTKSF-----------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLDKTTLRTMRRSVQMIFQDP--FASldprMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLsPDMMRRFPHEFSGG 468
Cdd:COG1127 71 GLSEKELYELRRRIGMLFQGGalFDS----LTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 469 QRQRIAIARSLMLDPKVIVADEAVSALD-----------VSIKAQvcnllldlqqnLNLAFLFISHDMAVVERVSHRVAV 537
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDpitsavideliRELRDE-----------LGLTSVVVTHDLDSAFAIADRVAV 214
|
250 260
....*....|....*....|....*
gi 549799341 538 MYLGEIVEIGPRAAVFDNPqHPYTK 562
Cdd:COG1127 215 LADGKIIAEGTPEELLASD-DPWVR 238
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
311-560 |
3.45e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 169.51 E-value: 3.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 311 RTPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVl 390
Cdd:COG3842 2 AMPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 kldkTTLRTMRRSVQMIFQDpFAsLDPRMSVGTAIMEPfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQR 470
Cdd:COG3842 70 ----TGLPPEKRNVGMVFQD-YA-LFPHLTVAENVAFG-LRMRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHD----MAvverVSHRVAVMYLGEIVEI 546
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQV 217
|
250
....*....|....
gi 549799341 547 GPRAAVFDNPQHPY 560
Cdd:COG3842 218 GTPEEIYERPATRF 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
313-552 |
1.58e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 164.46 E-value: 1.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKL 392
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKTTLRTMRRSVQMIFQDPfaSLDPRMSVGTAIMepfieH-RLGTK-----------QQAREKAADLLEKVGLSPDMMRR 460
Cdd:COG3638 71 RGRALRRLRRRIGMIFQQF--NLVPRLSVLTNVL-----AgRLGRTstwrsllglfpPEDRERALEALERVGLADKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 461 fPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYL 540
Cdd:COG3638 144 -ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 549799341 541 GEIVEIGPRAAV 552
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-266 |
1.62e-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: 163.83 E-value: 1.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVtslsIMRL---LDKKTSrieGKVMLGGRDLLALPE 95
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKST----LLRLivgLLRPDS---GEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRgKDISMIFQEP--MTSLNpifpIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGM 173
Cdd:cd03261 70 AELYRLR-RRMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTT 253
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
250
....*....|...
gi 549799341 254 DDIFHRgRHPYTR 266
Cdd:cd03261 222 EELRAS-DDPLVR 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
333-570 |
1.86e-46 |
|
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: 164.74 E-value: 1.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRR-SVQMIFQDp 411
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 FAsLDPRMSVGTAIMEPfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:cd03294 111 FA-LLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 492 VSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVPV 570
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDR 266
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
336-547 |
9.56e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 161.15 E-value: 9.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQDPfaSL 415
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNIGMVFQDY--AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:cd03259 84 FPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03259 162 DAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
340-560 |
9.90e-46 |
|
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: 162.08 E-value: 9.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDpfASLDPRM 419
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR---RKIGYVIQQ--IGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTAI-MEPFIEHRLgtKQQAREKAADLLEKVGLSPD-MMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:cd03295 91 TVEENIaLVPKLLKWP--KEKIRERADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 498 SIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPY 560
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
315-538 |
2.54e-45 |
|
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: 159.94 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldk 394
Cdd:cd03293 1 LEVRNVSKTY-------GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttlRTMRRSVQMIFQDPfaSLDPRMSVGTAIMEPfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIA 474
Cdd:cd03293 69 ---TGPGPDRGYVFQQD--ALLPWLTVLDNVALG-LELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDM--AVveRVSHRVAVM 538
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVL 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
19-242 |
3.11e-45 |
|
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: 159.94 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLlalpeeem 98
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIAGLERPTS---GEVLVDGEPV-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rKVRGKDISMIFQEPmtSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVM 178
Cdd:cd03293 69 -TGPGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVM 242
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-259 |
3.89e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.81 E-value: 3.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGRDLLalpEEEM 98
Cdd:COG1122 1 IELENL--SFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL-KPTS---GEVLVDGKDIT---KKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQEPMTslnpifpigkQIAEAlTVHQDI---------SSSAAKAEVIRLLEKVRIPNAKNRfddYPHQF 169
Cdd:COG1122 71 RELR-RKVGLVFQNPDD----------QLFAP-TVEEDVafgpenlglPREEIRERVEEALELVGLEHLADR---PPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|
gi 549799341 250 TGTTDDIFHR 259
Cdd:COG1122 215 DGTPREVFSD 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
331-543 |
2.06e-44 |
|
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: 157.65 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRR-SVQMIFQ 409
Cdd:cd03255 10 YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRrHIGFVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 410 DPfaSLDPRMSVGTAIMEPFIEHRLGtKQQAREKAADLLEKVGLsPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVAD 489
Cdd:cd03255 90 SF--NLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 549799341 490 EAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEI 543
Cdd:cd03255 166 EPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
333-568 |
2.45e-44 |
|
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: 161.94 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRR-SVQMIFQDp 411
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 FAsLDPRMSVGTAImePFIEHRLG-TKQQAREKAADLLEKVGLsPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:TIGR01186 80 FA-LFPHMTILQNT--SLGPELLGwPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-254 |
4.76e-44 |
|
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: 157.21 E-value: 4.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 14 SVSPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAL 93
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPTS---GTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 PEEEMRKVRGKDISMIFQE----P-MTSL-NPIFPigkqiAEaLTVHQDissSAAKAEviRLLEKVRIpnaKNRFDDYPH 167
Cdd:COG4181 80 DEDARARLRARHVGFVFQSfqllPtLTALeNVMLP-----LE-LAGRRD---ARARAR--ALLERVGL---GHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGvVAEVSDRTIVMFRGDV 247
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRL 224
|
....*..
gi 549799341 248 VETGTTD 254
Cdd:COG4181 225 VEDTAAT 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-272 |
6.01e-44 |
|
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: 157.51 E-value: 6.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLttSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPeee 97
Cdd:COG1120 1 MLEAENL--SVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKS----TLLRALAGLLKPSSGEVLLDGRDLASLS--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mRKVRGKDISMIFQEPmtslnpifpigkQIAEALTV----------HQDI---SSSAAKAEVIRLLEKVRIPNAKNRfdd 164
Cdd:COG1120 70 -RRELARRIAYVPQEP------------PAPFGLTVrelvalgrypHLGLfgrPSAEDREAVEEALERTGLEHLADR--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 165 YPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFR 244
Cdd:COG1120 134 PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
250 260
....*....|....*....|....*...
gi 549799341 245 GDVVETGTTDDIFhrgrhpyTRALLSAV 272
Cdd:COG1120 214 GRIVAQGPPEEVL-------TPELLEEV 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
40-257 |
1.68e-43 |
|
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: 156.84 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEMRKVRgKDISMIFQepmtslnp 119
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNGLLKPTS---GTVTIDGRDITAKKKKKLKDLR-KKVGLVFQ-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 120 iFPiGKQIAEAlTVHQDI---------SSSAAKAEVIRLLEKVRIPnaknrfDDY----PHQFSGGMRQRVMIAMALASK 186
Cdd:TIGR04521 90 -FP-EHQLFEE-TVYKDIafgpknlglSEEEAEERVKEALELVGLD------EEYlersPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 187 PKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-245 |
2.22e-43 |
|
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: 154.55 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMR 99
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKS----TLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 100 KvrgkDISMIFQEPMTslnpifpigkQIAeALTVHQDISSSA---------AKAEVIRLLEKVRIPNAKNRfddYPHQFS 170
Cdd:cd03225 75 R----KVGLVFQNPDD----------QFF-GPTVEEEVAFGLenlglpeeeIEERVEEALELVGLEGLRDR---SPFTLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
312-545 |
2.44e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.82 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:COG1136 2 SPLLELRNLTKSY-------GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTLRTMRR-SVQMIFQDPFasLDPRMSVGTAIMEPFIEHRLGtKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQR 470
Cdd:COG1136 75 LSERELARLRRrHIGFVFQFFN--LLPELTALENVALPLLLAGVS-RKERRERARELLERVGLG-DRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVE 545
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
17-242 |
3.09e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.63 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRL---LDKKTSrieGKVMLGGRDLLAL 93
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLiagLEKPTS---GEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 peeemrkvrGKDISMIFQEPmtSLnpiFP---IGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFS 170
Cdd:COG1116 79 ---------GPDRGVVFQEP--AL---LPwltVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDV----TIQGQILDliktLQEEEGMSVLFITHDmgvVAE---VSDRTIVM 242
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLR----LWQETGKTVLFVTHD---VDEavfLADRVVVL 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
336-552 |
3.10e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 154.65 E-value: 3.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIE-----PTSGDVMLDGYEVLKLDKTTLRtMRRSVQMIFQ- 409
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLE-LRRRVGMVFQk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 410 -DPFasldpRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRR-FPHEFSGGQRQRIAIARSLMLDPKVIV 487
Cdd:cd03260 90 pNPF-----PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 488 ADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:cd03260 165 LDEPTSALDPISTAKI--EELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
312-568 |
3.37e-43 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 155.47 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:PRK11701 4 QPLLSVRGLTKLY-----------GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTL------RTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEhrLGTKQ--QAREKAADLLEKVGLSPDMMRRFPH 463
Cdd:PRK11701 73 RDLYALseaerrRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMA--VGARHygDIRATAGDWLERVEIDAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250 260
....*....|....*....|....*
gi 549799341 544 VEIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-259 |
3.94e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.34 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsiMRL---LDKKTSrieGKVMLGGRDLLA 92
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMiagFETPDS---GRILLDGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEEEmrkvRgkDISMIFQEPmtslnPIFP---IGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQF 169
Cdd:COG3842 72 LPPEK----R--NVGMVFQDY-----ALFPhltVAENVAFGLRM-RGVPKAEIRARVAELLELVGLEGLADR---YPHQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
250
....*....|
gi 549799341 250 TGTTDDIFHR 259
Cdd:COG3842 217 VGTPEEIYER 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
315-543 |
4.58e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 4.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFDIRSGLfgrksgavhavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:COG4619 1 LELEGLSFRVGGKPIL-----------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRtmrRSVQMIFQDPFAsldPRMSVGTAIMEPFiehRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIA 474
Cdd:COG4619 70 PEWR---RQVAYVPQEPAL---WGGTVRDNLPFPF---QLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-256 |
7.05e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 153.49 E-value: 7.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDK-KTSRIEGKVMLGGRDLLALPE-- 95
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLiPGAPDEGEVLLDGKDIYDLDVdv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGkdisMIFQEPmtslNPiFP--IGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIP-NAKNRFDdyPHQFSGG 172
Cdd:cd03260 77 LELRRRVG----MVFQKP----NP-FPgsIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRLH--ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
....
gi 549799341 253 TDDI 256
Cdd:cd03260 224 TEQI 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
310-538 |
9.91e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.48 E-value: 9.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 310 GRTPILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV 389
Cdd:COG1116 3 AAAPALELRGVSKRF-------PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 390 LKLDKttlrtmRRSvqMIFQDPfaSLDPRMSVGTAIMEPFiEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQ 469
Cdd:COG1116 76 TGPGP------DRG--VVFQEP--ALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDM--AVveRVSHRVAVM 538
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAV--FLADRVVVL 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-256 |
1.82e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.91 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGRDLLALPEEEM 98
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL-RPTS---GEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvrgkdISMIFQEPmtSLNPIFPIgkqiAEALTVHQD---ISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQ 175
Cdd:COG1131 73 RR-----IGYVPQEP--ALYPDLTV----RENLRFFARlygLPRKEARERIDELLELFGLTDAADR---KVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
.
gi 549799341 256 I 256
Cdd:COG1131 218 L 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
329-552 |
1.89e-42 |
|
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: 153.11 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 329 GLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIF 408
Cdd:cd03256 5 NLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 409 QDPfaSLDPRMSVGTAIMEPfiehRLGTK-----------QQAREKAADLLEKVGLSPDMMRRfPHEFSGGQRQRIAIAR 477
Cdd:cd03256 85 QQF--NLIERLSVLENVLSG----RLGRRstwrslfglfpKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 478 SLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-271 |
3.03e-42 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 153.41 E-value: 3.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 15 VSPVLSVQNLTTSFRVDGGW-----KSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRD 89
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKS----TLAKMLAGMIEPTSGELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LlalpEEEMRKVRGKDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRI-PNAKNRfddYPHQ 168
Cdd:PRK15112 77 L----HFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASY---YPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 549799341 249 ETGTTDDIFHRGRHPYTRALLSA 271
Cdd:PRK15112 230 ERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
315-562 |
5.03e-42 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 151.50 E-value: 5.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFDirsglfgrkSGAVHavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:cd03261 1 IELRGLTKSFG---------GRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDP--FASldprMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDmMRRFPHEFSGGQRQR 472
Cdd:cd03261 70 AELYRLRRRMGMLFQSGalFDS----LTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGA-EDLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|
gi 549799341 553 FDNpQHPYTK 562
Cdd:cd03261 225 RAS-DDPLVR 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
18-249 |
5.07e-42 |
|
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: 150.96 E-value: 5.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRvDGGWKS-VVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEE 96
Cdd:TIGR02211 1 LLKCENLGKRYQ-EGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPTS---GEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRGKDISMIFQepMTSLNPIFPIGKQIA-EALTVHQDISSSAAKAEviRLLEKVripNAKNRFDDYPHQFSGGMRQ 175
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQ--FHHLLPDFTALENVAmPLLIGKKSVKEAKERAY--EMLEKV---GLEHRINHRPSELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGvVAEVSDRTIVMFRGDVVE 249
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQLFN 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
19-251 |
5.07e-42 |
|
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: 150.75 E-value: 5.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEm 98
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIAGLERPDSGEILIDGRDVTGVPPER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rkvrgKDISMIFQEPmtSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVM 178
Cdd:cd03259 72 -----RNIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-245 |
6.42e-42 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 150.37 E-value: 6.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAlPEEEM 98
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEEPDS---GTIIIDGLKLTD-DKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQepmtSLNpIFP---IGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNaknRFDDYPHQFSGGMRQ 175
Cdd:cd03262 72 NELR-QKVGMVFQ----QFN-LFPhltVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
315-543 |
1.11e-41 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 149.99 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKLDK 394
Cdd:cd03262 1 IEIKNLHKSF-----------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDG-LKLTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDpFaSLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIA 474
Cdd:cd03262 69 KNINELRQKVGMVFQQ-F-NLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEV-LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
315-568 |
1.82e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 153.38 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKldk 394
Cdd:COG1118 3 IEVRNISKRF-----------GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-RDLF--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDpFAsLDPRMSVGTAIMepF-IEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRI 473
Cdd:COG1118 68 TNLPPRERRVGFVFQH-YA-LFPHMTVAENIA--FgLRVRPPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 474 AIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVF 553
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
250
....*....|....*
gi 549799341 554 DNPQHPYTKKLMSAV 568
Cdd:COG1118 223 DRPATPFVARFLGCV 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-270 |
2.40e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 150.57 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 8 MEQTGGSVSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSL-SIMRLLDK-KTSRIEGKVML 85
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-TLLrCLNRMNDLiPGARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 86 GGRDLLAlPEEEMRKVRgKDISMIFQEPmtslNPiFP--IGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPN-AKNRF 162
Cdd:COG1117 76 DGEDIYD-PDVDVVELR-RRVGMVFQKP----NP-FPksIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDeVKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 163 DDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTIVM 242
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|....*...
gi 549799341 243 FRGDVVETGTTDDIFHRGRHPYTRALLS 270
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-552 |
3.52e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.33 E-value: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdGGWKsVVRNMSFEIAPRETVAIVGESGSGKSvTslsIMRLL------DkktsriEGKVMLGGRDL 90
Cdd:COG1129 3 PLLEMRGISKSF---GGVK-ALDGVSLELRPGEVHALLGENGAGKS-T---LMKILsgvyqpD------SGEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 91 -LALPEEEMRkvRGkdISMIFQEPmtSLNP-------IFpIGKQIAEALTVHQdissSAAKAEVIRLLEKVRI---PNAK 159
Cdd:COG1129 69 rFRSPRDAQA--AG--IAIIHQEL--NLVPnlsvaenIF-LGREPRRGGLIDW----RAMRRRARELLARLGLdidPDTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 160 NRfddyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRT 239
Cdd:COG1129 138 VG------DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLDEVFEIADRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 240 IVMFRGDVVETGTTDDIfhrgrhpyTRALLSAvpklgSMKERLLPARFPIIDIKTGEsqpvadvkdtvsggrtPILSVKD 319
Cdd:COG1129 211 TVLRDGRLVGTGPVAEL--------TEDELVR-----LMVGRELEDLFPKRAAAPGE----------------VVLEVEG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 320 LTTRfdirsglfgrksgavHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldktTLRT 399
Cdd:COG1129 262 LSVG---------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV------RIRS 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 400 MRRSVQM-------------IFQDpfasldprMSVGT----AIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFP 462
Cdd:COG1129 321 PRDAIRAgiayvpedrkgegLVLD--------LSIREnitlASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 463 HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQV-----------CnllldlqqnlnlAFLFISHDMAVVERV 531
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIyrlirelaaegK------------AVIVISSELPELLGL 460
|
570 580
....*....|....*....|.
gi 549799341 532 SHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG1129 461 SDRILVMREGRIVGELDREEA 481
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-263 |
1.05e-40 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 148.22 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsiMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINRLIEPTSGEIFIDGEDIREQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvrgkDISMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfDDYPHQFSGGMRQRVM 178
Cdd:cd03295 74 RR----KIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAEFA-DRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFh 258
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL- 224
|
....*
gi 549799341 259 rgRHP 263
Cdd:cd03295 225 --RSP 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-557 |
1.14e-40 |
|
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: 147.86 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevLKLDKTTLRTMRRSVQMIFQDPFASL 415
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG---KDITKKNLRELRRKVGLVFQNPDDQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 dprmsVGTAIME-----PFiehRLG-TKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVAD 489
Cdd:COG1122 89 -----FAPTVEEdvafgPE---NLGlPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 490 EAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:COG1122 160 EPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-552 |
1.30e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.80 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdGGwksVV--RNMSFEIAPRETVAIVGESGSGKSvtslSIMRLL------DkktsriEGKVMLGGR 88
Cdd:COG3845 4 PALELRGITKRF---GG---VVanDDVSLTVRPGEIHALLGENGAGKS----TLMKILyglyqpD------SGEILIDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 89 dllalpeeemrKVRGKD--------ISMIFQEPMtslnpifpigkqIAEALTVHQDI------------SSSAAKAEVIR 148
Cdd:COG3845 68 -----------PVRIRSprdaialgIGMVHQHFM------------LVPNLTVAENIvlgleptkggrlDRKAARARIRE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 149 LLEKVRI---PNAKnrfddyPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALdvTIQgQILDLIKTLQE--EEGMSVL 223
Cdd:COG3845 125 LSERYGLdvdPDAK------VEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSII 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 224 FITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIfhrgrhpyTRALLSAvpklgSMkerllparfpiidikTGESQPVADV 303
Cdd:COG3845 196 FITHKLREVMAIADRVTVLRRGKVVGTVDTAET--------SEEELAE-----LM---------------VGREVLLRVE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 304 KDTVSGGRtPILSVKDLTTrfdirsglfgRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVM 383
Cdd:COG3845 248 KAPAEPGE-VVLEVENLSV----------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 384 LDGYEVLKLDKTTLRtmRRSVQMIFQDPFAS-LDPRMSVGT-AIMEPFIEHRLGT-----KQQAREKAADLLEK---VGL 453
Cdd:COG3845 317 LDGEDITGLSPRERR--RLGVAYIPEDRLGRgLVPDMSVAEnLILGRYRRPPFSRggfldRKAIRAFAEELIEEfdvRTP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 454 SPDMMRRFpheFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS--------IKAQvcnllldlqQNLNLAFLFISHDM 525
Cdd:COG3845 395 GPDTPARS---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaiefihqrLLEL---------RDAGAAVLLISEDL 462
|
570 580
....*....|....*....|....*..
gi 549799341 526 AVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG3845 463 DEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
336-557 |
2.35e-40 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 147.00 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDkttlrTMRRSVQMIFQDpFAsL 415
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PHKRPVNTVFQN-YA-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPFIEHRLGtKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:cd03300 84 FPHLTVFENIAFGLRLKKLP-KAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
315-552 |
1.84e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDk 394
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttlRTMRRSVQMIFQDPfaSLDPRMSVGtAIMEPFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIA 474
Cdd:COG1131 69 ---AEVRRRIGYVPQEP--ALYPDLTVR-ENLRFFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-266 |
1.45e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.29 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLA-LPeee 97
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKT-TLLRIIAGLETPDS---GRIVLNGRDLFTnLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mrkVRGKDISMIFQEPMtslnpIFP---IGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMR 174
Cdd:COG1118 72 ---PRERRVGFVFQHYA-----LFPhmtVAENIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 175 QRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTD 254
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
250
....*....|..
gi 549799341 255 DIFhrgRHPYTR 266
Cdd:COG1118 220 EVY---DRPATP 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
17-256 |
1.54e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.50 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSL-SIMRLLDKKtsriEGKVMLGGRDLLALPE 95
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPT----SGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGkDISMIFQEP--------MT--------------SLNPIFPigkqiaealtvhqdissSAAKAEVIRLLEKV 153
Cdd:COG3638 73 RALRRLRR-RIGMIFQQFnlvprlsvLTnvlagrlgrtstwrSLLGLFP-----------------PEDRERALEALERV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 154 RIPN-AKNRFDdyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVV 232
Cdd:COG3638 135 GLADkAYQRAD----QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLA 210
|
250 260
....*....|....*....|....
gi 549799341 233 AEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:COG3638 211 RRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
344-491 |
1.79e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 138.93 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEvlkLDKTTLRTMRRSVQMIFQDPFasLDPRMSVGT 423
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 424 AIMEPFIEHRLgTKQQAREKAADLLEKVGLSPDM---MRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:pfam00005 79 NLRLGLLLKGL-SKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-275 |
2.23e-38 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 142.78 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVRGKDISMIFQEpmTSL 117
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKS----TLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTT 197
Cdd:cd03294 114 LPHRTVLENVAFGLEV-QGVPRAEREERAAEALELV---GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 198 ALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYTRALLSAVPKL 275
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRA 267
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-251 |
3.95e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 139.11 E-value: 3.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLttSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSL-SIMRLLdkktSRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03214 1 EVENL--SVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLL----KPSSGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdismifqepmtslnpifpigkqiaealTVHQdisssaakaevirLLEKVRIPNAKNRFDDyphQFSGGMRQRVM 178
Cdd:cd03214 72 ARKIA----------------------------YVPQ-------------ALELLGLAHLADRPFN---ELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-260 |
5.45e-38 |
|
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: 141.41 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLAlpEEEM 98
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPT----SGKVTVDGLDTLD--EENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKdISMIFQEPMTslnpifpigkQIAeALTVHQDI---------SSSAAKAEVIRLLEKVRIPNAKNRfddYPHQF 169
Cdd:TIGR04520 73 WEIRKK-VGMVFQNPDN----------QFV-GATVEDDVafglenlgvPREEMRKRVDEALKLVGMEDFRDR---EPHLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVE 249
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVA 216
|
250
....*....|.
gi 549799341 250 TGTTDDIFHRG 260
Cdd:TIGR04520 217 EGTPREIFSQV 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
336-542 |
5.60e-38 |
|
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: 138.47 E-value: 5.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTlRTMRRSVQMIFQDPfaSL 415
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL-PPLRRRIGMVFQDF--AL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPFiehrlgtkqqarekaadllekvglspdmmrrfphefSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:cd03229 88 FPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGE 542
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
313-569 |
7.43e-38 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 143.02 E-value: 7.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDIrsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP----TSGDVMLDGYE 388
Cdd:PRK15093 2 PLLDIRNLTIEFKT-------SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 389 VLKLdktTLRTMRR----SVQMIFQDPFASLDPRMSVGTAIMEPFIE--------HRLGTKQQareKAADLLEKVGLS-- 454
Cdd:PRK15093 75 LLRL---SPRERRKlvghNVSMIFQEPQSCLDPSERVGRQLMQNIPGwtykgrwwQRFGWRKR---RAIELLHRVGIKdh 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 455 PDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHR 534
Cdd:PRK15093 149 KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
250 260 270
....*....|....*....|....*....|....*
gi 549799341 535 VAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVP 569
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
313-568 |
9.14e-38 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 140.35 E-value: 9.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDIRSGLFgrksgavhaveKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKL 392
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCR-----------DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKTTL------RTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIEhrLGTKQ--QAREKAADLLEKVGLSPDMMRRFPHE 464
Cdd:TIGR02323 71 ELYQLseaerrRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMA--IGARHygNIRATAQDWLEEVEIDPTRIDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 465 FSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIV 544
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
250 260
....*....|....*....|....
gi 549799341 545 EIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:TIGR02323 229 ESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
336-557 |
1.88e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.38 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV---LKLDKTTLRTMRRSVQMIFQDpf 412
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 ASLDPRMSVgtaiMEPFIE---HRLG-TKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVA 488
Cdd:COG4161 91 YNLWPHLTV----MENLIEapcKVLGlSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 489 DEAVSALDVSIKAQVCNLLLDLQQNLNLAfLFISHDMAVVERVSHRVAVMYLGEIVEIGpRAAVFDNPQ 557
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQTGITQ-VIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQ 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-197 |
3.72e-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: 135.08 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVrgkdISMIFQEPmtSL 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKS----TLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE----IGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPN-AKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPT 196
Cdd:pfam00005 71 FPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 549799341 197 T 197
Cdd:pfam00005 150 A 150
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
18-242 |
7.28e-37 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 137.07 E-value: 7.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLdkkTSRIEGKVMLGGRDLLALPEEE 97
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLIGGL---RSVQEGSLKVLGQELHGASKKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRgKDISMIFQEpmTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQRV 177
Cdd:TIGR02982 77 LVQLR-RRIGYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVaEVSDRTIVM 242
Cdd:TIGR02982 151 AIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRIL-DVADRILQM 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-245 |
1.22e-36 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 135.01 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVtslsIMRLLDKKTSRIEGKVMLGGRDLLALpeEEM 98
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKST----LLRCIAGLEEPDSGSILIDGEDLTDL--EDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEPmtSLNPIFPIGKQIAEALtvhqdisssaakaevirllekvripnaknrfddyphqfSGGMRQRVM 178
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-265 |
1.71e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 136.97 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDK-----KTSRIEGKVMLGGRDLLA 92
Cdd:PRK14247 3 KIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKS----TLLRVFNRlielyPEARVSGEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEEEMRKvrgkDISMIFQEPmtslNPI--FPIGKQIAEALTVHQDISSSAAKAEVIR-LLEKVRI-PNAKNRFDDYPHQ 168
Cdd:PRK14247 75 MDVIELRR----RVQMVFQIP----NPIpnLSIFENVALGLKLNRLVKSKKELQERVRwALEKAQLwDEVKDRLDAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
250
....*....|....*..
gi 549799341 249 ETGTTDDIFHRGRHPYT 265
Cdd:PRK14247 225 EWGPTREVFTNPRHELT 241
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-257 |
1.73e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTtsFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtSL--SIMRLLdKKTSrieGKVMLGGRDLlal 93
Cdd:COG1121 4 MPAIELENLT--VSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKS--TLlkAILGLL-PPTS---GTVRLFGKPP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 peeemrKVRGKDISMIFQepMTSLNPIFPIgkqiaealTVHQ-------------DISSSAAKAEVIRLLEKVRIPNAKN 160
Cdd:COG1121 71 ------RRARRRIGYVPQ--RAEVDWDFPI--------TVRDvvlmgrygrrglfRRPSRADREAVDEALERVGLEDLAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 161 RfddyphQF---SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSD 237
Cdd:COG1121 135 R------PIgelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFD 207
|
250 260
....*....|....*....|
gi 549799341 238 RTIVMFRGdVVETGTTDDIF 257
Cdd:COG1121 208 RVLLLNRG-LVAHGPPEEVL 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-271 |
2.04e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.04 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 42 SFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEmRKVrgkdiSMIFQEpmtslNPIF 121
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS-TLLNLIAGFLPPDS---GRILWNGQDLTALPPAE-RPV-----SMLFQE-----NNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 122 PigkqiaeALTVHQDIS---------SSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPKLLIA 192
Cdd:COG3840 84 P-------HLTVAQNIGlglrpglklTAEQRAQVEQALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 193 DEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYTRALLSA 271
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
331-538 |
4.14e-36 |
|
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: 134.52 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEvlkLDKTTLRTMRRSVQMIFQD 410
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD---LTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 P----FASldprmSVGTAIMepF-IEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKV 485
Cdd:cd03225 84 PddqfFGP-----TVEEEVA--FgLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 549799341 486 IVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVM 538
Cdd:cd03225 156 LLLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
27-249 |
4.38e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.79 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSRIE----GKVMLGGRDLLALPEEEMRKVR 102
Cdd:COG2884 8 SKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLL----YGEErptsGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 103 gKDISMIFQEpmtslnpiF------PIGKQIAEALTVHqDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQR 176
Cdd:COG2884 79 -RRIGVVFQD--------FrllpdrTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 177 VMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
315-557 |
6.13e-36 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 134.87 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKL-- 392
Cdd:cd03219 1 LEVRGLTKRF-----------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKTTLRTMRRSvqmiFQDPfaSLDPRMSVGTAIM--------EPFIEHR-LGTKQQAREKAADLLEKVGLSpDMMRRFPH 463
Cdd:cd03219 70 HEIARLGIGRT----FQIP--RLFPELTVLENVMvaaqartgSGLLLARaRREEREARERAEELLERVGLA-DLADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELA-ELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
250
....*....|....
gi 549799341 544 VEIGPRAAVFDNPQ 557
Cdd:cd03219 222 IAEGTPDEVRNNPR 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-259 |
1.06e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 134.23 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKS----TLLRCLNGLVEPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQEPmtslnpifpigkQIAEALTVHQDIS-----------------SSAAKAEVIRLLEKVRI-PNAKN 160
Cdd:cd03256 74 RQLR-RQIGMIFQQF------------NLIERLSVLENVLsgrlgrrstwrslfglfPKEEKQRALAALERVGLlDKAYQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 161 RFDdyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTI 240
Cdd:cd03256 141 RAD----QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIV 216
|
250 260
....*....|....*....|...
gi 549799341 241 VMFRGDVVETGT----TDDIFHR 259
Cdd:cd03256 217 GLKDGRIVFDGPpaelTDEVLDE 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
336-557 |
2.08e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV---LKLDKTTLRTMRRSVQMIFQDpf 412
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 ASLDPRMSVgtaiMEPFIE---HRLG-TKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVA 488
Cdd:PRK11124 91 YNLWPHLTV----QQNLIEapcRVLGlSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 489 DEAVSALDVSIKAQVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMYLGEIVEIGPrAAVFDNPQ 557
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-266 |
2.55e-35 |
|
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: 133.13 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEm 98
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKT-TLLRLIAGFETPTS---GEILLDGKDITNLPPHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVM 178
Cdd:cd03300 72 -----RPVNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFh 258
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY- 219
|
....*...
gi 549799341 259 rgRHPYTR 266
Cdd:cd03300 220 --EEPANR 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
315-560 |
3.20e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.97 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldk 394
Cdd:COG3839 4 LELENVSKSY-----------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDpFAsLDPRMSVGTAIMEPFIEHRLgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIA 474
Cdd:COG3839 68 TDLPPKDRNIAMVFQS-YA-LYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHD----MAvverVSHRVAVMYLGEIVEIGPRA 550
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTPE 219
|
250
....*....|
gi 549799341 551 AVFDNPQHPY 560
Cdd:COG3839 220 ELYDRPANLF 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
334-576 |
3.42e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 137.47 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 334 KSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRS-VQMIFQDpF 412
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS-F 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 AsLDPRMSV--GTAIMepfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PRK10070 116 A-LMPHMTVldNTAFG---MELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVPV 570
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
|
250
....*....|..
gi 549799341 571 P------DPARR 576
Cdd:PRK10070 271 SqvfsakDIARR 282
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
336-551 |
4.68e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 4.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDpFaSL 415
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-F-RL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPFIEHRLgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:COG2884 91 LPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 496 D-----------VSIKAQvcnllldlqqnlNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAA 551
Cdd:COG2884 169 DpetsweimellEEINRR------------GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
336-559 |
4.81e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.52 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKlDKTTLRTMRRSVQMIFQDpFaSL 415
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEAGMVFQQ-F-YL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:PRK09493 89 FPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 496 DVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHP 559
Cdd:PRK09493 168 DPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
315-547 |
8.17e-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: 130.84 E-value: 8.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldk 394
Cdd:cd03301 1 VELENVTKRF-----------GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDpFAsLDPRMSVGTAIMEPfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIA 474
Cdd:cd03301 65 TDLPPKDRDIAMVFQN-YA-LYPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
317-560 |
9.40e-35 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 131.69 E-value: 9.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 317 VKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDktt 396
Cdd:cd03296 5 VRNVSKRF-----------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 397 lrTMRRSVQMIFQDpfASLDPRMSVGTAI-----MEPfiEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQ 471
Cdd:cd03296 71 --VQERNVGFVFQH--YALFRHMTVFDNVafglrVKP--RSERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 472 RIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAA 551
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*....
gi 549799341 552 VFDNPQHPY 560
Cdd:cd03296 224 VYDHPASPF 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
313-562 |
1.07e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 132.08 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIE--P---TSGDVMLDGY 387
Cdd:COG1117 10 PKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 EVL--KLDKTTLRtmrRSVQMIFQ--DPFAsldprMSvgtaIME----PFIEHRLGTKQQAREKAADLLEKVGLSP---D 456
Cdd:COG1117 79 DIYdpDVDVVELR---RRVGMVFQkpNPFP-----KS----IYDnvayGLRLHGIKSKSELDEIVEESLRKAALWDevkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 457 MMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD-----------VSIKAQVCNllldlqqnlnlafLFISHDM 525
Cdd:COG1117 147 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakieeliLELKKDYTI-------------VIVTHNM 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 549799341 526 AVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTK 562
Cdd:COG1117 214 QQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-256 |
1.29e-34 |
|
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: 131.52 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPeee 97
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKT-TLLRMLAGLLKPDS---GSILIDGEDVRKEP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mRKVRgKDISMIFQEpmtslNPIFPI--GKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQ 175
Cdd:COG4555 70 -REAR-RQIGVLPDE-----RGLYDRltVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDR---RVGELSTGMKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMsVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
.
gi 549799341 256 I 256
Cdd:COG4555 219 L 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-259 |
1.57e-34 |
|
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: 130.92 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSfrvdggWKS-VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdkktSRIEGKVMLGGRDLLALPEEE 97
Cdd:cd03299 1 LKVENLSKD------WKEfKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI----KPDSGKILLNGKDITNLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mrkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALTvHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRV 177
Cdd:cd03299 71 ------RDISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNR---KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
..
gi 549799341 258 HR 259
Cdd:cd03299 219 KK 220
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
21-270 |
2.12e-34 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 130.69 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPeeemrk 100
Cdd:TIGR00968 3 IANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKS-TLLRIIAGLEQPDS---GRIRLNGQDATRVH------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 101 VRGKDISMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIA 180
Cdd:TIGR00968 69 ARDRKIGFVFQH--YALFKHLTVRDNIAFGLEI-RKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 181 MALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFhrg 260
Cdd:TIGR00968 143 RALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVY--- 219
|
250
....*....|
gi 549799341 261 RHPYTRALLS 270
Cdd:TIGR00968 220 DHPANPFVMS 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
341-567 |
2.61e-34 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 130.98 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP----TSGDVMLDGYEVLKldkTTLRTmrRSVQMIFQDPFASLD 416
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP---CALRG--RKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 417 PRMSVGTAIMEPFiehRLGTKQQAREKAADLLEKVGLS--PDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK10418 94 PLHTMHTHARETC---LALGKPADDATLTAALEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 495 LDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSA 567
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-260 |
2.95e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRdllALPE 95
Cdd:PRK13635 3 EEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKS----TLAKLLNGLLLPEAGTITVGGM---VLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRgKDISMIFQEPmtslnpifpiGKQIAEAlTVHQDIS-----SSAAKAEVI-RLLEKVRIPNAKNRFDDYPHQF 169
Cdd:PRK13635 74 ETVWDVR-RQVGMVFQNP----------DNQFVGA-TVQDDVAfglenIGVPREEMVeRVDQALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVE 249
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
250
....*....|.
gi 549799341 250 TGTTDDIFHRG 260
Cdd:PRK13635 221 EGTPEEIFKSG 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-256 |
3.51e-34 |
|
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: 130.54 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFrvdGGWKsVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkkTSRI---EGKVMLGGRDLLA 92
Cdd:COG0411 2 DPLLEVRGLTKRF---GGLV-AVDDVSLEVERGEIVGLIGPNGAGKT----TLFNLI---TGFYrptSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEEEMRKvRGkdISMIFQEP-----MT----------------SLNPIFPIGKQIAEaltvhqdisSSAAKAEVIRLLE 151
Cdd:COG0411 71 LPPHRIAR-LG--IARTFQNPrlfpeLTvlenvlvaaharlgrgLLAALLRLPRARRE---------EREARERAEELLE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 152 KVRIpnaKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGV 231
Cdd:COG0411 139 RVGL---ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDL 215
|
250 260
....*....|....*....|....*
gi 549799341 232 VAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:COG0411 216 VMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
315-552 |
5.91e-34 |
|
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: 129.59 E-value: 5.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:COG4555 2 IEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTlrtmRRSVQMIFQDPFasLDPRMSVgTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFpHEFSGGQRQRIA 474
Cdd:COG4555 71 EA----RRQIGVLPDERG--LYDRLTV-RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLL-REILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-256 |
6.18e-34 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 129.09 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdGGWKsVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEm 98
Cdd:cd03219 1 LEVRGLTKRF---GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKT----TLFNLISGFLRPTSGSVLFDGEDITGLPPHE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdISMIFQepmtslNP-IFP---------IGKQIAEALTVHQDISS---SAAKAEVIRLLEKVRIPNaknRFDDY 165
Cdd:cd03219 72 IARLG--IGRTFQ------IPrLFPeltvlenvmVAAQARTGSGLLLARARreeREARERAEELLERVGLAD---LADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEeGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQG 219
|
250
....*....|.
gi 549799341 246 DVVETGTTDDI 256
Cdd:cd03219 220 RVIAEGTPDEV 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-245 |
6.83e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 127.13 E-value: 6.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDllalPEEEM 98
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKT-TLIKIILGLLKPDS---GEIKVLGKD----IKKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKdISMIFQEPMtslnpiFPigkqiaEALTVHQDIsssaakaevirllekvripnaknrfddyphQFSGGMRQRVM 178
Cdd:cd03230 69 EEVKRR-IGYLPEEPS------LY------ENLTVRENL------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-570 |
9.56e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 132.65 E-value: 9.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFDirsglfgrksgAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlk 391
Cdd:PRK11607 17 TPLLEIRNLTKSFD-----------GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTLRTMRRSVQMIFQDpfASLDPRMSVGTAIMEPFIEHRLgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQ 471
Cdd:PRK11607 81 VDLSHVPPYQRPINMMFQS--YALFPHMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 472 RIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAA 551
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
250
....*....|....*....
gi 549799341 552 VFDNPQHPYTKKLMSAVPV 570
Cdd:PRK11607 237 IYEHPTTRYSAEFIGSVNV 255
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-265 |
9.62e-34 |
|
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: 129.00 E-value: 9.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFrvdGGWKSVvRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPeeemrk 100
Cdd:cd03296 5 VRNVSKRF---GDFVAL-DDVSLDIPSGELVALLGPSGSGKT-TLLRLIAGLERPDS---GTILFGGEDATDVP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 101 VRGKDISMIFQEpmTSLNPIFPIGKQIAEALTV---HQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRV 177
Cdd:cd03296 71 VQERNVGFVFQH--YALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....*...
gi 549799341 258 hrgRHPYT 265
Cdd:cd03296 226 ---DHPAS 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-242 |
9.68e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.62 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWksVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTsriEGKVMLGGRDLLALPEEEM 98
Cdd:COG4619 1 LELEGL--SFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKS-TLLRALADLDPPT---SGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvrgkDISMIFQEPmtslnPIFP--IGKQIAEALTVHQDissSAAKAEVIRLLEKVRIPNAknrFDDYP-HQFSGGMRQ 175
Cdd:COG4619 73 RR----QVAYVPQEP-----ALWGgtVRDNLPFPFQLRER---KFDRERALELLERLGLPPD---ILDKPvERLSGGERQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVM 242
Cdd:COG4619 138 RLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
317-566 |
1.06e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 129.10 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 317 VKDLTTRFDIRSGLFGrksgavhavekVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSG-----DVMLDGYEVLK 391
Cdd:PRK11264 6 VKNLVKKFHGQTVLHG-----------IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTLRTMRRSVQMIFQDpfASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQ 471
Cdd:PRK11264 75 QQKGLIRQLRQHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 472 RIAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAA 551
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....*
gi 549799341 552 VFDNPQHPYTKKLMS 566
Cdd:PRK11264 231 LFADPQQPRTRQFLE 245
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
18-264 |
1.09e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 128.96 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEE 97
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKS----TLLRCINRLVEPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKdISMIFQEpmtsLNPIfpigkqiaEALTVHQDI-----------------SSSAAKAEVIRLLEKVRIPN-AK 159
Cdd:TIGR02315 74 LRKLRRR-IGMIFQH----YNLI--------ERLTVLENVlhgrlgykptwrsllgrFSEEDKERALSALERVGLADkAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 160 NRFDdyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRT 239
Cdd:TIGR02315 141 QRAD----QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI 216
|
250 260
....*....|....*....|....*.
gi 549799341 240 IVMFRGDVVETGTTDDIF-HRGRHPY 264
Cdd:TIGR02315 217 VGLKAGEIVFDGAPSELDdEVLRHIY 242
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
16-266 |
3.45e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 130.54 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPE 95
Cdd:TIGR03265 2 SPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKT-TLLRIIAGLERQTA---GTIYQGGRDITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEmrkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALTvHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQ 175
Cdd:TIGR03265 74 QK------RDYGIVFQS--YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:TIGR03265 142 RVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
250
....*....|.
gi 549799341 256 IFhrgRHPYTR 266
Cdd:TIGR03265 222 IY---RHPATP 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
333-566 |
4.59e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.39 E-value: 4.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVHAVEK-VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV---------LKL-DKTTLRTMR 401
Cdd:PRK10619 12 HKRYGEHEVLKgVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKVaDKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 402 RSVQMIFQDpfASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLML 481
Cdd:PRK10619 92 TRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 482 DPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYT 561
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
....*
gi 549799341 562 KKLMS 566
Cdd:PRK10619 249 QQFLK 253
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
315-547 |
4.77e-33 |
|
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: 126.08 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLkldk 394
Cdd:cd03263 1 LQIRNLTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQdpFASLDPRMSVgtaimepfIEH-----RL--GTKQQAREKAADLLEKVGLSPDMMRRfPHEFSG 467
Cdd:cd03263 68 TDRKAARQSLGYCPQ--FDALFDELTV--------REHlrfyaRLkgLPKSEIKEEVELLLRVLGLTDKANKR-ARTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCnlLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW--DLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-269 |
7.05e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.43 E-value: 7.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEmRK 100
Cdd:PRK10851 5 IANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKT-TLLRIIAGLEHQTS---GHIRFHGTDVSRLHARD-RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 101 VrgkdiSMIFQE-----PMTSLNpifpigkQIAEALTV---HQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGG 172
Cdd:PRK10851 76 V-----GFVFQHyalfrHMTVFD-------NIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
250
....*....|....*..
gi 549799341 253 TDDIFhrgRHPYTRALL 269
Cdd:PRK10851 221 PDQVW---REPATRFVL 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
313-571 |
7.94e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.44 E-value: 7.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFdirsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevLKL 392
Cdd:PRK13635 4 EIIRVEHISFRY---------PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKTTLRTMRRSVQMIFQDPfaslDPRMsVGTAIMEPF---IEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQ 469
Cdd:PRK13635 72 SEETVWDVRRQVGMVFQNP----DNQF-VGATVQDDVafgLENIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGPR 549
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
250 260 270
....*....|....*....|....*....|....*
gi 549799341 550 AAVFDNPQH--------PYTKKLMSA-----VPVP 571
Cdd:PRK13635 225 EEIFKSGHMlqeigldvPFSVKLKELlkrngILLP 259
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-245 |
9.37e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 123.12 E-value: 9.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMR 99
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKS----TLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 100 KvrgkDISMIFQepmtslnpifpigkqiaealtvhqdisssaakaevirllekvripnaknrfddyphqFSGGMRQRVMI 179
Cdd:cd00267 73 R----RIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 180 AMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-251 |
1.77e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.57 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSL-SIMRLLdKKTSrieGKVMLGGRdllalPEEEM 98
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLL-KPTS---GSIRVFGK-----PLEKE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvrgkDISMIFQEpmTSLNPIFPI-GKQIAE----ALTVHQDISSSAAKAEVIRLLEKVRIPNAKNR-FDdyphQFSGG 172
Cdd:cd03235 67 RK----RIGYVPQR--RSIDRDFPIsVRDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRqIG----ELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRtIVMFRGDVVETG 251
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-270 |
2.75e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 131.43 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLS-IMRLLDKKtsriEGKVMLGGRDLLALP 94
Cdd:COG4987 331 GPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKS-TLLAlLLRFLDPQ----SGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVrgkdISMIFQEPmtslnPIFpiGKQIAEALTVHQDissSAAKAEVIRLLEKVRIpnaKNRFDDYPH------- 167
Cdd:COG4987 404 EDDLRRR----IAVVPQRP-----HLF--DTTLRENLRLARP---DATDEELWAALERVGL---GDWLAALPDgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 ----QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMgVVAEVSDRTIVMF 243
Cdd:COG4987 467 eggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRL-AGLERMDRILVLE 543
|
250 260
....*....|....*....|....*..
gi 549799341 244 RGDVVETGTTDDIFHrgRHPYTRALLS 270
Cdd:COG4987 544 DGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-264 |
3.68e-32 |
|
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: 132.27 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSRI----EGKVMLGGRDLLALP 94
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLL----LGLyeptSGRILIDGIDLRQID 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKvrgkDISMIFQEPMtslnpIFPiGKqIAEALTVHQDissSAAKAEVIRLLEKVRIpnaknrfDDY----PH--- 167
Cdd:COG2274 544 PASLRR----QIGVVLQDVF-----LFS-GT-IRENITLGDP---DATDEEIIEAARLAGL-------HDFiealPMgyd 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 --------QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLqeEEGMSVLFITHDMGVVAEVsDRT 239
Cdd:COG2274 603 tvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLA-DRI 679
|
250 260
....*....|....*....|....*
gi 549799341 240 IVMFRGDVVETGTTDDIFHRGRHPY 264
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
40-254 |
5.68e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 5.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGR--DLLALP-EEEMRKVRgKDISMIFQEpmTS 116
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPRS---GTLNIAGNhfDFSKTPsDKAIRELR-RNVGMVFQQ--YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 LNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQRVMIAMALASKPKLLIADEPT 196
Cdd:PRK11124 93 LWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRF---PLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 197 TALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTD 254
Cdd:PRK11124 170 AALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
341-557 |
7.12e-32 |
|
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: 123.60 E-value: 7.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlkLDKTTLRTMRRSVQMIFQDpfASLDPRMS 420
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG-----KDITNLPPEKRDISYVPQN--YALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTAImEPFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIK 500
Cdd:cd03299 88 VYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 501 AQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-256 |
8.28e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.28 E-value: 8.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 22 QNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAlPEEEMRKV 101
Cdd:PRK09493 5 KNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEEITS---GDLIVDGLKVND-PKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 102 RgKDISMIFQE----P-MTSL-NPIF-PIgkQIAEAltvhqdiSSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMR 174
Cdd:PRK09493 76 R-QEAGMVFQQfylfPhLTALeNVMFgPL--RVRGA-------SKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 175 QRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTD 254
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
..
gi 549799341 255 DI 256
Cdd:PRK09493 222 VL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-270 |
1.14e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.32 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFRvdggWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTS-RIE-GKVMLGGRDLLALPEEEM 98
Cdd:PRK11264 6 VKNLVKKFH----GQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAgTIRvGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQepmtSLNpIFP---IGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKnrfDDYPHQFSGGMRQ 175
Cdd:PRK11264 81 RQLR-QHVGFVFQ----NFN-LFPhrtVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLfITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....*
gi 549799341 256 IFHRGRHPYTRALLS 270
Cdd:PRK11264 231 LFADPQQPRTRQFLE 245
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-240 |
1.29e-31 |
|
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: 121.95 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEMRK 100
Cdd:TIGR03608 1 LKNISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFDS---GQVYLNGQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 101 VRGKDISMIFQ-----EPMTslnpifpIGKQIAEALtVHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQ 175
Cdd:TIGR03608 73 FRREKLGYLFQnfaliENET-------VEENLDLGL-KYKKLSKKEKREKKKEALEKVGLNLKLKQ---KIYELSGGEQQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMgVVAEVSDRTI 240
Cdd:TIGR03608 142 RVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDP-EVAKQADRVI 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-566 |
1.47e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.10 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIE-----PTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQD 410
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR---RRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 PfaSLDPRMSVGTAI-MEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRF---PHEFSGGQRQRIAIARSLMLDPKVI 486
Cdd:PRK14247 91 P--NPIPNLSIFENVaLGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 487 VADEAVSALDVSIKAQVcnllldlqqnlNLAFLFISHDMAVV---------ERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:PRK14247 169 LADEPTANLDPENTAKI-----------ESLFLELKKDMTIVlvthfpqqaARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
....*....
gi 549799341 558 HPYTKKLMS 566
Cdd:PRK14247 238 HELTEKYVT 246
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-272 |
2.01e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 122.64 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 25 TTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLD-KKTSRIEGKVMLGGRDLLAlPEEEMRKVRg 103
Cdd:PRK14267 7 TVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElNEEARVEGEVRLFGRNIYS-PDVDPIEVR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 104 KDISMIFQEPmtslNPiFP---IGKQIAEALTVHQDISSSAAKAEVIR-LLEKVRI-PNAKNRFDDYPHQFSGGMRQRVM 178
Cdd:PRK14267 85 REVGMVFQYP----NP-FPhltIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFH 258
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....
gi 549799341 259 RGRHPYTRALLSAV 272
Cdd:PRK14267 238 NPEHELTEKYVTGA 251
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
331-552 |
4.21e-31 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 128.80 E-value: 4.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQD 410
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR---RQIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 P--FAsldprmsvGTaIMEPFiehRLGTKQQAREKAADLLEKVGLSPDMMRRfPH-----------EFSGGQRQRIAIAR 477
Cdd:COG2274 558 VflFS--------GT-IRENI---TLGDPDATDEEIIEAARLAGLHDFIEAL-PMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 478 SLMLDPKVIVADEAVSALDVSIKAQVCnlLLDLQQNLNLAFLFISHDMAVVERVsHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIIL--ENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEEL 696
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
314-568 |
4.42e-31 |
|
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: 121.69 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTtrfdirsglFGRKSGAVhaVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLd 393
Cdd:COG1120 1 MLEAENLS---------VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 ktTLRTMRRSVQMIFQDPFASLDprMSVGTAIM---EPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFpHEFSGGQR 470
Cdd:COG1120 69 --SRRELARRIAYVPQEPPAPFG--LTVRELVAlgrYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPV-DELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRA 550
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
250
....*....|....*...
gi 549799341 551 AVFdnpqhpyTKKLMSAV 568
Cdd:COG1120 224 EVL-------TPELLEEV 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-245 |
4.47e-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: 119.02 E-value: 4.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPEEEM 98
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT----SGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVrgkdISMIFQEPMtslnpIFpigkqiaeALTVHQDIsssaakaevirllekvripnaknrfddyphqFSGGMRQRVM 178
Cdd:cd03228 75 RKN----IAYVPQDPF-----LF--------SGTIRENI-------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVAEVsDRTIVMFRG 245
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
37-267 |
5.16e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 121.27 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGR--DLLALP-EEEMRKVRGKdISMIFQEp 113
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPDS---GQLNIAGHqfDFSQKPsEKAIRLLRQK-VGMVFQQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 114 mTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQRVMIAMALASKPKLLIAD 193
Cdd:COG4161 91 -YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF---PLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 194 EPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTdDIFhrgRHPYTRA 267
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHF---TQPQTEA 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
19-259 |
8.57e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 8.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEm 98
Cdd:COG3839 4 LELENVSKSY---GG-VEALKDIDLDIEDGEFLVLLGPSGCGKS-TLLRMIAGLEDPTS---GEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rkvRgkDISMIFQEPMtslnpIFPigkqiaeALTVHQDISSS-----AAKAE----VIRLLEKVRIPNAKNRfddYPHQF 169
Cdd:COG3839 75 ---R--NIAMVFQSYA-----LYP-------HMTVYENIAFPlklrkVPKAEidrrVREAAELLGLEDLLDR---KPKQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHD------MGvvaevsDRTIVMF 243
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMN 208
|
250
....*....|....*.
gi 549799341 244 RGDVVETGTTDDIFHR 259
Cdd:COG3839 209 DGRIQQVGTPEELYDR 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-254 |
1.18e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 119.53 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLalpeEEM 98
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLTGELRPTS---GTAYINGYSIR----TDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQEpmtslNPIFPigkqiaeALTVHQ---------DISSSAAKAEVIRLLEKVRIPNAKNRFddyPHQF 169
Cdd:cd03263 71 KAAR-QSLGYCPQF-----DALFD-------ELTVREhlrfyarlkGLPKSEIKEEVELLLRVLGLTDKANKR---ARTL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:cd03263 135 SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
....*
gi 549799341 250 TGTTD 254
Cdd:cd03263 213 IGSPQ 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-256 |
1.47e-30 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 119.40 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLalpeEEMRK 100
Cdd:cd03265 3 VENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKT-TTIKMLTTLLKPTS---GRATVAGHDVV----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 101 VRgKDISMIFQEPmtSLNPIFpigkQIAEALTVH---QDISSSAAKAEVIRLLEKVRIPNAKNRFDDYphqFSGGMRQRV 177
Cdd:cd03265 71 VR-RRIGIVFQDL--SVDDEL----TGWENLYIHarlYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-256 |
1.51e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 119.08 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPEEEM 98
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR----SGSIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvRGkdISMIFQEPMtslnpIFPigkqiaeALTVHQDISSSA---AKAEVIRLLEKV--RIPNAKNRFDDYPHQFSGGM 173
Cdd:cd03224 73 AR-AG--IGYVPEGRR-----IFP-------ELTVEENLLLGAyarRRAKRKARLERVyeLFPRLKERRKQLAGTLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTT 253
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
...
gi 549799341 254 DDI 256
Cdd:cd03224 217 AEL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
356-570 |
5.75e-30 |
|
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: 120.68 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 356 LVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQDpfASLDPRMSVGTAIMEPFIEHRLG 435
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQS--YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 436 tKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLN 515
Cdd:TIGR01187 74 -RAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 516 LAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAVPV 570
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
331-538 |
6.01e-30 |
|
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: 115.94 E-value: 6.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLrtmRRSVQMIFQD 410
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 PFasldpRMSvGTaIMEpfiehrlgtkqqarekaaDLLekvglspdmmrrfphefSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:cd03228 85 PF-----LFS-GT-IRE------------------NIL-----------------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 549799341 491 AVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVsHRVAVM 538
Cdd:cd03228 123 ATSALDPETEALI--LEALRALAKGKTVIVIAHRLSTIRDA-DRIIVL 167
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-257 |
6.41e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLT------TSFRvdggwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGRDLlALP 94
Cdd:PRK13637 5 IENLThiymegTPFE-----KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL-KPTS---GKIIIDGVDI-TDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVRgKDISMIFQEPMTSLnpiF--PIGKQIAEALTvHQDISSSAAKAEVIRLLEKVRIPnaknrFDDY----PHQ 168
Cdd:PRK13637 75 KVKLSDIR-KKVGLVFQYPEYQL---FeeTIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLD-----YEDYkdksPFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
....*....
gi 549799341 249 ETGTTDDIF 257
Cdd:PRK13637 225 LQGTPREVF 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-266 |
7.52e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.48 E-value: 7.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 10 QTGGSVSPVLSVQNLTTSFrvDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRD 89
Cdd:PRK11607 11 KTRKALTPLLEIRNLTKSF--DG--QHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LLALPEEEmrkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALTvhQD-ISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQ 168
Cdd:PRK11607 83 LSHVPPYQ------RPINMMFQS--YALFPHMTVEQNIAFGLK--QDkLPKAEIASRVNEMLGLVHMQEFAKR---KPHQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTI----QGQILDLIktlqEEEGMSVLFITHDMGVVAEVSDRTIVMFR 244
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
250 260
....*....|....*....|..
gi 549799341 245 GDVVETGTTDDIFhrgRHPYTR 266
Cdd:PRK11607 226 GKFVQIGEPEEIY---EHPTTR 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-272 |
7.75e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.68 E-value: 7.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVRGKDISMIFQEpmTSL 117
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPIGKQIAEALtvhqDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTT 197
Cdd:PRK10070 118 MPHMTVLDNTAFGM----ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 198 ALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYTRALLSAV 272
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
312-552 |
8.24e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.20 E-value: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:COG1129 2 EPLLEMRGISKSF-----------GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 ldKTTLRTMRRSVQMIFQDPfaSLDPRMSVGTAIM---EP----FIEHRlgtkqQAREKAADLLEKVGL--SPDMMRRfp 462
Cdd:COG1129 71 --RSPRDAQAAGIAIIHQEL--NLVPNLSVAENIFlgrEPrrggLIDWR-----AMRRRARELLARLGLdiDPDTPVG-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 463 hEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS-----------IKAQvcnllldlqqnlNLAFLFISHDMAVVERV 531
Cdd:COG1129 140 -DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReverlfriirrLKAQ------------GVAIIYISHRLDEVFEI 206
|
250 260
....*....|....*....|.
gi 549799341 532 SHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG1129 207 ADRVTVLRDGRLVGTGPVAEL 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
341-503 |
9.02e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP---TSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQDPFasLDP 417
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-----TALPAEQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 418 RMSVGTAImePF-IEHRLGtKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:COG4136 90 HLSVGENL--AFaLPPTIG-RAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
....*..
gi 549799341 497 VSIKAQV 503
Cdd:COG4136 166 AALRAQF 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-251 |
1.06e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 116.59 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTsLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEm 98
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTT-LRMIAGLEEPTS---GRIYIGGRDVTDLPPKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALTVHqDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVM 178
Cdd:cd03301 72 -----RDIAMVFQN--YALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQIEHLLDR---KPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
315-543 |
1.10e-29 |
|
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: 115.19 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldK 394
Cdd:cd03230 1 IEVRNLSKRY-----------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----K 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDPfaSLDPRMSVgtaimepfiehrlgtkqqarekaADLLekvglspdmmrrfphEFSGGQRQRIA 474
Cdd:cd03230 66 KEPEEVKRRIGYLPEEP--SLYENLTV-----------------------RENL---------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREF-WELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-270 |
1.64e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.82 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRL---LDKKTsriEGKVMLGGRDLLAlpe 95
Cdd:PRK11432 7 VVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLvagLEKPT---EGQIFIDGEDVTH--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 eemRKVRGKDISMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRFDDyphQFSGGMRQ 175
Cdd:PRK11432 73 ---RSIQQRDICMVFQS--YALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLAGFEDRYVD---QISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
250
....*....|....*
gi 549799341 256 IFhrgRHPYTRALLS 270
Cdd:PRK11432 224 LY---RQPASRFMAS 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
333-547 |
1.92e-29 |
|
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: 115.93 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldktTLRTMRRSVQMIFQDPf 412
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 aSLDPRMSvGTAIMEpfIEHRL-GTK-QQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:cd03265 83 -SVDDELT-GWENLY--IHARLyGVPgAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-265 |
1.93e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.89 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 14 SVSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTS-RIEGKVMLGGRDLLA 92
Cdd:PRK14271 17 AAAPAMAAVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyRYSGDVLLGGRSIFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPEE-EMRKvrgkDISMIFQEPmtslNPiFP--IGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNA-KNRFDDYPHQ 168
Cdd:PRK14271 93 YRDVlEFRR----RVGMLFQRP----NP-FPmsIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRLSDSPFR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
250
....*....|....*..
gi 549799341 249 ETGTTDDIFHRGRHPYT 265
Cdd:PRK14271 242 EEGPTEQLFSSPKHAET 258
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-265 |
3.30e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.41 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLD-KKTSRIEGKVMLGGRDLLAlP 94
Cdd:PRK14239 3 EPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlNPEVTITGSIVYNGHNIYS-P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVRgKDISMIFQEPmtslNPiFPIgkQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNA-----KNRFDDYPHQF 169
Cdd:PRK14239 78 RTDTVDLR-KEIGMVFQQP----NP-FPM--SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASiwdevKDRLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMsvLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIE 227
|
250
....*....|....*.
gi 549799341 250 TGTTDDIFHRGRHPYT 265
Cdd:PRK14239 228 YNDTKQMFMNPKHKET 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-542 |
4.38e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.11 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 334 KSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDkttLRTMRRSVQMIFQdpfa 413
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 414 sldprmsvgtaimepfiehrlgtkqqarekaadllekvglspdmmrrfpheFSGGQRQRIAIARSLMLDPKVIVADEAVS 493
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 549799341 494 ALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGE 542
Cdd:cd00267 110 GLDPASRERL-LELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-257 |
5.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGrdlLALPE 95
Cdd:PRK13632 5 SVMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL-KPQS---GEIKIDG---ITISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKdISMIFQEPMTSLnpifpIGkqiaeaLTVHQDI---------SSSAAKAEVIRLLEKVRIpnaKNRFDDYP 166
Cdd:PRK13632 76 ENLKEIRKK-IGIIFQNPDNQF-----IG------ATVEDDIafglenkkvPPKKMKDIIDDLAKKVGM---EDYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 167 HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGvvaEV--SDRTIVMFR 244
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD---EAilADKVIVFSE 217
|
250
....*....|...
gi 549799341 245 GDVVETGTTDDIF 257
Cdd:PRK13632 218 GKLIAQGKPKEIL 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-260 |
5.48e-29 |
|
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: 121.40 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 2 LLAATSMEQTGGSVS------PVLSVQNLttSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLS-IMRLLDK 74
Cdd:COG4988 314 LLDAPEPAAPAGTAPlpaagpPSIELEDV--SFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKS-TLLNlLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 75 KtsriEGKVMLGGRDLLALPEEEMRKvrgkDISMIFQEPMtslnpIFPIgkQIAEALTVHQdisSSAAKAEVIRLLEKVR 154
Cdd:COG4988 390 Y----SGSILINGVDLSDLDPASWRR----QIAWVPQNPY-----LFAG--TIRENLRLGR---PDASDEELEAALEAAG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 155 IpnakNRF-DDYPHQF-----------SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSV 222
Cdd:COG4988 452 L----DEFvAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTV 525
|
250 260 270
....*....|....*....|....*....|....*...
gi 549799341 223 LFITHDMGVVAEvSDRTIVMFRGDVVETGTTDDIFHRG 260
Cdd:COG4988 526 ILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-272 |
8.17e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLttSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEE 96
Cdd:PRK13548 1 AMLEARNL--SVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRGkdisMIFQEpmTSLNPIFPIGKQIAEALTVHQdISSSAAKAEVIRLLEKVRIPNAKNRfdDYPhQFSGGMRQR 176
Cdd:PRK13548 73 ELARRRA----VLPQH--SSLSFPFTVEEVVAMGRAPHG-LSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 177 VMIAMALA------SKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVET 250
Cdd:PRK13548 143 VQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
250 260
....*....|....*....|..
gi 549799341 251 GTTDDIFhrgrhpyTRALLSAV 272
Cdd:PRK13548 223 GTPAEVL-------TPETLRRV 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
345-559 |
1.06e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 345 SFDL--AEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQDP--FASLDPRMS 420
Cdd:COG3840 17 RFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-----TALPPAERPVSMLFQENnlFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTAImepfieH---RLGTKQQARekAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:COG3840 92 IGLGL------RpglKLTAEQRAQ--VEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 498 SIKA-------QVCNLLLDLQqnlnlafLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHP 559
Cdd:COG3840 163 ALRQemldlvdELCRERGLTV-------LMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
38-256 |
2.05e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 117.51 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSR-IE---GKVMLGGRDLLALPEEEMRKVRGKDISMIFQE- 112
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKS----TLVRCL----NRlIEptaGEVLIDGEDITKLSKKELRELRRKKMSMVFQHf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 113 ---P-MTSL-NPIFPigkqiaeaLTVhQDISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQRVMIAMALASKP 187
Cdd:COG4175 115 allPhRTVLeNVAFG--------LEI-QGVPKAERRERAREALELV---GLAGWEDSYPDELSGGMQQRVGLARALATDP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 188 KLLIADEPTTALDVTI----QGQILDliktLQEEEGMSVLFITHD------MGvvaevsDRTIVMFRGDVVETGTTDDI 256
Cdd:COG4175 183 DILLMDEAFSALDPLIrremQDELLE----LQAKLKKTIVFITHDldealrLG------DRIAIMKDGRIVQIGTPEEI 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-568 |
2.34e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.17 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIE-----PTSGDVMLDGYEVLKLDKTTLRtMRRSVQMIFQ- 409
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 410 -DPFASLDPRMSVGTAIMepfIEHRLGTKQQAREKAADLLEKVGL---SPDMMRRFPHEFSGGQRQRIAIARSLMLDPKV 485
Cdd:PRK14267 94 pNPFPHLTIYDNVAIGVK---LNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 486 IVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLM 565
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKI--EELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
...
gi 549799341 566 SAV 568
Cdd:PRK14267 249 TGA 251
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
38-266 |
2.97e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 115.18 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPeeemRKVRgKDISMIFQEPmtSL 117
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKT-TTIRMLTTLLRPTS---GTARVAGYDVVREP----RKVR-RSIGIVPQYA--SV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPiGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPKLLIADEPTT 197
Cdd:TIGR01188 78 DEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADR---PVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 198 ALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHR--GRHPYTR 266
Cdd:TIGR01188 154 GLDPRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRlgKDTLESR 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
340-557 |
4.14e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQDP---F--AS 414
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQNPdnqFigAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 415 LDPRMSVGtaimepfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK13632 101 VEDDIAFG-------LENKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 495 LDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
40-259 |
4.25e-28 |
|
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: 115.97 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvtslSIMRL---LDKKTsriEGKVMLGGRDLL------ALPEEEMRkvrgkdISMIF 110
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKT----TLLRAiagLERPD---SGRIRLGGEVLQdsargiFLPPHRRR------IGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 111 QEPmtSLnpiFPigkqiaeALTVHQDI----------SSSAAKAEVIRLLEkvrIPNAKNRfddYPHQFSGGMRQRVMIA 180
Cdd:COG4148 84 QEA--RL---FP-------HLSVRGNLlygrkrapraERRISFDEVVELLG---IGHLLDR---RPATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 181 MALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHR 259
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
27-357 |
4.27e-28 |
|
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: 115.86 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdkKTSRIEGKVMLGGRDLLALPEEEmrkvrgKDI 106
Cdd:TIGR03258 10 HLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFV--KAAGLTGRIAIADRDLTHAPPHK------RGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 107 SMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASK 186
Cdd:TIGR03258 82 ALLFQN--YALFPHLKVEDNVAFGLRA-QKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 187 PKLLIADEPTTALDVTIQGQILDLIKTLQEE-EGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYT 265
Cdd:TIGR03258 156 PDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 266 RALLSAVPKLGSMKERLLPARfPIIDIKTGE------SQPVADVKDTVSGGRTPILSVKDlttrfdiRSGLFGRKSGAVH 339
Cdd:TIGR03258 236 AEFLGAANILPAIALGITEAP-GLVDVSCGGavifafGDGRHDGRDKLACIRPEHLALTP-------RPAGEGRFHATIA 307
|
330 340
....*....|....*....|....
gi 549799341 340 AVE------KVSFDLAEGETLSLV 357
Cdd:TIGR03258 308 SVEwhgaalHLLCDLDAACDEPML 331
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
343-547 |
4.83e-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: 112.00 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 343 KVSFDLaEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyeVLKLD---KTTLRTMRRSVQMIFQDpfASLDPRM 419
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDsrkKINLPPQQRKIGLVFQQ--YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTAIMEPFIEHRLGTKQQareKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSI 499
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRI---SVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 549799341 500 KAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
340-550 |
6.10e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.72 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVL-KLDKTTLRTMRRSVQMIFQDPFASLdpr 418
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRPVRKRIGMVFQFPESQL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 msvgtaiMEPFIEHRL--GTK------QQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PRK13646 99 -------FEDTVEREIifGPKnfkmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG-PRA 550
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTsPKE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-242 |
6.28e-28 |
|
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: 112.14 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFR---VDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLL------DkktsriEGKVML- 85
Cdd:COG4778 2 TTLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIygnylpD------SGSILVr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 86 ---GGRDLLALPEEEMRKVRGKDISMIFQ----EPMTSLNPIfpigkqIAEALtVHQDISSSAAKAEVIRLLEKVRIPna 158
Cdd:COG4778 72 hdgGWVDLAQASPREILALRRRTIGYVSQflrvIPRVSALDV------VAEPL-LERGVDREEARARARELLARLNLP-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 159 KNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDR 238
Cdd:COG4778 143 ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADR 221
|
....
gi 549799341 239 TIVM 242
Cdd:COG4778 222 VVDV 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-265 |
6.71e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.83 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRI--EGKVMLGGRDLLALPEEEMRKvrgkDISMIFQE 112
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkvDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 113 PmtslNPiFP---IGKQIAEALTVHQDISSSAAKAEVIRLLEKVRI-PNAKNRFDDYPHQFSGGMRQRVMIAMALASKPK 188
Cdd:PRK14246 99 P----NP-FPhlsIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPYT 265
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
336-543 |
7.41e-28 |
|
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: 111.35 E-value: 7.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDpfASL 415
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPF--IEHrlgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVS 493
Cdd:cd03292 90 LPDRNVYENVAFALevTGV---PPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 549799341 494 ALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:cd03292 166 NLDPDTTWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-543 |
8.80e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 117.34 E-value: 8.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFrvdGGWKSVvRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSRI------EGKVMLGGRD 89
Cdd:PRK13549 3 EYLLEMKNITKTF---GGVKAL-DNVSLKVRAGEIVSLCGENGAGKS----TLMKVL----SGVyphgtyEGEIIFEGEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LLAlpeEEMRKVRGKDISMIFQE-----PMTSLNPIFpIGKQIAEALTVHQDisssAAKAEVIRLLEKVRI---PNAKNR 161
Cdd:PRK13549 71 LQA---SNIRDTERAGIAIIHQElalvkELSVLENIF-LGNEITPGGIMDYD----AMYLRAQKLLAQLKLdinPATPVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 162 fddyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEeGMSVLFITHDMGVVAEVSDrTIV 241
Cdd:PRK13549 143 ------NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISD-TIC 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 242 MFRGdvvetgttddifhrGRHPYTR--ALLSAVPKLGSMKERLLPARFPiidiktGESQPVADVkdtvsggrtpILSVKD 319
Cdd:PRK13549 215 VIRD--------------GRHIGTRpaAGMTEDDIITMMVGRELTALYP------REPHTIGEV----------ILEVRN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 320 LTTRFDIRSGlfgRKSgavhaVEKVSFDLAEGETLSLVGESGCGKSTT---------GRSitrlieptSGDVMLDGYEVl 390
Cdd:PRK13549 265 LTAWDPVNPH---IKR-----VDDVSFSLRRGEILGIAGLVGAGRTELvqclfgaypGRW--------EGEIFIDGKPV- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLdKTTLRTMRRSVQMIFQDPFA-SLDPRMSVGTAIMEPFI-----------EHRLGTKQQA----REKAADLLEKVGls 454
Cdd:PRK13549 328 KI-RNPQQAIAQGIAMVPEDRKRdGIVPVMGVGKNITLAALdrftggsriddAAELKTILESiqrlKVKTASPELAIA-- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 455 pdmmrrfphEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHR 534
Cdd:PRK13549 405 ---------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEI-YKLINQLVQQGVAIIVISSELPEVLGLSDR 474
|
....*....
gi 549799341 535 VAVMYLGEI 543
Cdd:PRK13549 475 VLVMHEGKL 483
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
267-550 |
9.08e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 117.94 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 267 ALLSAVPKLGSMK---ERLlparFPIIDiktgESQPVADVKDTVSGGRTPILSVKDLTtrfdirsglFGRKSGAVHAVEK 343
Cdd:COG4987 291 PLPAAAQHLGRVRaaaRRL----NELLD----APPAVTEPAEPAPAPGGPSLELEDVS---------FRYPGAGRPVLDG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDP--FASldprmSV 421
Cdd:COG4987 354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR---RRIAVVPQRPhlFDT-----TL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 GTAImepfiehRLGTKQQAREKAADLLEKVGLSpDMMRRFPH-----------EFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:COG4987 426 RENL-------RLARPDATDEELWAALERVGLG-DWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDE 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 491 AVSALDVSIKAQVCnlLLDLQQNLNLAFLFISHDMAVVERVsHRVAVMYLGEIVEIGPRA 550
Cdd:COG4987 498 PTEGLDAATEQALL--ADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHE 554
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
311-551 |
9.91e-28 |
|
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: 111.76 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 311 RTPILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVL 390
Cdd:COG4181 5 SAPIIELRGLTKTV-------GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLD---KTTLRtmRRSVQMIFQDpFaSLDPRMsvgTA---IMEPfIEhrLGTKQQAREKAADLLEKVGLSpDMMRRFPHE 464
Cdd:COG4181 78 ALDedaRARLR--ARHVGFVFQS-F-QLLPTL---TAlenVMLP-LE--LAGRRDARARARALLERVGLG-HRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 465 FSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIV 544
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*..
gi 549799341 545 EIGPRAA 551
Cdd:COG4181 226 EDTAATA 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
340-548 |
1.42e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.57 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDP--FAsldp 417
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR---RQIGVVPQDTflFS---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 418 rMSVGTAImepfiehRLGTKQQAREKAADLLEKVGLSpDMMRRFPH-----------EFSGGQRQRIAIARSLMLDPKVI 486
Cdd:COG1132 428 -GTIRENI-------RYGRPDATDEEVEEAAKAAQAH-EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 487 VADEAVSALDVSIKAQVcnllldlqqnlNLAF---------LFISHDMAVVERVsHRVAVMYLGEIVEIGP 548
Cdd:COG1132 499 ILDEATSALDTETEALI-----------QEALerlmkgrttIVIAHRLSTIRNA-DRILVLDDGRIVEQGT 557
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
39-245 |
1.54e-27 |
|
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: 110.42 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 39 RNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVRGKdISMIFQEpmTSLN 118
Cdd:TIGR02673 19 HDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR-IGVVFQD--FRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 119 PIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNaknRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTA 198
Cdd:TIGR02673 92 PDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 549799341 199 LDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:TIGR02673 168 LDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
53-266 |
1.59e-27 |
|
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: 113.36 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 53 IVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEmrkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALT 132
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 133 VhQDISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIK 212
Cdd:TIGR01187 69 M-RKVPRAEIKPRVLEALRLV---QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 549799341 213 TLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFhrgRHPYTR 266
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIY---EEPANL 195
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-256 |
1.60e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 112.88 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 22 QNLTTSFrvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLS-IMRLLDKkTSrieGKVMLGGRDLLALPEEEMRk 100
Cdd:COG1125 5 ENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRmINRLIEP-TS---GRILIDGEDIRDLDPVELR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 101 vRGkdismifqepmtslnpifpIGKQIAEA-----LTVHQDI---------SSSAAKAEVIRLLEKVRIPNAKNRfDDYP 166
Cdd:COG1125 76 -RR-------------------IGYVIQQIglfphMTVAENIatvprllgwDKERIRARVDELLELVGLDPEEYR-DRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 167 HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGD 246
Cdd:COG1125 135 HELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGR 214
|
250
....*....|
gi 549799341 247 VVETGTTDDI 256
Cdd:COG1125 215 IVQYDTPEEI 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
311-556 |
2.00e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.27 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 311 RTPILSVKDLTTRFDIRSglfgrksgavhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVl 390
Cdd:PRK09452 11 LSPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 kldkTTLRTMRRSVQMIFQDpFAsLDPRMSVgtaimepFIEHRLGTKQQAREKA------ADLLEKVGLSpDMMRRFPHE 464
Cdd:PRK09452 79 ----THVPAENRHVNTVFQS-YA-LFPHMTV-------FENVAFGLRMQKTPAAeitprvMEALRMVQLE-EFAQRKPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 465 FSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIV 544
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
250
....*....|..
gi 549799341 545 EIGPRAAVFDNP 556
Cdd:PRK09452 225 QDGTPREIYEEP 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-272 |
3.26e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.98 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:COG4559 2 LEAENL--SVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdisMIFQEpmTSLNPIFPIGKQIAEALTVHQdiSSSAAKAEVIRL-LEKVRIPNAKNRfdDYPhQFSGGMRQRV 177
Cdd:COG4559 74 ARRRA----VLPQH--SSLAFPFTVEEVVALGRAPHG--SSAAQDRQIVREaLALVGLAHLAGR--SYQ-TLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALA-------SKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVET 250
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
250 260
....*....|....*....|..
gi 549799341 251 GTTDDIFhrgrhpyTRALLSAV 272
Cdd:COG4559 222 GTPEEVL-------TDELLERV 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-238 |
4.38e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.48 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEE 97
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGSS---GEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKDISMIFQEPM--TSLNPIFPIgkQIAEALtvhQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQ 175
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMliPTLNALENV--ELPALL---RGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDR 238
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRR 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
33-274 |
4.39e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.44 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 33 GWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTsriEGKVMLGGRD----------LLALPEEEMRKVR 102
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS---EGSIVVNGQTinlvrdkdgqLKVADKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 103 GKdISMIFQE-----PMTSLnpifpigKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNrfDDYPHQFSGGMRQRV 177
Cdd:PRK10619 92 TR-LTMVFQHfnlwsHMTVL-------ENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
250
....*....|....*..
gi 549799341 258 HRGRHPYTRALLSAVPK 274
Cdd:PRK10619 241 GNPQSPRLQQFLKGSLK 257
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-535 |
4.45e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.16 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGR--------DLLA 92
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKILAGELEPDSGEVSIPKGlrigylpqEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 LPE----EEMRKVRG--KDISMIFQEPMTSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKnrFDDYP 166
Cdd:COG0488 73 DDDltvlDTVLDGDAelRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEED--LDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 167 HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDvtIQGqILDLIKTLQEEEGmSVLFITHD-------MGVVAEVSDRT 239
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKNYPG-TVLVVSHDryfldrvATRILELDRGK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 240 IVMFRGDvvetgttddifhrgrhpYT------------------------RALLSAVPKLG----------SMKERLlpA 285
Cdd:COG0488 227 LTLYPGN-----------------YSayleqraerleqeaaayakqqkkiAKEEEFIRRFRakarkakqaqSRIKAL--E 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 286 RFPIIDIKTGESQPVADVKDTVSGGRtPILSVKDLTTRFDirsglfGRKsgavhAVEKVSFDLAEGETLSLVGESGCGKS 365
Cdd:COG0488 288 KLEREEPPRRDKTVEIRFPPPERLGK-KVLELEGLSKSYG------DKT-----LLDDLSLRIDRGDRIGLIGPNGAGKS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 366 TTGRSITRLIEPTSGDVmldgyevlKLDKTtlrtmrrsVQMIF--QDpFASLDPRMSVgtaimepfIEH-RLGTKQQARE 442
Cdd:COG0488 356 TLLKLLAGELEPDSGTV--------KLGET--------VKIGYfdQH-QEELDPDKTV--------LDElRDGAPGGTEQ 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 443 KAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADE--------AVSALDVSIKaqvcnllldlqqnl 514
Cdd:COG0488 411 EVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEptnhldieTLEALEEALD-------------- 476
|
570 580
....*....|....*....|....*
gi 549799341 515 nlAF----LFISHDMAVVERVSHRV 535
Cdd:COG0488 477 --DFpgtvLLVSHDRYFLDRVATRI 499
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
40-251 |
4.52e-27 |
|
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: 109.31 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIaPRETVAIVGESGSGKSvTSLSIMRLLDKKTS---RIEGKVMLGGRDLLALPEEEMRkvrgkdISMIFQEpmTS 116
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKS-TLLRCIAGLEKPDGgtiVLNGTVLFDSRKKINLPPQQRK------IGLVFQQ--YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 LNPIFPIGKQIAEALTVHqdiSSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPKLLIADEPT 196
Cdd:cd03297 86 LFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 197 TALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
331-547 |
8.81e-27 |
|
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: 109.11 E-value: 8.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLrtmRRSVQMIFQ- 409
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQVGVVLQe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 410 ---------DPFASLDPRMSVGTAI-------MEPFI-EHRLGTKQQAREKAADLlekvglspdmmrrfphefSGGQRQR 472
Cdd:cd03252 85 nvlfnrsirDNIALADPGMSMERVIeaaklagAHDFIsELPEGYDTIVGEQGAGL------------------SGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVsiKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIG 547
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDY--ESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-260 |
9.28e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.21 E-value: 9.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsiMRLLDKKTSRIEGKVMLGGRdllALPEEE 97
Cdd:PRK13650 4 IIEVKNLTFKYKEDQE-KYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLLEAESGQIIIDGD---LLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKdISMIFQEPmtslnpifpiGKQIAEAlTVHQD---------ISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQ 168
Cdd:PRK13650 76 VWDIRHK-IGMVFQNP----------DNQFVGA-TVEDDvafglenkgIPHEEMKERVNEALELVGMQDFKER---EPAR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVtiQGQiLDLIKTLQ---EEEGMSVLFITHDMGVVAeVSDRTIVMFRG 245
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP--EGR-LELIKTIKgirDDYQMTVISITHDLDEVA-LSDRVLVMKNG 216
|
250
....*....|....*
gi 549799341 246 DVVETGTTDDIFHRG 260
Cdd:PRK13650 217 QVESTSTPRELFSRG 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-248 |
9.48e-27 |
|
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: 108.11 E-value: 9.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLTTSFrvdGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLlalpeeeMR 99
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES----SGSILLNGKPI-------KA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 100 KVRGKDISMIFQEPMTSLnpifpIGKQIAEALTVHQDISSsAAKAEVIRLLEKVRIPNAKnrfDDYPHQFSGGMRQRVMI 179
Cdd:cd03226 67 KERRKSIGYVMQDVDYQL-----FTDSVREELLLGLKELD-AGNEQAETVLKDLDLYALK---ERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 180 AMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-252 |
1.42e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKS-VTSLsIMRLLDKKtsriEGKVMLGGRDLLALPEEEMRKVrgkd 105
Cdd:COG1132 346 SFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKStLVNL-LLRFYDPT----SGRILIDGVDIRDLTLESLRRQ---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 106 ISMIFQEPMtslnpIFpigkqiaeALTVHQDIS---SSAAKAEVIRLLEKVripNAKNRFDDYPHQF-----------SG 171
Cdd:COG1132 416 IGVVPQDTF-----LF--------SGTIRENIRygrPDATDEEVEEAAKAA---QAHEFIEALPDGYdtvvgergvnlSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVAEVsDRTIVMFRGDVVETG 251
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQG 556
|
.
gi 549799341 252 T 252
Cdd:COG1132 557 T 557
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-257 |
1.64e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDllALPEEEMRKVRGKdISMIFQEPm 114
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS----EGKVYVDGLD--TSDEENLWDIRNK-AGMVFQNP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 tslnpifpiGKQIAeALTVHQDIS----SSAAKAEVIRLlekvRIPNAKNRFDDY------PHQFSGGMRQRVMIAMALA 184
Cdd:PRK13633 95 ---------DNQIV-ATIVEEDVAfgpeNLGIPPEEIRE----RVDESLKKVGMYeyrrhaPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 185 SKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGTTDDIF 257
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
315-556 |
1.78e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.96 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldk 394
Cdd:PRK11432 7 VVLKNITKRF-----------GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttlrtmrRSVQ-----MIFQDpfASLDPRMSVGTAI-----MepfiehrLG-TKQQAREKAADLLEKVGLSpDMMRRFPH 463
Cdd:PRK11432 73 -------RSIQqrdicMVFQS--YALFPHMSLGENVgyglkM-------LGvPKEERKQRVKEALELVDLA-GFEDRYVD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:PRK11432 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
250
....*....|...
gi 549799341 544 VEIGPRAAVFDNP 556
Cdd:PRK11432 216 MQIGSPQELYRQP 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-328 |
2.05e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.43 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLA----- 92
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD----SGEVLWDGEPLDPedrrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 ---LPEEemrkvRGkdismifqepmtsLNPIFPIGKQIAEALTVHqDISSSAAKAEVIRLLEKVRIPNAKNRfddyP-HQ 168
Cdd:COG4152 73 igyLPEE-----RG-------------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANK----KvEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 249 ETGTTDDIfhRGRHPYTRALLSAVPKLGsmkerLLPARFPIIDIKTGESQPVADVKDTVSGGrtPILsvKDLTTRFDIRS 328
Cdd:COG4152 209 LSGSVDEI--RRQFGRNTLRLEADGDAG-----WLRALPGVTVVEEDGDGAELKLEDGADAQ--ELL--RALLARGPVRE 277
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-251 |
2.37e-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: 106.98 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLL--DKKTSRIEGKVM--LGGRDLLALP 94
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlpDSGEVLFDGKPLdiAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEE--MRKVRGKDISMIFqepmTSLnpifpigkqiaealtvhQDISSSAAKAEVIRLLEKVRIPNAKNRFDDyphQFSGG 172
Cdd:cd03269 77 EERglYPKMKVIDQLVYL----AQL-----------------KGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
314-547 |
2.42e-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: 107.07 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDIrsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLD 393
Cdd:cd03266 1 MITADALTKRFRD-------VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRrsvqmIFQDPFAsLDPRMSVgTAIMEPFieHRL-GTKQQAREKAAD-LLEKVGLSPDMMRRfPHEFSGGQRQ 471
Cdd:cd03266 74 AEARRRLG-----FVSDSTG-LYDRLTA-RENLEYF--AGLyGLKGDELTARLEeLADRLGMEELLDRR-VGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 472 RIAIARSLMLDPKVIVADEAVSALDVsIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
343-560 |
3.40e-26 |
|
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: 110.20 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 343 KVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLK--LDKTTLRTMRRSVQMIFQDpfASLDPRMS 420
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFdsRKGIFLPPEKRRIGYVFQE--ARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTAIMEPFIEHRLGTKQQAREKAADLLekvGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIK 500
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELL---GIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 501 AQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPY 560
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
344-556 |
3.63e-26 |
|
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: 110.19 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLkLD---KTTLRTMRRSVQMIFQDpfASLDPRMS 420
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVL-QDsarGIFLPPHRRRIGYVFQE--ARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 V------GtaimepfieHRLGTKQQAREKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:COG4148 94 VrgnllyG---------RKRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 495 LDVSIKAQVcnllldlqqnlnLAFL------------FISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNP 556
Cdd:COG4148 164 LDLARKAEI------------LPYLerlrdeldipilYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
315-544 |
3.84e-26 |
|
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: 104.82 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDk 394
Cdd:cd03216 1 LELRGITKRF-----------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 tTLRTMRRSVQMIFQdpfasldprmsvgtaimepfiehrlgtkqqarekaadllekvglspdmmrrfpheFSGGQRQRIA 474
Cdd:cd03216 69 -PRDARRAGIAMVYQ-------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVS-----------IKAQvcnllldlqqnlNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAeverlfkvirrLRAQ------------GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
.
gi 549799341 544 V 544
Cdd:cd03216 161 V 161
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
340-547 |
6.38e-26 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 106.55 E-value: 6.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdktTLRTMRRSVQMIFQDPFasldprM 419
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQIGLVSQDVF------L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTaIMEPFIEHRLGTKQQAREKAAdlleKVGLSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVA 488
Cdd:cd03251 88 FNDT-VAENIAYGRPGATREEVEEAA----RAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 489 DEAVSALDVSIKAQVCNLLLDLQQNLNLafLFISHDMAVVERvSHRVAVMYLGEIVEIG 547
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNRTT--FVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
314-543 |
7.37e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.51 E-value: 7.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDirsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEvlkLD 393
Cdd:PRK13650 4 IIEVKNLTFKYK--------EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDPfaslDPRMsVGtAIMEPFIEHRLGTK----QQAREKAADLLEKVGLSpDMMRRFPHEFSGGQ 469
Cdd:PRK13650 73 EENVWDIRHKIGMVFQNP----DNQF-VG-ATVEDDVAFGLENKgiphEEMKERVNEALELVGMQ-DFKEREPARLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVErVSHRVAVMYLGEI 543
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-543 |
9.38e-26 |
|
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: 111.07 E-value: 9.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdGGWKSVvRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDK--KTSRIEGKVMLGGRDLLAlpe 95
Cdd:TIGR02633 1 LLEMKGIVKTF---GGVKAL-DGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvyPHGTWDGEIYWSGSPLKA--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQE-----PMTSLNPIFpIGKQIA-EALTVHQDISSSAAKAevirLLEKVRIPNAKNRFDdyPHQF 169
Cdd:TIGR02633 70 SNIRDTERAGIVIIHQEltlvpELSVAENIF-LGNEITlPGGRMAYNAMYLRAKN----LLRELQLDADNVTRP--VGDY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDrTIVMFRGdvve 249
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCD-TICVIRD---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 250 tgttddifhrGRHPYTRAL--LSAVPKLGSMKERLLPARFPiidiktGESQPVADVkdtvsggrtpILSVKDLTTrFDIR 327
Cdd:TIGR02633 217 ----------GQHVATKDMstMSEDDIITMMVGREITSLYP------HEPHEIGDV----------ILEARNLTC-WDVI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 328 SGLFGRksgavhaVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPT-SGDVMLDGYEVLKldKTTLRTMRRSVQM 406
Cdd:TIGR02633 270 NPHRKR-------VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDI--RNPAQAIRAGIAM 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 407 IFQD-PFASLDPRMSVGTAIMEPFIEHRLG-------TKQQAREKAADLLEKVGLSPDMmrrfP-HEFSGGQRQRIAIAR 477
Cdd:TIGR02633 341 VPEDrKRHGIVPILGVGKNITLSVLKSFCFkmridaaAELQIIGSAIQRLKVKTASPFL----PiGRLSGGNQQKAVLAK 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 478 SLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
344-544 |
9.81e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.03 E-value: 9.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlklDKTTLRTMRRSVQMIFQDP----FASldprm 419
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG------KPIKAKERRKSIGYVMQDVdyqlFTD----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVgtaimepFIEHRLGTKQQAR--EKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:cd03226 88 SV-------REELLLGLKELDAgnEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 549799341 498 SIKAQVCnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIV 544
Cdd:cd03226 160 KNMERVG-ELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
51-260 |
9.94e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 9.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 51 VAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEMRKVRGKDISMIFQepmtslnpiFPiGKQIAEA 130
Cdd:PRK13634 36 VAIIGHTGSGKS-TLLQHLNGLLQPTS---GTVTIGERVITAGKKNKKLKPLRKKVGIVFQ---------FP-EHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 131 lTVHQDI---------SSSAAKAEVIRLLEKVRIPNAKnrFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDV 201
Cdd:PRK13634 102 -TVEKDIcfgpmnfgvSEEDAKQKAREMIELVGLPEEL--LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 202 TIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRG 260
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
340-557 |
1.04e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKLDKTTLRTMRRSVQMIFQDP----FAsl 415
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKKSLLEVRKTVGIVFQNPddqlFA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 dPRMSVGTAimepFIEHRLG-TKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK13639 94 -PTVEEDVA----FGPLNLGlSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 495 LDVSIKAQVCNLLLDLQQNLNLafLFIS-HDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGIT--IIIStHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-272 |
1.33e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.25 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTsrieGKVMLGGRDLLALPEEEM 98
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS----GTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rkvrGKDISMIFQEPMTSlnpifpigkqiaEALTVHQDIS-------------SSAAKAEVIRLLEKVRIPN-AKNRFDD 164
Cdd:PRK11231 75 ----ARRLALLPQHHLTP------------EGITVRELVAygrspwlslwgrlSAEDNARVNQAMEQTRINHlADRRLTD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 165 yphqFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFR 244
Cdd:PRK11231 139 ----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLAN 213
|
250 260
....*....|....*....|....*...
gi 549799341 245 GDVVETGTTDDIFhrgrhpyTRALLSAV 272
Cdd:PRK11231 214 GHVMAQGTPEEVM-------TPGLLRTV 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-552 |
1.46e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.53 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 8 MEQTGGSVSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGG 87
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKS----TLMKIIAGIVPPDSGTLEIGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 88 RDLLALPEEEMRKVrgkDISMIFQEPMtslnpIFPigkqiaeALTVHQDISSSAAKAEVI--RLLEKVRIPNAKNRFDDY 165
Cdd:PRK15439 73 NPCARLTPAKAHQL---GIYLVPQEPL-----LFP-------NLSVKENILFGLPKRQASmqKMKQLLAALGCQLDLDSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEeGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:PRK15439 138 AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 246 DVVETGTTDDIfhrgrhpYTRALLSAVPKlGSMKERLLPARFPIIDIKTGESQPVADvkdtvsggrTPILSVKDLTtrfd 325
Cdd:PRK15439 217 TIALSGKTADL-------STDDIIQAITP-AAREKSLSASQKLWLELPGNRRQQAAG---------APVLTVEDLT---- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 326 irsglfgrKSGAVHavekVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDktTLRTMRRSVQ 405
Cdd:PRK15439 276 --------GEGFRN----ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS--TAQRLARGLV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 406 MIFQDPFAS---LDPRMSVGTAimePFIEHRLGTKQQ-AREKAadLLEKVGLSpdMMRRFPHE------FSGGQRQRIAI 475
Cdd:PRK15439 342 YLPEDRQSSglyLDAPLAWNVC---ALTHNRRGFWIKpARENA--VLERYRRA--LNIKFNHAeqaartLSGGNQQKVLI 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 476 ARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
346-547 |
2.29e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 104.11 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 346 FDL--AEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlkLDKTTLRTMRRSVQMIFQDP--FASLDPRMSV 421
Cdd:cd03298 17 FDLtfAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----VDVTAAPPADRPVSMLFQENnlFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 GTAIMEpfiehRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKA 501
Cdd:cd03298 92 GLGLSP-----GLKLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 549799341 502 QVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
315-547 |
2.35e-25 |
|
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: 104.28 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:cd03269 1 LEVENVTKRF-----------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTL----------RTMRRSVQMIFqdpFASLdprmsvgtaimepfiehRLGTKQQAREKAADLLEKVGLSPDMMRRFpHE 464
Cdd:cd03269 70 NRIgylpeerglyPKMKVIDQLVY---LAQL-----------------KGLKKEEARRRIDEWLERLELSEYANKRV-EE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 465 FSGGQRQRIAIARSLMLDPKVIVADEAVSALDVsIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIV 544
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
...
gi 549799341 545 EIG 547
Cdd:cd03269 208 LYG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
312-554 |
2.37e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlk 391
Cdd:COG1121 4 MPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 ldkTTLRTMRRSV----QMifqdpfASLDPR--MSVGTAIMEPFIEHR---LGTKQQAREKAADLLEKVGLSpDMMRRFP 462
Cdd:COG1121 68 ---KPPRRARRRIgyvpQR------AEVDWDfpITVRDVVLMGRYGRRglfRRPSRADREAVDEALERVGLE-DLADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 463 HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV-----------SIKAQVCnllldlqqnlnlAFLFISHDMAVVERV 531
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAateealyellrELRREGK------------TILVVTHDLGAVREY 205
|
250 260
....*....|....*....|...
gi 549799341 532 SHRVAVMyLGEIVEIGPRAAVFD 554
Cdd:COG1121 206 FDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-228 |
2.54e-25 |
|
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: 103.71 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLttSFRVDGGWksVVRNMSFEIAPRETVAIVGESGSGKsvTSLsiMRLLDKKTSRIEGKVMLGGRDLLALPEE 96
Cdd:COG4133 1 MMLEAENL--SCRRGERL--LFSGLSFTLAAGEALALTGPNGSGK--TTL--LRILAGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 emrkvRGKDISMIFQEPM--TSLNPifpigkqiAEALTVHQDISSSAAKAEVI-RLLEKVRIPNAKNRFddyPHQFSGGM 173
Cdd:COG4133 73 -----YRRRLAYLGHADGlkPELTV--------RENLRFWAALYGLRADREAIdEALEAVGLAGLADLP---VRQLSAGQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMsVLFITHD 228
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
287-551 |
2.77e-25 |
|
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: 110.23 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 287 FPIIDiktGESQPVADVKDTVSGGRTPILSVKDLTTRFDirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKST 366
Cdd:COG4988 312 FALLD---APEPAAPAGTAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 367 TGRSITRLIEPTSGDVMLDGYEVLKLDKTTLrtmRRSVQMIFQDP--FAsldprmsvGTaIMEpFIehRLGTKQQAREKA 444
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPylFA--------GT-IRE-NL--RLGRPDASDEEL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 445 ADLLEKVGLSpDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcnLLLDLQQN 513
Cdd:COG4988 444 EAALEAAGLD-EFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI--LQALRRLA 520
|
250 260 270
....*....|....*....|....*....|....*...
gi 549799341 514 LNLAFLFISHDMAVVERVSHRVaVMYLGEIVEIGPRAA 551
Cdd:COG4988 521 KGRTVILITHRLALLAQADRIL-VLDDGRIVEQGTHEE 557
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-262 |
2.78e-25 |
|
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: 104.47 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAlpeeemrkvRGKDISMIFQEpmTSL 117
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQPTS---GGVILEGKQITE---------PGPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPIGKQIAEAL-TVHQDISSSAAKAEVIRLLEKVRIPNAKnrfDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPT 196
Cdd:TIGR01184 66 LPWLTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 197 TALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI-FHRGRH 262
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-563 |
2.84e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.13 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKLDKTTLR----TMRRSVQMIFQDPfaSLD 416
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG-KVLYFGKDIFQidaiKLRKEVGMVFQQP--NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 417 PRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRF---PHEFSGGQRQRIAIARSLMLDPKVIVADEAVS 493
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 494 ALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKK 563
Cdd:PRK14246 183 MIDIVNSQAI--EKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-229 |
3.09e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.51 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPE 95
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPTS---GDVIFNGQPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQepMTSLNPIFPIGKQIAEALTVHQDISSSAAKaeviRLLEKVRIPNAKNRFDDYPHQFSGGMRQ 175
Cdd:PRK11629 79 AAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINS----RALEMLAAVGLEHRANHRPSELSGGERQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDM 229
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-236 |
3.10e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.72 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsfrVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLS-IMRLLDKKTSrIEGKVMLGGRDLLALPEEE 97
Cdd:COG4136 2 LSLENLT----ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAaIAGTLSPAFS-ASGEVLLNGRRLTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRkvrgkdISMIFQEPMtsLNPIFPIGKQIAEALTvhQDISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQRV 177
Cdd:COG4136 76 RR------IGILFQDDL--LFPHLSVGENLAFALP--PTIGRAQRRARVEQALEEA---GLAGFADRDPATLSGGQRARV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVS 236
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
344-535 |
3.61e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.13 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMR-RSVQMIFQdpFASLDPRMSVG 422
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 423 TAIMEPFIehrLGTK--QQAREKAADLLEKVGLSPDMMRRfPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIK 500
Cdd:PRK11629 106 ENVAMPLL---IGKKkpAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|....*
gi 549799341 501 AQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRV 535
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
344-503 |
3.62e-25 |
|
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: 104.54 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDkttLRTMRRSVQMIFQDP--FAsldprmsv 421
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPvlFD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 gTAIMEPFIEHRLGTKQQAREKAAdlleKVGLSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:cd03249 91 -GTIAENIRYGKPDATDEEVEEAA----KKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDE 165
|
170
....*....|...
gi 549799341 491 AVSALDVSIKAQV 503
Cdd:cd03249 166 ATSALDAESEKLV 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
336-547 |
4.18e-25 |
|
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: 102.51 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRrsvqmifqdpfasl 415
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 dprmsvgtAIMEpfiehrlgtkqQArekaadlLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:cd03214 76 --------AYVP-----------QA-------LELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
312-538 |
4.79e-25 |
|
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: 103.67 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFDI--RSGLfgrksgAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLD-GYE 388
Cdd:COG4778 2 TTLLEVENLSKTFTLhlQGGK------RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 389 VLKLDKTTLRTM----RRSVQMIFQdpFASLDPRMSVGTAIMEPFIEhrLGT-KQQAREKAADLLEKVGLSPDMMRRFPH 463
Cdd:COG4778 76 WVDLAQASPREIlalrRRTIGYVSQ--FLRVIPRVSALDVVAEPLLE--RGVdREEARARARELLARLNLPERLWDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVM 538
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
313-524 |
5.02e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.56 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkl 392
Cdd:COG4525 2 SMLTVRHVSVRY-------PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 dktTLRTMRRSVqmIFQDpfASLDPRMSVGTAIMEPFIEHRLGtKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQR 472
Cdd:COG4525 72 ---TGPGADRGV--VFQK--DALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGLA-DFARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHD 524
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-555 |
5.03e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKlDKTTLRTMRRSVQMIFQDPFASLdprm 419
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQL---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 svgtaiMEPFIEH-------RLG-TKQQAREKAADLLEKVGLSPDMMR-RFPHEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PRK13637 97 ------FEETIEKdiafgpiNLGlSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDN 555
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-257 |
5.87e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 5 ATSMEQTGgSVSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVM 84
Cdd:PRK09452 2 KKLNKQPS-SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 85 LGGRDLLALPEEEmrkvrgKDISMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRfdd 164
Cdd:PRK09452 73 LDGQDITHVPAEN------RHVNTVFQS--YALFPHMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQR--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 165 YPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFR 244
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD 220
|
250
....*....|...
gi 549799341 245 GDVVETGTTDDIF 257
Cdd:PRK09452 221 GRIEQDGTPREIY 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-250 |
6.40e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 101.35 E-value: 6.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdGGWKsVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03216 1 LELRGITKRF---GGVK-ALDGVSLSVRRGEVHALLGENGAGKS----TLMKILSGLYKPDSGEILVDGKEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvRGkdISMIfqepmtslnpifpigkqiaealtvhqdisssaakaevirllekvripnaknrfddypHQFSGGMRQRVM 178
Cdd:cd03216 73 RR-AG--IAMV---------------------------------------------------------YQLSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVET 250
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
344-571 |
7.49e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 7.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV-LKLDKTTLRTMRRSVQMIFQDPFASLDPRmSVG 422
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQLFEN-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 423 TAIMepFIEHRLG-TKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKA 501
Cdd:PRK13641 105 KDVE--FGPKNFGfSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 502 QVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQhpYTKKLMSAVPVP 571
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE--WLKKHYLDEPAT 249
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-252 |
7.69e-25 |
|
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: 102.96 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGWksVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDkktsRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RkvrgKDISMIFQEPMT-------SLNPifpigkqiaeaLTVHQDisssaakAEVIRLLEKVRIpnaKNRFDDYPHQ--- 168
Cdd:cd03244 77 R----SRISIIPQDPVLfsgtirsNLDP-----------FGEYSD-------EELWQALERVGL---KEFVESLPGGldt 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 --------FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTlqEEEGMSVLFITHDMGVVAEvSDRTI 240
Cdd:cd03244 132 vveeggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRIL 208
|
250
....*....|..
gi 549799341 241 VMFRGDVVETGT 252
Cdd:cd03244 209 VLDKGRVVEFDS 220
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
19-238 |
9.89e-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: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSF---RVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMR--LLDKKT--SRIEGKVMlggrDLL 91
Cdd:TIGR02324 2 LEVEDLSKTFtlhQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnyLPDSGRilVRHEGAWV----DLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 ALPEEEMRKVRGKDISMIFQepMTSLNPIFPIGKQIAEALtVHQDISSSAAKAEVIRLLEKVRIPnaKNRFDDYPHQFSG 171
Cdd:TIGR02324 78 QASPREVLEVRRKTIGYVSQ--FLRVIPRVSALEVVAEPL-LERGVPREAARARARELLARLNIP--ERLWHLPPATFSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDR 238
Cdd:TIGR02324 153 GEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAK-ARGAALIGIFHDEEVRELVADR 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-556 |
1.02e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.08 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKS--GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQD 410
Cdd:PRK11650 10 RKSydGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELEPADRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 pFAsLDPRMSV-----------GTAIMEpfIEHRLgtkqqarEKAADLLEkvgLSPdMMRRFPHEFSGGQRQRIAIARSL 479
Cdd:PRK11650 85 -YA-LYPHMSVrenmayglkirGMPKAE--IEERV-------AEAARILE---LEP-LLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 480 MLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMavVE--RVSHRVAVMYLGEIVEIGPRAAVFDNP 556
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ--VEamTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
340-569 |
1.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.01 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLklDKTTLRTMRRSVQMIFQDPFASLdprm 419
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 sVGTAIME--PFIEHRLGTKQ-QAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK13633 99 -VATIVEEdvAFGPENLGIPPeEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 497 VSIKAQVCNLLLDLQQNLNLAFLFISHDM-AVVErvSHRVAVMYLGEIVEIGPRAAVFdnPQHPYTKKLMSAVP 569
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIF--KEVEMMKKIGLDVP 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-259 |
1.69e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDggwKSVVRNMSFeIAPRET-VAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRdllALPEE 96
Cdd:PRK13652 3 LIETRDLCYSYSGS---KEALNNINF-IAPRNSrIAVIGPNGAGKS----TLFRHFNGILKPTSGSVLIRGE---PITKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRgKDISMIFQEPMtslNPIFpigkqiaeALTVHQDIS----SSAAKAEVI--RLLEKVRIPNAKNRFDDYPHQFS 170
Cdd:PRK13652 72 NIREVR-KFVGLVFQNPD---DQIF--------SPTVEQDIAfgpiNLGLDEETVahRVSSALHMLGLEELRDRVPHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVET 250
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
....*....
gi 549799341 251 GTTDDIFHR 259
Cdd:PRK13652 220 GTVEEIFLQ 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-260 |
1.78e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTsriEGKVMLGGrdlLALPEEEMRKVRgKDI 106
Cdd:PRK13648 14 SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKS-TIAKLMIGIEKVK---SGEIFYNN---QAITDDNFEKLR-KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 107 SMIFQEPMTSLnpIFPIGK-QIAEALTVHQdISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQRVMIAMALAS 185
Cdd:PRK13648 86 GIVFQNPDNQF--VGSIVKyDVAFGLENHA-VPYDEMHRRVSEALKQV---DMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 186 KPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGTTDDIFHRG 260
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
313-566 |
1.85e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLttrfdirSGLFGRKSgavhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRL--IEP---TSGDVMLDGY 387
Cdd:PRK14239 4 PILQVSDL-------SVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 EVLKLDKTTLRtMRRSVQMIFQ--DPFA-SLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVglsPDMMRRFPHE 464
Cdd:PRK14239 73 NIYSPRTDTVD-LRKEIGMVFQqpNPFPmSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEV---KDRLHDSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 465 FSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIV 544
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI--EETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250 260
....*....|....*....|..
gi 549799341 545 EIGPRAAVFDNPQHPYTKKLMS 566
Cdd:PRK14239 227 EYNDTKQMFMNPKHKETEDYIS 248
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-255 |
2.43e-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: 101.85 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPeeeMRKVRGKdISMIFQEPMts 116
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQ-IGLVSQEPV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 lnpIFPIgkqiaealTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQF-----------SGGMRQRVMIAMALAS 185
Cdd:cd03249 88 ---LFDG--------TIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 186 KPKLLIADEPTTALDVTIQGQI---LDLIKtlqeeEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGTTDD 255
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVqeaLDRAM-----KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-256 |
2.44e-24 |
|
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: 101.98 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPE 95
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR----SGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKvRGkdISMIfqepmtslnpifPIGKQIAEALTVHQDI----SSSAAKAEVIRLLEKV--RIPNAKNRFDDYPHQF 169
Cdd:COG0410 73 HRIAR-LG--IGYV------------PEGRRIFPSLTVEENLllgaYARRDRAEVRADLERVyeLFPRLKERRRQRAGTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
....*..
gi 549799341 250 TGTTDDI 256
Cdd:COG0410 217 EGTAAEL 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
35-252 |
2.57e-24 |
|
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: 101.92 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVrgkdISMIFQEpm 114
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA----IGVVPQD-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 tslNPIF--PIGKQIAEAltvhqdiSSSAAKAEVIRLLEKVRIPNAKNRFDD-YPHQ-------FSGGMRQRVMIAMALA 184
Cdd:cd03253 84 ---TVLFndTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRFPDgYDTIvgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 185 SKPKLLIADEPTTALDVT----IQGQILDLIKtlqeeeGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGT 252
Cdd:cd03253 154 KNPPILLLDEATSALDTHtereIQAALRDVSK------GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-251 |
2.85e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 100.75 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEM 98
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKT-TTMKIILGLIKPDS---GEITFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RkvrgkdISMIFQEPmtSLNPifpigkqiaeALTVHQDISSSAA-----KAEVIRLLEKVripNAKNRFDDYPHQFSGGM 173
Cdd:cd03268 73 R------IGALIEAP--GFYP----------NLTARENLRLLARllgirKKRIDEVLDVV---GLKDSAKKKVKGFSLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-568 |
3.28e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 3.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSG-----DVMLDGYEVLklDKTTLRTMRRSVQMIFQDPfasl 415
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIF--NYRDVLEFRRRVGMLFQRP---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DP-RMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGL---SPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:PRK14271 111 NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 492 VSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:PRK14271 191 TSALDPTTTEKI--EEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
314-581 |
3.99e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.39 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVML-DGYEVLKL 392
Cdd:PRK13631 21 ILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKTT------------LRTMRRSVQMIFQDPFASLDpRMSVGTAIMepFIEHRLG-TKQQAREKAADLLEKVGLSPDMMR 459
Cdd:PRK13631 95 NNHElitnpyskkiknFKELRRRVSMVFQFPEYQLF-KDTIEKDIM--FGPVALGvKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 460 RFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMY 539
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMD 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 549799341 540 LGEIVEIGPRAAVFDNpQHPYTKKLMSAVPVPDPARRQIKRN 581
Cdd:PRK13631 251 KGKILKTGTPYEIFTD-QHIINSTSIQVPRVIQVINDLIKKD 291
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
314-552 |
4.52e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.88 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYevlKLD 393
Cdd:COG4152 1 MLELKGLTKRF-----------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTM------RrsvqmifqdpfaSLDPRMSVGTAIMepfiehRLG-----TKQQAREKAADLLEKVGLSPDMMRRFp 462
Cdd:COG4152 67 PEDRRRIgylpeeR------------GLYPKMKVGEQLV------YLArlkglSKAEAKRRADEWLERLGLGDRANKKV- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 463 HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDvSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGE 542
Cdd:COG4152 128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
250
....*....|
gi 549799341 543 IVEIGPRAAV 552
Cdd:COG4152 207 KVLSGSVDEI 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
346-547 |
5.35e-24 |
|
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: 100.32 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 346 FDL--AEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlkLDKTTLRTMRRSVQMIFQDP--FASLDPRMSV 421
Cdd:TIGR01277 17 FDLnvADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND-----QSHTGLAPYQRPVSMLFQENnlFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 GTAImEPFIehRLGTKQQarEKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKA 501
Cdd:TIGR01277 92 GLGL-HPGL--KLNAEQQ--EKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 549799341 502 QVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-251 |
5.69e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 100.26 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFE--IAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEmrkvrgKDISMIFQEpmtsl 117
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKS-TLLNLIAGFETPQS---GRVLINGVDVTAAPPAD------RPVSMLFQE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFPigkqiaeALTVHQDIS---------SSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQRVMIAMALASKPK 188
Cdd:cd03298 79 NNLFA-------HLTVEQNVGlglspglklTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-251 |
5.88e-24 |
|
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: 100.52 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsiMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLLEPDAGFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVrgkdismifqepmtslnPIFPIGKQIAEALTVHQDI---------SSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQF 169
Cdd:cd03266 78 RRL-----------------GFVSDSTGLYDRLTARENLeyfaglyglKGDELTARLEELADRLGM---EELLDRRVGGF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
..
gi 549799341 250 TG 251
Cdd:cd03266 217 EG 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
40-247 |
8.42e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 99.79 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVRGKdISMIFQEpmTSLNP 119
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 120 IFPIGKQIAEALTVHQDISSSAAKaEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTAL 199
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRK-RVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 549799341 200 DVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDV 247
Cdd:cd03292 168 DPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
42-256 |
9.63e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 42 SFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEmrkvrgKDISMIFQEpmtslNPIF 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIAGFLTPAS---GSLTLNGQDHTTTPPSR------RPVSMLFQE-----NNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 122 PigkqiaeALTVHQDIS---------SSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQRVMIAMALASKPKLLIA 192
Cdd:PRK10771 84 S-------HLTVAQNIGlglnpglklNAAQREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 193 DEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-257 |
1.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.39 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTsrieGKVMLGGRDLLA-LPEEEMRKVRgKDISMIFQEPMTs 116
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT----GTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPES- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 lnpifpigkQIAEAlTVHQDI---------SSSAAKAEVIRLLEKVRIPnaKNRFDDYPHQFSGGMRQRVMIAMALASKP 187
Cdd:PRK13646 97 ---------QLFED-TVEREIifgpknfkmNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 188 KLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-228 |
1.29e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAlPee 96
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIAGFLAPSS---GEITLDGVPVTG-P-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 emrkvrGKDISMIFQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQR 176
Cdd:COG4525 75 ------GADRGVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 549799341 177 VMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHD 228
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
340-547 |
1.45e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.04 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdktTLRTMRRSVQMIFQDP--FA-SLD 416
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRRNIAVVFQDAglFNrSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 417 PRMSVG--TAIMEpfiEHRLGTKqqaREKAADLLEKVGLSPDMM-----RRFphefSGGQRQRIAIARSLMLDPKVIVAD 489
Cdd:PRK13657 427 DNIRVGrpDATDE---EMRAAAE---RAQAHDFIERKPDGYDTVvgergRQL----SGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 490 EAVSALDVSIKAQVcNLLLDLQQNLNLAFLfISHDMAVVeRVSHRVAVMYLGEIVEIG 547
Cdd:PRK13657 497 EATSALDVETEAKV-KAALDELMKGRTTFI-IAHRLSTV-RNADRILVFDNGRVVESG 551
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-268 |
1.62e-23 |
|
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: 99.48 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKvrgkDI 106
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKS----TLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR----QV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 107 SMIFQEpmtslNPIFpigkqiaeALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQF-----------SGGMRQ 175
Cdd:cd03252 79 GVVLQE-----NVLF--------NRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVaEVSDRTIVMFRGDVVETGTTDD 255
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDE 222
|
250
....*....|....
gi 549799341 256 IF-HRGRHPYTRAL 268
Cdd:cd03252 223 LLaENGLYAYLYQL 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
42-264 |
1.87e-23 |
|
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: 102.11 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 42 SFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDL------LALPEEEMRkvrgkdISMIFQEpmT 115
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKT----TLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRR------IGYVFQE--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 116 SLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLekvripNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEP 195
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISFERVIELL------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 196 TTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRGRHPY 264
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-257 |
1.91e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSF---RVDGGWksVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGRDLLALP 94
Cdd:PRK13631 21 ILRVKNLYCVFdekQENELV--ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEM---RKVRG-----KDISMIFQEPMTSLnpiFP--IGKQIA---EALTVHQDISSSAAKAEVIRLlekvripNAKNR 161
Cdd:PRK13631 99 LITNpysKKIKNfkelrRRVSMVFQFPEYQL---FKdtIEKDIMfgpVALGVKKSEAKKLAKFYLNKM-------GLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 162 F-DDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTlQEEEGMSVLFITHDMGVVAEVSDRTI 240
Cdd:PRK13631 169 YlERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVI 247
|
250
....*....|....*..
gi 549799341 241 VMFRGDVVETGTTDDIF 257
Cdd:PRK13631 248 VMDKGKILKTGTPYEIF 264
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
315-555 |
2.05e-23 |
|
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: 99.05 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdk 394
Cdd:cd03224 1 LEVENLNAGY-----------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRRSVQMIFQDPfaSLDPRMSVgtaiMEPFiehRLGTKQQAREKAADLLEKV-GLSP---DMMRRFPHEFSGGQR 470
Cdd:cd03224 68 PPHERARAGIGYVPEGR--RIFPELTV----EENL---LLGAYARRRAKRKARLERVyELFPrlkERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRA 550
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
....*
gi 549799341 551 AVFDN 555
Cdd:cd03224 218 ELLAD 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-266 |
2.18e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.11 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVdggwKSVVRNMSFEIAPRETVAIVGESGSGKS--VTSLSIMRLLDKKTsRIEGKVMLGGRDLLAlP 94
Cdd:PRK14258 6 PAIKVNNLSFYYDT----QKILEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNELESEV-RVEGRVEFFNQNIYE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVRgKDISMIFQEPmtslnPIFPIGKQIAEALTVH----------QDISSSAAKAEviRLLEKVripnaKNRFDD 164
Cdd:PRK14258 80 RVNLNRLR-RQVSMVHPKP-----NLFPMSVYDNVAYGVKivgwrpkleiDDIVESALKDA--DLWDEI-----KHKIHK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 165 YPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTiVMFR 244
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFT-AFFK 225
|
250 260
....*....|....*....|....*...
gi 549799341 245 GD------VVETGTTDDIFHRGRHPYTR 266
Cdd:PRK14258 226 GNenrigqLVEFGLTKKIFNSPHDSRTR 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-248 |
2.56e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGGW-KSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMR---LLDkktsriEGKVMLGGRDLLALP 94
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIAgslPPD------SGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEmrkvRGKDISMIFQEPM--TslnpifpigkqiAEALTVHQDIS---------------SSAAKAEVIRLLEKVRIpN 157
Cdd:COG1101 75 EYK----RAKYIGRVFQDPMmgT------------APSMTIEENLAlayrrgkrrglrrglTKKRRELFRELLATLGL-G 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 158 AKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSD 237
Cdd:COG1101 138 LENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGN 217
|
250
....*....|.
gi 549799341 238 RTIVMFRGDVV 248
Cdd:COG1101 218 RLIMMHEGRII 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
345-551 |
3.14e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 345 SFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlkLDKTTLRTMRRSVQMIFQDP--FASLDPRMSVG 422
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----QDHTTTPPSRRPVSMLFQENnlFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 423 TAiMEPFIehRLGTKQqaREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKA- 501
Cdd:PRK10771 94 LG-LNPGL--KLNAAQ--REKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQe 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 502 ------QVCnllldlqQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAA 551
Cdd:PRK10771 168 mltlvsQVC-------QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-251 |
4.46e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 97.65 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsFRVDGGWksVVRNMSFEIaPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEeM 98
Cdd:cd03264 1 LQLENLT--KRYGKKR--ALDGVSLTL-GPGMYGLLGPNGAGKT----TLMRILATLTPPSSGTIRIDGQDVLKQPQK-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVrgkdISMIFQEPMTSlnPIFPIGKQIAEALTVHqDISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGGMRQRVM 178
Cdd:cd03264 71 RRR----IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELV---NLGDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEgmSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-257 |
4.96e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRvDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLlALPEEE 97
Cdd:PRK13639 1 ILETRDLKYSYP-DG--TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT----SGEVLIKGEPI-KYDKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRgKDISMIFQEPMtslNPIFpigkqiaeALTVHQDI---------SSSAAKAEVIRLLEKVRIPNAKNRfddYPHQ 168
Cdd:PRK13639 73 LLEVR-KTVGIVFQNPD---DQLF--------APTVEEDVafgplnlglSKEEVEKRVKEALKAVGMEGFENK---PPHH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
....*....
gi 549799341 249 ETGTTDDIF 257
Cdd:PRK13639 217 KEGTPKEVF 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-247 |
5.43e-23 |
|
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: 96.13 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKS----TLARLILGLLRPTSGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdismifqepmtslnpifpigkqiaealTVHQDIS-SSAAKAEVIrllekvripnaknrfddyphqFSGGMRQRV 177
Cdd:cd03246 75 GDHVG----------------------------YLPQDDElFSGSIAENI---------------------LSGGQRQRL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVsDRTIVMFRGDV 247
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
313-562 |
6.85e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 6.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDIRSglfgrksgavhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEpTSGDVMLDG------ 386
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-----------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 387 ---YEvlklDKTTLRTMRRSVQMIFQDPfaSLDPrMSV------GTAIM--EPFIEhrLGTKQQAREKAADLLEKVglsP 455
Cdd:PRK14258 74 qniYE----RRVNLNRLRRQVSMVHPKP--NLFP-MSVydnvayGVKIVgwRPKLE--IDDIVESALKDADLWDEI---K 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 456 DMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRV 535
Cdd:PRK14258 142 HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFT 221
|
250 260 270
....*....|....*....|....*....|..
gi 549799341 536 AVMY-----LGEIVEIGPRAAVFDNPQHPYTK 562
Cdd:PRK14258 222 AFFKgnenrIGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
35-257 |
7.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLL---DKKTSRIegkVMLGgrdlLALPEEEMRKVRGKdISMIFQ 111
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKI---TVDG----ITLTAKTVWDIREK-VGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 112 EPmtslnpifpiGKQIAEAlTVHQDIS-----SSAAKAEVIRLLEKVRIPNAKNRF-DDYPHQFSGGMRQRVMIAMALAS 185
Cdd:PRK13640 92 NP----------DNQFVGA-TVGDDVAfglenRAVPRPEMIKIVRDVLADVGMLDYiDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 186 KPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGvVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-260 |
8.23e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 97.30 E-value: 8.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 26 TSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPEEEMRKVrgkd 105
Cdd:cd03254 8 VNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ----KGQILIDGIDIRDISRKSLRSM---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 106 ISMIFQEPMtslnpIFPigKQIAEALTVHQDIsssAAKAEVIRLLEKVR----IPNAKNRFDDYP----HQFSGGMRQRV 177
Cdd:cd03254 79 IGVVLQDTF-----LFS--GTIMENIRLGRPN---ATDEEVIEAAKEAGahdfIMKLPNGYDTVLgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGTTDDIF 257
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
...
gi 549799341 258 HRG 260
Cdd:cd03254 226 AKK 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
294-497 |
9.77e-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: 102.05 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 294 TGESQPVADV---KDTVSGGRTPILSVKDLTTRFDirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRS 370
Cdd:TIGR02868 311 LDAAGPVAEGsapAAGAVGLGKPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 371 ITRLIEPTSGDVMLDGYEVLKLDKTTLrtmRRSVQMIFQDP--FASldprmSVGTAImepfiehRLGTKQQAREKAADLL 448
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAhlFDT-----TVRENL-------RLARPDATDEELWAAL 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 449 EKVGLSpDMMRRFPH-----------EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:TIGR02868 446 ERVGLA-DWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
312-557 |
1.01e-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: 97.36 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:COG0410 1 MPMLEVENLHAGY-----------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDktTLRTMRRSV------QMIFqdpfasldPRMSVgtaimepfIEH-RLGTKQQ-AREKAADLLEKVglspdmMRRFP- 462
Cdd:COG0410 70 LP--PHRIARLGIgyvpegRRIF--------PSLTV--------EENlLLGAYARrDRAEVRADLERV------YELFPr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 463 -HEF--------SGGQRQRIAIARSLMLDPKVIVADEA-----------VSALDVSIKAQvcnllldlqqnlNLAFLFIS 522
Cdd:COG0410 126 lKERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPslglapliveeIFEIIRRLNRE------------GVTILLVE 193
|
250 260 270
....*....|....*....|....*....|....*
gi 549799341 523 HDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:COG0410 194 QNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
336-544 |
1.04e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.87 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDPFASL 415
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAImePFIEHRlGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:PRK10908 93 DRTVYDNVAI--PLIIAG-ASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 549799341 496 DVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIV 544
Cdd:PRK10908 169 DDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
340-548 |
1.08e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 102.49 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdktTLRTMRRSVQMIFQDPFASLDPRM 419
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLRRQVALVSQDVVLFNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 -SVGTAIMEPFIEHRLgtkqQAREKAADLLEKVGLSPDMMRRFPHE----FSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:TIGR02203 424 nNIAYGRTEQADRAEI----ERALAAAYAQDFVDKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 549799341 495 LDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGP 548
Cdd:TIGR02203 500 LDNESERLV--QAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-549 |
1.35e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 96.53 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 339 HAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMrrsVQMIFQDPFasldpr 418
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---IGVVLQDTF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 MSVGTaIMEPFiehRLGTKQQAREKAADLLEKVGLSpDMMRRFP-----------HEFSGGQRQRIAIARSLMLDPKVIV 487
Cdd:cd03254 88 LFSGT-IMENI---RLGRPNATDEEVIEAAKEAGAH-DFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 488 ADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGPR 549
Cdd:cd03254 163 LDEATSNIDTETEKLI--QEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
344-547 |
1.50e-22 |
|
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: 102.51 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDPF----------A 413
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLR---RQMGVVLQENVlfsrsirdniA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 414 SLDPRMSVGTAI-------MEPFI-EHRLGTKQQAREKAADLlekvglspdmmrrfphefSGGQRQRIAIARSLMLDPKV 485
Cdd:TIGR01846 553 LCNPGAPFEHVIhaaklagAHDFIsELPQGYNTEVGEKGANL------------------SGGQRQRIAIARALVGNPRI 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 486 IVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVeRVSHRVAVMYLGEIVEIG 547
Cdd:TIGR01846 615 LIFDEATSALDYESEALI--MRNMREICRGRTVIIIAHRLSTV-RACDRIIVLEKGQIAESG 673
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-248 |
1.88e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPE 95
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPTS---GTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQE--PMTSLNpifpiGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGM 173
Cdd:PRK10535 78 DALAQLRREHFGFIFQRyhLLSHLT-----AAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEvSDRTIVMFRGDVV 248
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
340-553 |
2.28e-22 |
|
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: 101.32 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDP--FAsldp 417
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELR---ARMALVPQDPvlFA---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 418 rmsvgTAIMEPFIEHRLGTKQQAREKAADLLEKVGLspdmMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVI 486
Cdd:TIGR02204 428 -----ASVMENIRYGRPDATDEEVEAAARAAHAHEF----ISALPEGYdtylgergvtlSGGQRQRIAIARAILKDAPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 487 VADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGPRAAVF 553
Cdd:TIGR02204 499 LLDEATSALDAESEQLV--QQALETLMKGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-270 |
2.29e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 10 QTGGSVSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDK-KTSRIEGKVMLGGR 88
Cdd:PRK14243 2 STLNGTETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLiPGFRVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 89 DLLAlPEEEMRKVRgKDISMIFQEPmtslNPiFPigKQIAEALTVHQDISssAAKAEVIRLLEK-----VRIPNAKNRFD 163
Cdd:PRK14243 78 NLYA-PDVDPVEVR-RRIGMVFQKP----NP-FP--KSIYDNIAYGARIN--GYKGDMDELVERslrqaALWDEVKDKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 164 DYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEegMSVLFITHDMGVVAEVSDRTiVMF 243
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMT-AFF 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 549799341 244 RGDVVETG----------TTDDIFHRGRHPYTRALLS 270
Cdd:PRK14243 224 NVELTEGGgrygylvefdRTEKIFNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
314-565 |
3.31e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDirsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYevlKLD 393
Cdd:PRK13642 4 ILEVENLVFKYE--------KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDPFASLdprmsVGtAIMEPFIEHRLGTKQQAREKAADLLEKVGLSPDMM---RRFPHEFSGGQR 470
Cdd:PRK13642 73 AENVWNLRRKIGMVFQNPDNQF-----VG-ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLdfkTREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGPRA 550
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
250 260
....*....|....*....|...
gi 549799341 551 AVFDNPQH--------PYTKKLM 565
Cdd:PRK13642 226 ELFATSEDmveigldvPFSSNLM 248
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
40-259 |
4.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.74 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPE-EEMRKVRgKDISMIFQepmtsln 118
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKS----TIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQ------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 119 piFPIGKQIAEalTVHQDIS-------SSAAKAEVIRLlEKVRIPN-AKNRFDDYPHQFSGGMRQRVMIAMALASKPKLL 190
Cdd:PRK13649 93 --FPESQLFEE--TVLKDVAfgpqnfgVSQEEAEALAR-EKLALVGiSESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 191 IADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHR 259
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-257 |
4.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 15 VSPVLSVQNLTTSFRVDGGWKSVvRNMSFEIAPRETVAIVGESGSGKSVTSlsimRLLDKKTSRIEGKVMLGGRDLLAlp 94
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTA----RLIDGLFEEFEGKVKIDGELLTA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 eEEMRKVRGKdISMIFQEPMTSLnpifpIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMR 174
Cdd:PRK13642 74 -ENVWNLRRK-IGMVFQNPDNQF-----VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 175 QRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGTTD 254
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
...
gi 549799341 255 DIF 257
Cdd:PRK13642 226 ELF 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
316-538 |
6.10e-22 |
|
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: 94.52 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 316 SVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldkt 395
Cdd:cd03235 1 EVEDLTVSY-----------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 396 tlrtMRRSVQMIFQdpFASLDPRM------SVGTAIMePFIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQ 469
Cdd:cd03235 66 ----ERKRIGYVPQ--RRSIDRDFpisvrdVVLMGLY-GHKGLFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVM 538
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-256 |
6.82e-22 |
|
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: 99.49 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSF-RVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVmlgGRDLLALPE 95
Cdd:TIGR03269 278 PIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRV---GDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 E-EMRKVRGKD-ISMIFQEpmTSLNPIFPIGKQIAEALTVhqDISSSAAKAEVIRLLEKVRIPN--AKNRFDDYPHQFSG 171
Cdd:TIGR03269 355 PgPDGRGRAKRyIGILHQE--YDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLKMVGFDEekAEEILDKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*
gi 549799341 252 TTDDI 256
Cdd:TIGR03269 511 DPEEI 515
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
344-548 |
6.87e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 94.99 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQDpfasldprmsvgT 423
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRRAIGVVPQD------------T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 AIMEPFIEH--RLG----TKQQARE--KAADLLEKVglspdmmRRFPHEF-----------SGGQRQRIAIARSLMLDPK 484
Cdd:cd03253 85 VLFNDTIGYniRYGrpdaTDEEVIEaaKAAQIHDKI-------MRFPDGYdtivgerglklSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 485 VIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGP 548
Cdd:cd03253 158 ILLLDEATSALDTHTEREI--QAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-262 |
7.35e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTsrieGKVMLGGRDLLALPEEEMRKvrgkDI 106
Cdd:PRK13657 341 SFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS----GRILIDGTDIRTVTRASLRR----NI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 107 SMIFQEPMtslnpIFpiGKQIAEALTVHQdisSSAAKAEVIRLLEKVR----IPNAKNRFD----DYPHQFSGGMRQRVM 178
Cdd:PRK13657 412 AVVFQDAG-----LF--NRSIEDNIRVGR---PDATDEEMRAAAERAQahdfIERKPDGYDtvvgERGRQLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGTTDDIFH 258
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
....
gi 549799341 259 RGRH 262
Cdd:PRK13657 559 RGGR 562
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
40-257 |
7.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.05 E-value: 7.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLA-LPEEEMRKVRgKDISMIFQEPMTsln 118
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKS----TLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLR-KKVSLVFQFPEA--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 119 pifpigkQIAEAlTVHQDI---------SSSAAKAEVIRLLEKVRIPnaKNRFDDYPHQFSGGMRQRVMIAMALASKPKL 189
Cdd:PRK13641 97 -------QLFEN-TVLKDVefgpknfgfSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 190 LIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-546 |
8.10e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 8.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 15 VSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALP 94
Cdd:PRK09700 2 ATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSGIHEPTKGTITINNINYNKLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVrgkDISMIFQE-----PMTSLNPIFpIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQF 169
Cdd:PRK09700 74 HKLAAQL---GIGIIYQElsvidELTVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 250 TGTTDDIFHRGrhpytrallsaVPKLgsMKERLLPARFPiidiktgesqpvADVKDTVSGGRTPILSVKDLTTRFDIRsg 329
Cdd:PRK09700 226 SGMVSDVSNDD-----------IVRL--MVGRELQNRFN------------AMKENVSNLAHETVFEVRNVTSRDRKK-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 330 lfgrksgavhaVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldKTTLRTMRRSVQMIFQ 409
Cdd:PRK09700 279 -----------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVKKGMAYITE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 410 D-------PFASLDPRMSVGTAIMEPFIEHRLGTKQQAREK--AADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLM 480
Cdd:PRK09700 346 SrrdngffPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQrtAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLC 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 481 LDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEI 546
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-251 |
1.16e-21 |
|
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: 93.36 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSfrVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTsrIEGKVMLGGRDLLALPEEEm 98
Cdd:cd03217 1 LEIKDLHVS--VGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEV--TEGEILFKGEDITDLPPEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdISMIFQEPMtslnpifpigkqiaealtvhqDISSsaakaevIRLLEKVRIPNAKnrfddyphqFSGGMRQRVM 178
Cdd:cd03217 74 RARLG--IFLAFQYPP---------------------EIPG-------VKNADFLRYVNEG---------FSGGEKKRNE 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEV-SDRTIVMFRGDVVETG 251
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
313-497 |
1.22e-21 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 93.31 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDIRSgLFgrksgavhavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKL 392
Cdd:COG4133 1 MMLEAENLSCRRGERL-LF----------SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DkttlRTMRRSVQMIFQDPfaSLDPRMSVgtaimepfIEH-----RLGTKQQAREKAADLLEKVGLSPdMMRRFPHEFSG 467
Cdd:COG4133 70 R----EDYRRRLAYLGHAD--GLKPELTV--------RENlrfwaALYGLRADREAIDEALEAVGLAG-LADLPVRQLSA 134
|
170 180 190
....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
340-557 |
1.30e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLdGYEVLKLDK--TTLRTMRRSVQMIFQDPFASLdp 417
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKknKKLKPLRKKVGIVFQFPEHQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 418 rmsvgtaiMEPFIEHRLG--------TKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVAD 489
Cdd:PRK13634 99 --------FEETVEKDICfgpmnfgvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 490 EAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
311-524 |
1.85e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 311 RTPILSVKDLttrfdirsglfGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVL 390
Cdd:PRK10247 4 NSPLLQLQNV-----------GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLDKttlRTMRRSVQMIFQDPfasldprMSVGTAIMEPFIEHRLGTKQQAREKA-ADLLEKVGLSPDMMRRFPHEFSGGQ 469
Cdd:PRK10247 73 TLKP---EIYRQQVSYCAQTP-------TLFGDTVYDNLIFPWQIRNQQPDPAIfLDDLERFALPDTILTKNIAELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHD 524
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-245 |
1.86e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.11 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTtsfrvdggWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEE 96
Cdd:cd03215 3 PVLEVRGLS--------VKGAVRDVSFEVRAGEIVGIAGLVGNGQT----ELAEALFGLRPPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKvrgKDISMIFQEPM-TSLNPIFPIgkqiaealtvhqdisssaakAEVIRLlekvripnaknrfddyPHQFSGGMRQ 175
Cdd:cd03215 71 DAIR---AGIAYVPEDRKrEGLVLDLSV--------------------AENIAL----------------SSLLSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVtiqGQILDLIKTLQE--EEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDV---GAKAEIYRLIRElaDAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
336-557 |
2.11e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 96.25 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQD----P 411
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAERGVGMVFQSyalyP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 FASLDPRMSVG---TAIMEPFIEHRLgtkqqarEKAADLLEKVGLspdmMRRFPHEFSGGQRQRIAIARSLMLDPKVIVA 488
Cdd:PRK11000 89 HLSVAENMSFGlklAGAKKEEINQRV-------NQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 489 DEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ 557
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-242 |
2.33e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 97.74 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRvdGGWKsVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPE 95
Cdd:TIGR02857 319 ASSLEFSGVSVAYP--GRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT----EGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 eemrKVRGKDISMIFQEPMtslnpIFPigKQIAEALTVHQDISSSAAKAEVIRL-----LEKVRIPNAKNRFDDYPHQFS 170
Cdd:TIGR02857 392 ----DSWRDQIAWVPQHPF-----LFA--GTIAENIRLARPDASDAEIREALERagldeFVAALPQGLDTPIGEGGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMgVVAEVSDRTIVM 242
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
312-556 |
3.73e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:PRK11300 3 QPLLSVSGLMMRF-----------GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LdkTTLRTMRRSVQMIFQDpfASLDPRMSVGTAIMepFIEHR----------LGTK------QQAREKAADLLEKVGLSp 455
Cdd:PRK11300 72 L--PGHQIARMGVVRTFQH--VRLFREMTVIENLL--VAQHQqlktglfsglLKTPafrraeSEALDRAATWLERVGLL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 456 DMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRV 535
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 549799341 536 AVMYLGEIVEIGPRAAVFDNP 556
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
340-595 |
3.73e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV---LKLDKTtLRTMRRSVQMIFQDPFASLD 416
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKE-VKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 417 PRMSVGTAIMEPFieHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK13645 105 QETIEKDIAFGPV--NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 497 VSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNpqhpytKKLMSAVPVPDPARR 576
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKIEIDPPKLY 256
|
250 260
....*....|....*....|..
gi 549799341 577 QIK---RNMATDEIRSPIRPVD 595
Cdd:PRK13645 257 QLMyklKNKGIDLLNKNIRTIE 278
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-548 |
4.43e-21 |
|
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: 92.17 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDkttLRTMRRSVQMIFQDPF------- 412
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 ASLDprmsvgtaimePFIEHRLGTKQQAREKAAdLLEKVGLSPDMMrRFPHE-----FSGGQRQRIAIARSLMLDPKVIV 487
Cdd:cd03244 96 SNLD-----------PFGEYSDEELWQALERVG-LKEFVESLPGGL-DTVVEeggenLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 488 ADEAVSALDVSIKAQVcnllldlQQNLNLAF-----LFISHdmavveRV-----SHRVAVMYLGEIVEIGP 548
Cdd:cd03244 163 LDEATASVDPETDALI-------QKTIREAFkdctvLTIAH------RLdtiidSDRILVLDKGRVVEFDS 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-259 |
6.30e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.00 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRV----DGGWKSV-------------VRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrie 80
Cdd:COG4586 1 IIEVENLSKTYRVyekePGLKGALkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTGILVPTS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 81 GKVMLGGRDllalPEEEMRKVRgKDISMIF-QEpmTSLNPIFPIgkqiAEALTVHQ---DISSSAAK---AEVIRLLE-- 151
Cdd:COG4586 77 GEVRVLGYV----PFKRRKEFA-RRIGVVFgQR--SQLWWDLPA----IDSFRLLKaiyRIPDAEYKkrlDELVELLDlg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 152 -----KVRipnaknrfddyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFIT 226
Cdd:COG4586 146 elldtPVR-------------QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTS 212
|
250 260 270
....*....|....*....|....*....|...
gi 549799341 227 HDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHR 259
Cdd:COG4586 213 HDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-247 |
7.88e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.43 E-value: 7.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTsrieGKVMLGGRDLLALPEEEM 98
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLAGLETPS----AGELLAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RkvrgkdisMIFQEpmTSLNPIFPIGKQIAEALTVHQdisssaaKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGMRQRVM 178
Cdd:PRK11247 84 R--------LMFQD--ARLLPWKKVIDNVGLGLKGQW-------RDAALQALAAVGL---ADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDV 247
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
340-547 |
8.71e-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: 96.73 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDPFasldprM 419
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR---QFINYLPQEPY------I 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTAIMEPFIEHRLGTKQQAREKAADLLEkvglSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVA 488
Cdd:TIGR01193 560 FSGSILENLLLGAKENVSQDEIWAACEIAE----IKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 489 DEAVSALDVSIKAQVcnlLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIG 547
Cdd:TIGR01193 636 DESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-260 |
1.25e-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: 91.14 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKS-VTSLsIMRLLDKKtsriEGKVMLGGRDLLALPEEE 97
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKStLVNL-IPRFYDVD----SGRILIDGHDVRDYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRkvrgKDISMIFQEPMtslnpIFpigkqiaeALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQF-------- 169
Cdd:cd03251 74 LR----RQIGLVSQDVF-----LF--------NDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYdtvigerg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 ---SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVaEVSDRTIVMFRGD 246
Cdd:cd03251 137 vklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTI-ENADRIVVLEDGK 213
|
250
....*....|....
gi 549799341 247 VVETGTTDDIFHRG 260
Cdd:cd03251 214 IVERGTHEELLAQG 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
341-558 |
1.37e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.99 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldktTLRTMRRSVqmIFQDpfASLDPRMS 420
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI------TEPGPDRMV--VFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 V--GTAIMEPFIEHRLGTKQQaREKAADLLEKVGLSPDMMRRfPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS 498
Cdd:TIGR01184 71 VreNIALAVDRVLPDLSKSER-RAIVEEHIALVGLTEAADKR-PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 499 IKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVM------YLGEIVEIG-----PRAAVFDNPQH 558
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPfprprDRLEVVEDPSY 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-251 |
1.39e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 90.73 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEMRKvrgkDI 106
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS-TLLKLLAGLYKPTS---GSVLLDGTDIRQLDPADLRR----NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 107 SMIFQEPMtslnpIFpigkqiaeALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQF-----------SGGMRQ 175
Cdd:cd03245 81 GYVPQDVT-----LF--------YGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEgmSVLFITHDMGVVAEVsDRTIVMFRGDVVETG 251
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
310-552 |
1.75e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 310 GRTPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV 389
Cdd:COG3845 1 MMPPALELRGITKRF-----------GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 390 lkldktTLRT----MRRSVQMIFQDPfaSLDPRMSV------GtaiMEPFIEHRLGTKQqAREKAADLLEKVGLSPDMMR 459
Cdd:COG3845 70 ------RIRSprdaIALGIGMVHQHF--MLVPNLTVaenivlG---LEPTKGGRLDRKA-ARARIRELSERYGLDVDPDA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 460 RfPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL---------DV--SIKAQVCnllldlqqnlnlAFLFISHDMAVV 528
Cdd:COG3845 138 K-VEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqeadelfEIlrRLAAEGK------------SIIFITHKLREV 204
|
250 260
....*....|....*....|....
gi 549799341 529 ERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:COG3845 205 MAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
344-543 |
1.91e-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: 90.61 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKttlRTMRRSVQMIFQDP--FA-SLDPRMS 420
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH---KYLHSKVSLVGQEPvlFArSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTA------IMEP--------FI-EHRLGTKQQAREKAADLlekvglspdmmrrfphefSGGQRQRIAIARSLMLDPKV 485
Cdd:cd03248 110 YGLQscsfecVKEAaqkahahsFIsELASGYDTEVGEKGSQL------------------SGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 486 IVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEI 543
Cdd:cd03248 172 LILDEATSALDAESEQQV--QQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
38-282 |
1.92e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPE-EEMRKVRGkdisMIFQEPMTS 116
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ----KGKVLVSGIDTGDFSKlQGIRKLVG----IVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 LnpifpIGKQIAEALTVHQD---ISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPKLLIAD 193
Cdd:PRK13644 90 F-----VGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 194 EPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVaEVSDRTIVMFRGDVVETGTTDDIFhrgRHPYTRALLSAVP 273
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVL---SDVSLQTLGLTPP 236
|
....*....
gi 549799341 274 KLGSMKERL 282
Cdd:PRK13644 237 SLIELAENL 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-272 |
3.20e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.53 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIM-RLLDKKtsriEGKVMLGGRDLLALPEEEM 98
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD----SGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVrgkdISMIFQEPMTSLNpifpigkqiaeaLTVHQDIS-----------SSAAKAEVIRLLEKVRIPNAKNRFDDyph 167
Cdd:COG4604 74 AKR----LAILRQENHINSR------------LTVRELVAfgrfpyskgrlTAEDREIIDEAIAYLDLEDLADRYLD--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDV 247
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
250 260
....*....|....*....|....*
gi 549799341 248 VETGTTDDIFhrgrhpyTRALLSAV 272
Cdd:COG4604 215 VAQGTPEEII-------TPEVLSDI 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
38-282 |
4.13e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.68 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 38 VRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdKKTSrieGKVMLGGRDLlALPEEEMRKVRgKDISMIFQEPMtsl 117
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL-KPSS---GRILFDGKPI-DYSRKGLMKLR-ESVGMVFQDPD--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 118 NPIFpigkqiaeALTVHQDISSSA---------AKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPK 188
Cdd:PRK13636 93 NQLF--------SASVYQDVSFGAvnlklpedeVRKRVDNALKRTGIEHLKDK---PTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFhrGRHPYTRAL 268
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF--AEKEMLRKV 239
|
250
....*....|....
gi 549799341 269 LSAVPKLGSMKERL 282
Cdd:PRK13636 240 NLRLPRIGHLMEIL 253
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
35-260 |
5.12e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 5.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLlalPEEEMRKVRGKdISMIFQEPM 114
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQ-VALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 tslnpIF--PIGKQIAEALTVHQD--ISSSAAKAEVIRLLEKvrIPNAKN-RFDDYPHQFSGGMRQRVMIAMALASKPKL 189
Cdd:TIGR00958 566 -----LFsgSVRENIAYGLTDTPDeeIMAAAKAANAHDFIME--FPNGYDtEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 190 LIADEPTTALDVTIQgqilDLIKTLQEEEGMSVLFITHDMGVVaEVSDRTIVMFRGDVVETGTTDDIFHRG 260
Cdd:TIGR00958 639 LILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
40-257 |
5.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTsrieGKVMLGGrdlLALPE-----EEMRKVRgKDISMIFQEPM 114
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISET----GQTIVGD---YAIPAnlkkiKEVKRLR-KEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 TSLnpiF--PIGKQIAEAlTVHQDISSSAAKAEVIRLLEKVRIPnaknrfDDY----PHQFSGGMRQRVMIAMALASKPK 188
Cdd:PRK13645 101 YQL---FqeTIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLP------EDYvkrsPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIF 257
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-245 |
7.88e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 33 GWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEMRKVRgKDISMIFQE 112
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERPSA---GKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 113 PMTSL------NPIFPIGKQIAEALTVHQDISSSAAKaevIRLLEKvripnAKNrfddYPHQFSGGMRQRVMIAMALASK 186
Cdd:PRK10908 88 HHLLMdrtvydNVAIPLIIAGASGDDIRRRVSAALDK---VGLLDK-----AKN----FPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 187 PKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-251 |
1.01e-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: 86.98 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALpEEEM 98
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPVSDL-EKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVrgkdISMIFQEPMtslnpIFpigkqiaeALTVHQDISSsaakaevirllekvripnaknrfddyphQFSGGMRQRVM 178
Cdd:cd03247 74 SSL----ISVLNQRPY-----LF--------DTTLRNNLGR----------------------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTIQGQILDLIktLQEEEGMSVLFITHDMGVVAEVsDRTIVMFRGDVVETG 251
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
344-568 |
1.28e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.53 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkTTLRTMRRSVQMIFQDpfASLDPRMSVGT 423
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHARDRKVGFVFQH--YALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 AI-----MEPfiEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS 498
Cdd:PRK10851 94 NIafgltVLP--RRERPNAAAIKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 499 IKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQHPYTKKLMSAV 568
Cdd:PRK10851 171 VRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
338-544 |
1.31e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 87.65 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 338 VHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLrtmRRSVQMIFQDP---FAS 414
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVtlfYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 415 LDPRMSVGtaimEPFIEhrlgtkQQAREKAADLLekvGLSpDMMRRFPHEF-----------SGGQRQRIAIARSLMLDP 483
Cdd:cd03245 94 LRDNITLG----APLAD------DERILRAAELA---GVT-DFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 484 KVIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVShRVAVMYLGEIV 544
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERL--KERLRQLLGDKTLIIITHRPSLLDLVD-RIIVMDSGRIV 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-252 |
1.35e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 87.47 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDggWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKktsrIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03369 7 IEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA----EEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RkvrgKDISMIFQEPM----TSLNPIFPIGK----QIAEALTVHQDISSsaakaevirllekvripnaknrfddyphqFS 170
Cdd:cd03369 81 R----SSLTIIPQDPTlfsgTIRSNLDPFDEysdeEIYGALRVSEGGLN-----------------------------LS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTlqEEEGMSVLFITHDMGVVAEVsDRTIVMFRGDVVET 250
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
..
gi 549799341 251 GT 252
Cdd:cd03369 205 DH 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
337-553 |
1.48e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 337 AVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTT-LRTMRRSVQMIFQDPFASL 415
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAIMEPfieHRLG-TKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK13643 98 FEETVLKDVAFGP---QNFGiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 495 LDVSIKAQVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVF 553
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-259 |
1.57e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRV------------------DGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMrlldkktS 77
Cdd:COG1134 2 SSMIEVENVSKSYRLyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLI-------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 78 RI----EGKVmlggrdllalpeeemrKVRGKDISMIfqEPMTSLNPifpigkqiaeALTVHQDISSSAA-----KAEVIR 148
Cdd:COG1134 74 GIleptSGRV----------------EVNGRVSALL--ELGAGFHP----------ELTGRENIYLNGRllglsRKEIDE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 149 LLEKVR----IpnakNRFDDYP-HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVL 223
Cdd:COG1134 126 KFDEIVefaeL----GDFIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVI 200
|
250 260 270
....*....|....*....|....*....|....*.
gi 549799341 224 FITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHR 259
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
42-253 |
2.12e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.22 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 42 SFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEmrkvrgKDISMIFQEpmtslNPIF 121
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS----TLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQE-----NNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 122 PigkqiaeALTVHQDISSSAAKAEVIRLLEKVRIPNAKNR--FDDY----PHQFSGGMRQRVMIAMALASKPKLLIADEP 195
Cdd:TIGR01277 83 A-------HLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQvgIADYldrlPEQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 196 TTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTT 253
Cdd:TIGR01277 156 FSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
345-556 |
2.35e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.48 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 345 SFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQmifQDPfasldprMSVGTA 424
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVG---QEP-------VLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 425 IMEPfIEHRLGTKQQAREKAAdllEKVGLSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVADEAVS 493
Cdd:TIGR00958 571 VREN-IAYGLTDTPDEEIMAA---AKAANAHDFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 494 ALDVSIKAQVcnllLDLQQNLNLAFLFISHDMAVVERvSHRVAVMYLGEIVEIGPRAAVFDNP 556
Cdd:TIGR00958 647 ALDAECEQLL----QESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
335-556 |
2.65e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 335 SGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQDPfas 414
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 415 ldprmsvGTAIMEPFIEH-------RLGTKQQARE-KAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVI 486
Cdd:PRK13652 88 -------DDQIFSPTVEQdiafgpiNLGLDEETVAhRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 487 VADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNP 556
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-252 |
3.03e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRllDKKTSRIEGKVMLGGRDLLALPEEEm 98
Cdd:COG0396 1 LEIKNLH--VSVEG--KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKYEVTSGSILLDGEDILELSPDE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdISMIFQEPM------------TSLNpifpigkQIAEaltvhQDISSSAAKAEVIRLLEKVRIPnaknrfDDYP 166
Cdd:COG0396 74 RARAG--IFLAFQYPVeipgvsvsnflrTALN-------ARRG-----EELSAREFLKLLKEKMKELGLD------EDFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 167 HQ-----FSGGMRQRVMIAMALASKPKLLIADEPTTALDVtiqgqilDLIKTLQE------EEGMSVLFITHDMGVVAEV 235
Cdd:COG0396 134 DRyvnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI-------DALRIVAEgvnklrSPDRGILIITHYQRILDYI 206
|
250
....*....|....*...
gi 549799341 236 S-DRTIVMFRGDVVETGT 252
Cdd:COG0396 207 KpDFVHVLVDGRIVKSGG 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
170-402 |
3.99e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.72 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEE-EGMSVLFITHDMGVvAEVSDRTIVMFRGDVV 248
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErPGMSVLVATAYMEE-AERFDWLVAMDAGRVL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 249 ETGTTDDIFHRgrhpyTRAllsavPKLGSMKERLLPARfpiidiKTGESQPVADVKDTVSGGRTPILSVKDLTTRFdirs 328
Cdd:NF033858 217 ATGTPAELLAR-----TGA-----DTLEAAFIALLPEE------KRRGHQPVVIPPRPADDDDEPAIEARGLTMRF---- 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 329 glfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRR 402
Cdd:NF033858 277 -------GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATRRR 340
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
328-543 |
4.48e-19 |
|
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: 84.96 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 328 SGLFGRKSGAVHAV-EKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQM 406
Cdd:cd03246 4 ENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG---DHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 407 IFQDpfasldprmsvgtaimepfIEHRLGTkqqarekaadLLEKVglspdmmrrfpheFSGGQRQRIAIARSLMLDPKVI 486
Cdd:cd03246 81 LPQD-------------------DELFSGS----------IAENI-------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 487 VADEAVSALDVSIKAQVCNLLLDLQQNLNLAfLFISHDMAVVERVShRVAVMYLGEI 543
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATR-IVIAHRPETLASAD-RILVLEDGRV 173
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
296-548 |
5.46e-19 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 91.17 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 296 ESQPVADVKDTVSGGRTPilsVKDLTTRFDIRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLI 375
Cdd:TIGR03797 427 RAKPILEALPEVDEAKTD---PGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 376 EPTSGDVMLDGYEVLKLDKttlRTMRRSVQMIFQDPfasldpRMSVGTaIMEPFIEHRLGTKQQAREKAadllEKVGLSP 455
Cdd:TIGR03797 504 TPESGSVFYDGQDLAGLDV---QAVRRQLGVVLQNG------RLMSGS-IFENIAGGAPLTLDEAWEAA----RMAGLAE 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 456 DMmRRFP---H--------EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLnlafLFISHD 524
Cdd:TIGR03797 570 DI-RAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR----IVIAHR 644
|
250 260
....*....|....*....|....
gi 549799341 525 MAVVeRVSHRVAVMYLGEIVEIGP 548
Cdd:TIGR03797 645 LSTI-RNADRIYVLDAGRVVQQGT 667
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
310-557 |
5.54e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 310 GRTPILSVKDLTtrfdirsglFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMldgYEV 389
Cdd:PRK13648 3 DKNSIIVFKNVS---------FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF---YNN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 390 LKLDKTTLRTMRRSVQMIFQDPfasldPRMSVGTAIMEPF---IEHRLGTKQQAREKAADLLEKVglspDMMRRF---PH 463
Cdd:PRK13648 71 QAITDDNFEKLRKHIGIVFQNP-----DNQFVGSIVKYDVafgLENHAVPYDEMHRRVSEALKQV----DMLERAdyePN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHrVAVMYLGEI 543
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTV 220
|
250
....*....|....
gi 549799341 544 VEIGPRAAVFDNPQ 557
Cdd:PRK13648 221 YKEGTPTEIFDHAE 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
340-496 |
6.05e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEvlkLDKTTLRTMRRSVQMI------FQDPFA 413
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQVALVsqnvhlFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 414 SldprmSVGTAIMEPFiehrlgTKQQArEKAAdlleKVGLSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLD 482
Cdd:PRK11176 435 N-----NIAYARTEQY------SREQI-EEAA----RMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRD 498
|
170
....*....|....
gi 549799341 483 PKVIVADEAVSALD 496
Cdd:PRK11176 499 SPILILDEATSALD 512
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-543 |
9.42e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRvdgGWKSVvRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDL-LALP 94
Cdd:PRK10762 2 QALLQLKGIDKAFP---GVKAL-SGAALNVYPGRVMALVGENGAGKS----TMMKVLTGIYTRDAGSILYLGKEVtFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 eeemRKVRGKDISMIFQEpmtsLNPIFPIgkQIAEALTVHQDISSSAAK-------AEVIRLLEKVRIPNAknrfddyPH 167
Cdd:PRK10762 74 ----KSSQEAGIGIIHQE----LNLIPQL--TIAENIFLGREFVNRFGRidwkkmyAEADKLLARLNLRFS-------SD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSG----GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEeGMSVLFITHDMGVVAEVSDRTIVM- 242
Cdd:PRK10762 137 KLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFr 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 243 ---FRGD-VVETGTTDDIFHRgrhpytrallsavpklgsMKERLLPARFPIIDIKTGESQpvadvkdtvsggrtpiLSVK 318
Cdd:PRK10762 216 dgqFIAErEVADLTEDSLIEM------------------MVGRKLEDQYPRLDKAPGEVR----------------LKVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 319 DLttrfdirsglfgrkSGAvhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLklDKTTLR 398
Cdd:PRK10762 262 NL--------------SGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--TRSPQD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 399 TMRRSVQMIFQDPFA-------SLDPRMSVgTAImePFIEHRLGTKQQAREKAA--DLLEKVGLSPDMMRRFPHEFSGGQ 469
Cdd:PRK10762 324 GLANGIVYISEDRKRdglvlgmSVKENMSL-TAL--RYFSRAGGSLKHADEQQAvsDFIRLFNIKTPSMEQAIGLLSGGN 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMYLGEI 543
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL-VSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
317-496 |
9.60e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 317 VKDLTTRFDIRSGLfgrksgAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDV-----------MLD 385
Cdd:PRK13651 5 VKNIVKIFNKKLPT------ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 386 GYEVLKLD----KTTLRT------MRRSVQMIFQdpFASLDprmsvgtaIMEPFIEH-------RLGT-KQQAREKAADL 447
Cdd:PRK13651 79 EKEKVLEKlviqKTRFKKikkikeIRRRVGVVFQ--FAEYQ--------LFEQTIEKdiifgpvSMGVsKEEAKKRAAKY 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 549799341 448 LEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK13651 149 IELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
314-557 |
1.01e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTtrfdirsglFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGD---VMLDGyevL 390
Cdd:PRK13640 5 IVEFKHVS---------FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG---I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 391 KLDKTTLRTMRRSVQMIFQDPfaslDPRMsVGTAIMEPF---IEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSG 467
Cdd:PRK13640 73 TLTAKTVWDIREKVGIVFQNP----DNQF-VGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVErVSHRVAVMYLGEIVEIG 547
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQG 225
|
250
....*....|
gi 549799341 548 PRAAVFDNPQ 557
Cdd:PRK13640 226 SPVEIFSKVE 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
296-537 |
1.04e-18 |
|
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: 89.65 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 296 ESQPVADVKDTVSGGRTPILSVKDLTTRFdirSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLI 375
Cdd:TIGR02857 296 ALFAVLDAAPRPLAGKAPVTAAPASSLEF---SGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 376 EPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDPFasldprMSVGTaIMEpfiEHRLGTKQQAREKAADLLEKVGLS- 454
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWR---DQIAWVPQHPF------LFAGT-IAE---NIRLARPDASDAEIREALERAGLDe 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 455 -----PDMMRRF----PHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDM 525
Cdd:TIGR02857 440 fvaalPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV--LEALRALAQGRTVLLVTHRL 517
|
250
....*....|..
gi 549799341 526 AVVERVSHRVAV 537
Cdd:TIGR02857 518 ALAALADRIVVL 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-257 |
1.13e-18 |
|
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: 85.29 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPeeeM 98
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKT-TTFYMIVGLVKPDS---GKILLDGQDITKLP---M 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEPmtslnPIFpigkqiaEALTVHQDISssaAKAEVIRLLEKVRIPNAKNRFDDYP-----HQF---- 169
Cdd:cd03218 70 HKRARLGIGYLPQEA-----SIF-------RKLTVEENIL---AVLEIRGLSKKEREEKLEELLEEFHithlrKSKassl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVE 249
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
|
....*...
gi 549799341 250 TGTTDDIF 257
Cdd:cd03218 214 EGTPEEIA 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-247 |
1.19e-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: 85.22 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 13 GSVSP-----VLSVQNLTTSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGG 87
Cdd:cd03248 1 GSLAPdhlkgIVKFQNVTFAYPTRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 88 RDLLALPEEEMRKVrgkdISMIFQEPMTSlnpifpigkqiaeALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPH 167
Cdd:cd03248 76 KPISQYEHKYLHSK----VSLVGQEPVLF-------------ARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELAS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 -----------QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKtlQEEEGMSVLFITHDMGVVaEVS 236
Cdd:cd03248 139 gydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTV-ERA 215
|
250
....*....|.
gi 549799341 237 DRTIVMFRGDV 247
Cdd:cd03248 216 DQILVLDGGRI 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
314-553 |
1.41e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFdirsglfgrkSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKLD 393
Cdd:PRK13636 5 ILKVEELNYNY----------SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-KPIDYS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDP-----FASLDPRMSVGTAIMEPfiehrlgTKQQAREKAADLLEKVGLSPdmMRRFP-HEFSG 467
Cdd:PRK13636 74 RKGLMKLRESVGMVFQDPdnqlfSASVYQDVSFGAVNLKL-------PEDEVRKRVDNALKRTGIEH--LKDKPtHCLSF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 468 GQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
....*.
gi 549799341 548 PRAAVF 553
Cdd:PRK13636 225 NPKEVF 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-251 |
1.50e-18 |
|
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: 85.08 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 21 VQNLTTSFRV---DGGWKS--------------VVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKV 83
Cdd:cd03267 3 VSNLSKSYRVyskEPGLIGslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKT-TTLKILSGLLQPTS---GEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 84 MLGGRdllaLPEEEMRKVRgKDISMIFQEpMTSLNPIFPIgkqiAEALTVHQDI---SSSAAKAEVIRLLEKVRIpnakN 160
Cdd:cd03267 79 RVAGL----VPWKRRKKFL-RRIGVVFGQ-KTQLWWDLPV----IDSFYLLAAIydlPPARFKKRLDELSELLDL----E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 161 RFDDYP-HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRT 239
Cdd:cd03267 145 ELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRV 224
|
250
....*....|..
gi 549799341 240 IVMFRGDVVETG 251
Cdd:cd03267 225 LVIDKGRLLYDG 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-256 |
2.29e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.04 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 14 SVSPVLSVQNLTTSFrvdGGWKSVvRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLAL 93
Cdd:PRK11300 1 MSQPLLSVSGLMMRF---GGLLAV-NNVNLEVREQEIVSLIGPNGAGKT-TVFNCLTGFYKPTG---GTILLRGQHIEGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 PEEEM-RK--VRGKDISMIFQEpMTSLnpifpigkqiaEALTV--HQDISSS------------AAKAEVIRL----LEK 152
Cdd:PRK11300 73 PGHQIaRMgvVRTFQHVRLFRE-MTVI-----------ENLLVaqHQQLKTGlfsgllktpafrRAESEALDRaatwLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 153 VRIPNAKNRFDD---YPHQfsggmrQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDM 229
Cdd:PRK11300 141 VGLLEHANRQAGnlaYGQQ------RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDM 214
|
250 260
....*....|....*....|....*..
gi 549799341 230 GVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK11300 215 KLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-260 |
2.90e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRI--EGKVM-LGGRDLLALPEEemrkvrgkdISMIFQEP 113
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLdYSKRGLLALRQQ---------VATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 114 MTSlnpIF--PIGKQIAEALTvhqdiSSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQ-FSGGMRQRVMIAMALASKPKLL 190
Cdd:PRK13638 87 EQQ---IFytDIDSDIAFSLR-----NLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 191 IADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRG 260
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-268 |
3.03e-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: 88.23 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEM 98
Cdd:TIGR02203 331 VEFRNVTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvrgkDISMIFQEPMTSLNPIFpigKQIAEALTvhqdisSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQ--------FS 170
Cdd:TIGR02203 405 RR----QVALVSQDVVLFNDTIA---NNIAYGRT------EQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeeEGMSVLFITHDMGVVaEVSDRTIVMFRGDVVET 250
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTI-EKADRIVVMDDGRIVER 548
|
250
....*....|....*....
gi 549799341 251 GTTDDIF-HRGRHPYTRAL 268
Cdd:TIGR02203 549 GTHNELLaRNGLYAQLHNM 567
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
315-547 |
4.01e-18 |
|
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: 82.36 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTtrfdirsglFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:cd03247 1 LSINNVS---------FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttlrTMRRSVQMIFQDPFAsldprmsvgtaimepFiehrlgtkqqarekAADLLEKVGlspdmmRRfpheFSGGQRQRIA 474
Cdd:cd03247 72 ----ALSSLISVLNQRPYL---------------F--------------DTTLRNNLG------RR----FSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVShRVAVMYLGEIVEIG 547
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQL--LSLIFEVLKDKTLIWITHHLTGIEHMD-KILFLENGKIIMQG 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-248 |
5.89e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 82.21 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVD--GGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSR--IEGKVMLGGRDLlal 93
Cdd:cd03213 3 TLSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS----TLLNALAGRRTGlgVSGEVLINGRPL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 PEEEMRKVrgkdISMIFQEPMTSLNpifpigkqiaeaLTVHQDISSSAAkaevIRLLekvripnaknrfddyphqfSGGM 173
Cdd:cd03213 76 DKRSFRKI----IGYVPQDDILHPT------------LTVRETLMFAAK----LRGL-------------------SGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDvtiQGQILDLIKTLQE--EEGMSVLFITHD-MGVVAEVSDRTIVMFRGDVV 248
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLD---SSSALQVMSLLRRlaDTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
312-554 |
6.87e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 6.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFDIRSGLFGR-----------KSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSG 380
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSlkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 381 DVMLDGyevlkldkttlrtmrRSVQMIfqDPFASLDPRMS-------VGTAimepfiehrLG-TKQQAREKAADLLEKVG 452
Cdd:COG1134 82 RVEVNG---------------RVSALL--ELGAGFHPELTgreniylNGRL---------LGlSRKEIDEKFDEIVEFAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 453 LSP--DM-MRRfpheFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQvCNLLLDLQQNLNLAFLFISHDMAVVE 529
Cdd:COG1134 136 LGDfiDQpVKT----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK-CLARIRELRESGRTVIFVSHSMGAVR 210
|
250 260
....*....|....*....|....*
gi 549799341 530 RVSHRVAVMYLGEIVEIGPRAAVFD 554
Cdd:COG1134 211 RLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
315-547 |
1.13e-17 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 81.86 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfGRKsgavHAVEKVSFDLAEGeTLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldk 394
Cdd:cd03264 1 LQLENLTKRY-------GKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 tTLRTMRRSVQMIFQDPfaSLDPRMSVgtaimEPFIEH--RLG--TKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQR 470
Cdd:cd03264 66 -QPQKLRRRIGYLPQEF--GVYPNFTV-----REFLDYiaWLKgiPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALD-----------VSIKAQVCnllldlqqnlnlaFLFISHDMAVVERVSHRVAVMY 539
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLDpeerirfrnllSELGEDRI-------------VILSTHIVEDVESLCNQVAVLN 203
|
....*...
gi 549799341 540 LGEIVEIG 547
Cdd:cd03264 204 KGKLVFEG 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
40-282 |
1.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 40 NMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGgrDLLALP---EEEMRKVRgKDISMIFQEPMTS 116
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKS----TLLQHLNGLLQPTEGKVTVG--DIVVSStskQKEIKPVR-KKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 LNPIfPIGKQIAEAltvHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPT 196
Cdd:PRK13643 97 LFEE-TVLKDVAFG---PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 197 TALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHrgRHPYTRALLSAVPKLG 276
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ--EVDFLKAHELGVPKAT 249
|
....*.
gi 549799341 277 SMKERL 282
Cdd:PRK13643 250 HFADQL 255
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-227 |
1.34e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRvDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSRI----EGKVML-GGRDLLAL 93
Cdd:COG4178 363 LALEDLTLRTP-DG--RPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRAI----AGLwpygSGRIARpAGARVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 PeeemrkvrgkdismifQEPMtslnpiFPIGKqIAEALT---VHQDISSsaakAEVIRLLEKVRIPNAKNRFD---DYPH 167
Cdd:COG4178 432 P----------------QRPY------LPLGT-LREALLypaTAEAFSD----AELREALEAVGLGHLAERLDeeaDWDQ 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKtlQEEEGMSVLFITH 227
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-256 |
1.36e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEE 96
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKT----TLLRAINGTLTPTAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMrkvrGKDISMIFQEpmTSLNPIFPIGKQIAEALTVHQ---DISSSAAKAEVIRLLEKVRIpnakNRFDDYP-HQFSGG 172
Cdd:PRK09536 74 AA----SRRVASVPQD--TSLSFEFDVRQVVEMGRTPHRsrfDTWTETDRAAVERAMERTGV----AQFADRPvTSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
....
gi 549799341 253 TDDI 256
Cdd:PRK09536 223 PADV 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-228 |
1.46e-17 |
|
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: 85.88 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 11 TGGSVSPVLSVQNLttSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDL 90
Cdd:TIGR02868 327 AVGLGKPTLELRDL--SAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL----QGEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 91 LALPEEEMRKVrgkdISMIFQEPMtslnpIFpigkqiaeALTVHQDI---SSSAAKAEVIRLLEKVRIPNAKNRFDDYPH 167
Cdd:TIGR02868 400 SSLDQDEVRRR----VSVCAQDAH-----LF--------DTTVRENLrlaRPDATDEELWAALERVGLADWLRALPDGLD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 168 --------QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIktLQEEEGMSVLFITHD 228
Cdd:TIGR02868 463 tvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-259 |
1.52e-17 |
|
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: 85.96 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLD---KKTSrieGKVMLGGRDLLALPE 95
Cdd:COG4618 331 LSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKS----TLARLLVgvwPPTA---GSVRLDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEmrkvRGKDISMIFQEPmtSLnpiFPIgkqiaealTVHQDIS----------SSAAKA----EVIrllekVRIPNAKN- 160
Cdd:COG4618 402 EE----LGRHIGYLPQDV--EL---FDG--------TIAENIArfgdadpekvVAAAKLagvhEMI-----LRLPDGYDt 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 161 RFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVtiQGQiLDLIKTLQE--EEGMSVLFITHDMGVVAEVsDR 238
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD--EGE-AALAAAIRAlkARGATVVVITHRPSLLAAV-DK 535
|
250 260
....*....|....*....|.
gi 549799341 239 TIVMFRGDVVETGTTDDIFHR 259
Cdd:COG4618 536 LLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-256 |
2.15e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 33 GWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMrkvrGKDISMIFQE 112
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV----ARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 113 PMTSLNpiFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIA 192
Cdd:PRK10253 90 ATTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 193 DEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
336-552 |
2.90e-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: 81.42 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdKTTLRTmRRSV------QMIFq 409
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL-PPHERA-RAGIayvpqgREIF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 410 dpfasldPRMSVGTAIMepfiehrLGTKQQAREKAADLLEKVGLSP---DMMRRFPHEFSGGQRQRIAIARSLMLDPKVI 486
Cdd:TIGR03410 88 -------PRLTVEENLL-------TGLAALPRRSRKIPDEIYELFPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 487 VADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-256 |
3.22e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLL--DkktsriEGKVMLGGRDLLALP 94
Cdd:COG1137 2 MTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVkpD------SGRIFLDGEDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 eeeM--RKVRGkdISMIFQEPmtSlnpIFpigkqiaEALTVHQDI---------SSSAAKAEVIRLLEKVRIPNAKNRfd 163
Cdd:COG1137 72 ---MhkRARLG--IGYLPQEA--S---IF-------RKLTVEDNIlavlelrklSKKEREERLEELLEEFGITHLRKS-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 164 dYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALD-VTIqGQILDLIKTLQeEEGMSVLfIT-HDmgvVAE---VSDR 238
Cdd:COG1137 133 -KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHN---VREtlgICDR 205
|
250
....*....|....*...
gi 549799341 239 TIVMFRGDVVETGTTDDI 256
Cdd:COG1137 206 AYIISEGKVLAEGTPEEI 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
351-496 |
3.80e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTSGDvMLDGyevlkldKTTLRTMRRSVQMIFQDpfASLDPRMSVgtaimepfI 430
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG-------TAPLAEAREDTRLMFQD--ARLLPWKKV--------I 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 431 EH-RLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK11247 100 DNvGLGLKGQWRDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
315-547 |
3.87e-17 |
|
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: 80.65 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFDIRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVmldgyevlkldk 394
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttlrTMRRSVQMIFqDPFASLDPRMSVGTAIMepFIEHRLG-TKQQAREKAADLLEKVGLSPDMMRRFPHeFSGGQRQRI 473
Cdd:cd03220 80 ----TVRGRVSSLL-GLGGGFNPELTGRENIY--LNGRLLGlSRKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 474 AIARSLMLDPKVIVADEAVSALDVSIKAQvCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEK-CQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
340-525 |
3.90e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldktTLRTMRRSVqmIFQD----PFASL 415
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAERGV--VFQNegllPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGtaimepfIEHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:PRK11248 88 QDNVAFG-------LQLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDM 525
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-257 |
4.22e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRvdggWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLdkktSRIEGKVMLGGRDLLALPEEE 97
Cdd:PRK10895 3 TLTAKNLAKAYK----GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIV----PRDAGNIIIDDEDISLLPLHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mRKVRGkdISMIFQEPmtSLNPIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKnrfDDYPHQFSGGMRQRV 177
Cdd:PRK10895 75 -RARRG--IGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLR---DSMGQSLSGGERRRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTiqgQILDLIKTLQ--EEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDD 255
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPI---SVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
..
gi 549799341 256 IF 257
Cdd:PRK10895 224 IL 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
315-547 |
4.47e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 80.15 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDk 394
Cdd:cd03369 7 IEVENLSVRY---------APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 ttLRTMRRSVQMIFQDPFasldprMSVGT--AIMEPFIEHrlgTKQQAREkaADLLEKVGLSpdmmrrfpheFSGGQRQR 472
Cdd:cd03369 77 --LEDLRSSLTIIPQDPT------LFSGTirSNLDPFDEY---SDEEIYG--ALRVSEGGLN----------LSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVShRVAVMYLGEIVEIG 547
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALI--QKTIREEFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
43-256 |
5.45e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 80.28 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 43 FEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEemrkvrgkdISMIFQEPMTSLNpiFP 122
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKT----TLLRAILGLIPPAKGTVKVAGASPGKGWRH---------IGYVPQRHEFAWD--FP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 123 IgkqiaealTVHQDISSSAAK-------------AEVIRLLEKVRIPNAKNRfddyP-HQFSGGMRQRVMIAMALASKPK 188
Cdd:TIGR03771 66 I--------SVAHTVMSGRTGhigwlrrpcvadfAAVRDALRRVGLTELADR----PvGELSGGQRQRVLVARALATRPS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRtIVMFRGDVVETGTTDDI 256
Cdd:TIGR03771 134 VLLLDEPFTGLDMPTQELLTELFIELA-GAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQL 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
340-566 |
5.53e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITR---LIEP--TSGDVMLDGYEVLKLDKTTLRtMRRSVQMIFQ--DPF 412
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDPVE-VRRRIGMVFQkpNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 A-SLDPRMSVGTAI------MEPFIEHRLgtKQQAR-EKAADLLEKVGLSpdmmrrfpheFSGGQRQRIAIARSLMLDPK 484
Cdd:PRK14243 104 PkSIYDNIAYGARIngykgdMDELVERSL--RQAALwDEVKDKLKQSGLS----------LSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 485 VIVADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVM---------YLGEIVEIGPRAAVFDN 555
Cdd:PRK14243 172 VILMDEPCSALDPISTLRI--EELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNS 249
|
250
....*....|.
gi 549799341 556 PQHPYTKKLMS 566
Cdd:PRK14243 250 PQQQATRDYVS 260
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-256 |
5.87e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 26 TSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPeeemrkvrgkd 105
Cdd:PRK10575 17 VSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKS----TLLKMLGRHQPPSEGEILLDAQPLESWS----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 106 iSMIFQEPMTSLNPIFPIgkqiAEALTVHQDIS-------------SSAAKAEVIRLLEKVRIPNAKNRFDDyphQFSGG 172
Cdd:PRK10575 80 -SKAFARKVAYLPQQLPA----AEGMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD---SLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
....
gi 549799341 253 TDDI 256
Cdd:PRK10575 232 PAEL 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
37-256 |
7.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLL-----------------DKKTSRIEGKVmlggrDLLALPEEEMR 99
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKT-TFIEHLNALllpdtgtiewifkdeknKKKTKEKEKVL-----EKLVIQKTRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 100 KVRG-----KDISMIFQepmtslnpiFPiGKQIAEAlTVHQDI---------SSSAAKAEVIRLLEKVRIPnaKNRFDDY 165
Cdd:PRK13651 96 KIKKikeirRRVGVVFQ---------FA-EYQLFEQ-TIEKDIifgpvsmgvSKEEAKKRAAKYIELVGLD--ESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRG 245
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|.
gi 549799341 246 DVVETGTTDDI 256
Cdd:PRK13651 242 KIIKDGDTYDI 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-500 |
8.00e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdGGWKSVvRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSRI------EGKVMLGGRdll 91
Cdd:NF040905 1 ILEMRGITKTF---PGVKAL-DDVNLSVREGEIHALCGENGAGKS----TLMKVL----SGVyphgsyEGEILFDGE--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 alpEEEMRKVRG---KDISMIFQE----PMTSL--NpIFpIGKQIAEaltvHQDISSSAAKAEVIRLLEKVRIpnaknrf 162
Cdd:NF040905 66 ---VCRFKDIRDseaLGIVIIHQElaliPYLSIaeN-IF-LGNERAK----RGVIDWNETNRRARELLAKVGL------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 163 DDYPHQFSG----GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDR 238
Cdd:NF040905 130 DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 239 TIVMFRGDVVET------GTTDDIFHRGrhpytrallsavpklgsMKERLLPARFPIIDIKTGEsqpvadvkdtvsggrt 312
Cdd:NF040905 209 ITVLRDGRTIETldcradEVTEDRIIRG-----------------MVGRDLEDRYPERTPKIGE---------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDIRSglfGRKsgavhAVEKVSFDLAEGETLSLVGESGCGK-----STTGRSITRLIeptSGDVMLDGY 387
Cdd:NF040905 256 VVFEVKNWTVYHPLHP---ERK-----VVDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGRNI---SGTVFKDGK 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 EVlkldktTLRTMRRSVQ--------------MIFQDP------FASLdPRMSVGTAIMEpFIEHRLGT--KQQAREKAA 445
Cdd:NF040905 325 EV------DVSTVSDAIDaglayvtedrkgygLNLIDDikrnitLANL-GKVSRRGVIDE-NEEIKVAEeyRKKMNIKTP 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 446 DLLEKVGlspdmmrrfphEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIK 500
Cdd:NF040905 397 SVFQKVG-----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAK 440
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
344-553 |
9.24e-17 |
|
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: 83.64 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDP------------ 411
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG---RHIGYLPQDVelfdgtiaenia 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 -FASLDPRMSVgtaimepfiehrlgtkqqareKAADLlekVGLSpDMMRRFPHEF-----------SGGQRQRIAIARSL 479
Cdd:COG4618 428 rFGDADPEKVV---------------------AAAKL---AGVH-EMILRLPDGYdtrigeggarlSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 480 MLDPKVIVADEAVSALD-----------VSIKAQvcnllldlqqnlNLAFLFISHDMAVVERVsHRVAVMYLGEIVEIGP 548
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDdegeaalaaaiRALKAR------------GATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGP 549
|
....*
gi 549799341 549 RAAVF 553
Cdd:COG4618 550 RDEVL 554
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-255 |
9.75e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPE 95
Cdd:PRK11160 336 QVSLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVrgkdISMIFQEPMtslnpIFpiGKQIAEALTVHQDissSAAKAEVIRLLEKVRIPN---AKNRFD----DYPHQ 168
Cdd:PRK11160 410 AALRQA----ISVVSQRVH-----LF--SATLRDNLLLAAP---NASDEALIEVLQQVGLEKlleDDKGLNawlgEGGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIktLQEEEGMSVLFITHDMGVVAEVsDRTIVMFRGDVV 248
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
....*..
gi 549799341 249 ETGTTDD 255
Cdd:PRK11160 553 EQGTHQE 559
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-496 |
1.09e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRS-VQMIFQDpfAS 414
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQR--YH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 415 LDPRMSVGTAIMEPFIEHRLGTKQQaREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYAGLERKQR-LLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
..
gi 549799341 495 LD 496
Cdd:PRK10535 175 LD 176
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
341-552 |
1.40e-16 |
|
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: 83.17 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKttlRTMRRSVQMIFQDP--FASldpr 418
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR---ETFGKHIGYLPQDVelFPG---- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 mSVGTAIMepfiehRLGTKQQARE-----KAADLLEkvglspdMMRRFPHEF-----------SGGQRQRIAIARSLMLD 482
Cdd:TIGR01842 407 -TVAENIA------RFGENADPEKiieaaKLAGVHE-------LILRLPDGYdtvigpggatlSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 483 PKVIVADEAVSALD-----------VSIKAQVCNLlldlqqnlnlafLFISHDMAVVERVShRVAVMYLGEIVEIGPRAA 551
Cdd:TIGR01842 473 PKLVVLDEPNSNLDeegeqalanaiKALKARGITV------------VVITHRPSLLGCVD-KILVLQDGRIARFGERDE 539
|
.
gi 549799341 552 V 552
Cdd:TIGR01842 540 V 540
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-272 |
1.53e-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: 79.74 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTtsFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSI------------MRLLDKKtsriegkv 83
Cdd:COG1119 1 DPLLELRNVT--VRRGG--KTILDDISWTVKPGEHWAILGPNGAGKS-TLLSLitgdlpptygndVRLFGER-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 84 mLGGrdllalpeEEMRKVRGK------DISMIFQEPMTSLNPIfpigkqiaeaLT-------VHQDISSsAAKAEVIRLL 150
Cdd:COG1119 68 -RGG--------EDVWELRKRiglvspALQLRFPRDETVLDVV----------LSgffdsigLYREPTD-EQRERARELL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 151 EKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMG 230
Cdd:COG1119 128 ELLGLAHLADR---PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 549799341 231 VVAEVSDRTIVMFRGDVVETGTTDDIFhrgrhpyTRALLSAV 272
Cdd:COG1119 205 EIPPGITHVLLLKDGRVVAAGPKEEVL-------TSENLSEA 239
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-252 |
2.19e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 82.56 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 39 RNMSFEIAPRETVAIVGESGSGKSvtslSIMRLL----DKKtsriEGKVMLGGRDLLALPEEEMRKVrgkdISMIFQEpm 114
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfyDVT----SGRILIDGQDIRDVTQASLRAA----IGIVPQD-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 TSLnpiF--PIGKQIAEALTvhqdissSAAKAEVIRLLEKVRIpnaknrfddypHQF-------------------SGGM 173
Cdd:COG5265 441 TVL---FndTIAYNIAYGRP-------DASEEEVEAAARAAQI-----------HDFieslpdgydtrvgerglklSGGE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDlikTLQE-EEGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGT 252
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA---ALREvARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
338-496 |
2.52e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 338 VHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldKTTLRTMRRSVQMIFQDP------ 411
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLK--DINLKWWRSKIGVVSQDPllfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 -----------------------------FASLDPRMS------------VGTAIMEPFIEHRLGTKQQAREKAADLLEK 450
Cdd:PTZ00265 476 iknnikyslyslkdlealsnyynedgndsQENKNKRNScrakcagdlndmSNTTDSNELIEMRKNYQTIKDSEVVDVSKK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 451 VgLSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PTZ00265 556 V-LIHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
351-496 |
2.67e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMR-RSVQMIFQDPFasLDPRMSVGTAIMEPF 429
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFM--LIPTLNALENVELPA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 430 IeHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK10584 114 L-LRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-245 |
2.88e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 8 MEQTGGSVSpvLSVQNLTTSfrvdgGwksvVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGG 87
Cdd:PRK10762 249 LDKAPGEVR--LKVDNLSGP-----G----VNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALPRTSGYVTLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 88 RDLLAL-PEE----------EMRKVRGKDISMIFQEPM--TSLNPIFPIGKQIAealtvHQDisSSAAKAEVIRLLeKVR 154
Cdd:PRK10762 314 HEVVTRsPQDglangivyisEDRKRDGLVLGMSVKENMslTALRYFSRAGGSLK-----HAD--EQQAVSDFIRLF-NIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 155 IPNAKNRFDDyphqFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAE 234
Cdd:PRK10762 386 TPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLG 460
|
250
....*....|.
gi 549799341 235 VSDRTIVMFRG 245
Cdd:PRK10762 461 MSDRILVMHEG 471
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
30-229 |
3.13e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.97 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 30 VDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLAlPEEEmrkvRGkdisMI 109
Cdd:PRK11248 9 ADYGGKPALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGSITLDGKPVEG-PGAE----RG----VV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 110 FQEpmTSLNPIFPIGKQIAEALTVhQDISSSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQRVMIAMALASKPKL 189
Cdd:PRK11248 76 FQN--EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRY---IWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 549799341 190 LIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDM 229
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-251 |
3.61e-16 |
|
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: 77.96 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 26 TSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVmlggrdllalpeeemrKVRGKD 105
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS-TLLRLLAGIYPPDS---GTV----------------TVRGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 106 ISMIfqEPMTSLNPifpigkqiaeALTVHQDISSSAA-----KAEVIRLLEKVRIPNAKNRFDDYP-HQFSGGMRQRVMI 179
Cdd:cd03220 86 SSLL--GLGGGFNP----------ELTGRENIYLNGRllglsRKEIDEKIDEIIEFSELGDFIDLPvKTYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 180 AMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
344-496 |
4.64e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 81.40 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdktTLRTMRRSVQMIFQDpfasldprmsvgT 423
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLRAAIGIVPQD------------T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 AIMEPFIEH-----RLGTKQQAREKAADL--LEkvglspDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKV 485
Cdd:COG5265 442 VLFNDTIAYniaygRPDASEEEVEAAARAaqIH------DFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPI 515
|
170
....*....|.
gi 549799341 486 IVADEAVSALD 496
Cdd:COG5265 516 LIFDEATSALD 526
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
37-240 |
5.23e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSVtslsimrLLdkktsriegKVMLGgrdLLALPEEEMRKVRGKDISMIFQEpmTS 116
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKST-------LL---------KVLAG---VLRPTSGTVRRAGGARVAYVPQR--SE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 LNPIFPigkqiaeaLTVHQDIS-------------SSAAKAEVIRLLEKVRIPN-AKNRFDDyphqFSGGMRQRVMIAMA 182
Cdd:NF040873 66 VPDSLP--------LTVRDLVAmgrwarrglwrrlTRDDRAAVDDALERVGLADlAGRQLGE----LSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 183 LASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTI 240
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRADPCVL 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-496 |
5.54e-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: 77.58 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 339 HAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdkTTLRTMRRSVQMIFQDpfASLDPR 418
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMHKRARLGIGYLPQE--ASIFRK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 419 MSVGTAIMePFIEHRLGTKQQAREKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:cd03218 90 LTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
344-571 |
5.64e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKLDKTTLRTMRRSVQMIFQDP-----FASLDPR 418
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALRQQVATVFQDPeqqifYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 MSvgtaimepFIEHRLGTKQQAREKAADllekVGLSPDMMRRFPHE----FSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK13638 99 IA--------FSLRNLGVPEAEITRRVD----EALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 495 LDVSIKAQVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ--------HPYTKKLMS 566
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEameqagltQPWLVKLHT 245
|
....*
gi 549799341 567 AVPVP 571
Cdd:PRK13638 246 QLGLP 250
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-272 |
6.31e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGgwksvvrnMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLdkktSRIEGKVMLGGRDLLALPEEEM 98
Cdd:COG4138 1 LQLNDVAVAGRLGP--------ISAQVNAGELIHLIGPNGAGKS-TLLARMAGL----LPGQGEILLNGRPLSDWSAAEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdisMIFQEPMTSLN-PIFpigkqiaEALTVHQD--ISSSAAKAEVIRLLEKVRIPNAKNRfddyP-HQFSGGMR 174
Cdd:COG4138 68 ARHRA----YLSQQQSPPFAmPVF-------QYLALHQPagASSEAVEQLLAQLAEALGLEDKLSR----PlTQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 175 QRVMIAMALA-------SKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDV 247
Cdd:COG4138 133 QRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
250 260
....*....|....*....|....*
gi 549799341 248 VETGTTDDIFhrgrhpyTRALLSAV 272
Cdd:COG4138 212 VASGETAEVM-------TPENLSEV 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-242 |
7.67e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.79 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGgrdllalpeeem 98
Cdd:cd03221 1 IELENL--SKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLIAGELEPDEGIVTWG------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 rkvrgkdismifqepmtslnpifpigkqiaealtvhqdisssaakaevirllEKVRIPnaknrfddYPHQFSGGMRQRVM 178
Cdd:cd03221 61 ----------------------------------------------------STVKIG--------YFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 179 IAMALASKPKLLIADEPTTALDVTiqgQILDLIKTLQEEEGmSVLFITHDMGVVAEVSDRTIVM 242
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLE---SIEALEEALKEYPG-TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-295 |
1.09e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 33 GWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVRgKDISMIFQE 112
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 113 P--MTSLNpIFpigKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFddyPHQFSGGMRQRVMIAMALASKPKLL 190
Cdd:PRK11831 93 GalFTDMN-VF---DNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 191 IADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIfHRGRHPYTRALLS 270
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPDPRVRQFLD 244
|
250 260
....*....|....*....|....*
gi 549799341 271 AVpklgsmKERLLPARFPIIDIKTG 295
Cdd:PRK11831 245 GI------ADGPVPFRYPAGDYHAD 263
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-279 |
1.13e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.47 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRvDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSimrlLDKKTSRIEGKVMLGGRdllALPEEE 97
Cdd:PRK13647 4 IIEVEDLHFRYK-DG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLH----LNGIYLPQRGRVKVMGR---EVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKdISMIFQEPMtslNPIFpigkqiaeALTVHQDIS-----SSAAKAEVI-RLLEKVRIPNAKNRFDDYPHQFSG 171
Cdd:PRK13647 74 EKWVRSK-VGLVFQDPD---DQVF--------SSTVWDDVAfgpvnMGLDKDEVErRVEEALKAVRMWDFRDKPPYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
250 260 270
....*....|....*....|....*....|....*
gi 549799341 252 -----TTDDIFHRG--RHPYTRALLSAVPKLGSMK 279
Cdd:PRK13647 221 dksllTDEDIVEQAglRLPLVAQIFEDLPELGQSK 255
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
317-544 |
1.27e-15 |
|
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: 76.60 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 317 VKDLTTRFDIRS----------GLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDG 386
Cdd:cd03267 3 VSNLSKSYRVYSkepgligslkSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 387 YEVLKLDKTTLR----TMRRSVQMIFQDPfasldprmsvgtaIMEPFIEHRL------GTKQQAREKAADLLEKVGLSPD 456
Cdd:cd03267 83 LVPWKRRKKFLRrigvVFGQKTQLWWDLP-------------VIDSFYLLAAiydlppARFKKRLDELSELLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 457 MMRRFPHefsgGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVA 536
Cdd:cd03267 150 PVRQLSL----GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
....*...
gi 549799341 537 VMYLGEIV 544
Cdd:cd03267 226 VIDKGRLL 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-228 |
1.36e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLttSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPE 95
Cdd:PRK10247 5 SPLLQLQNV--GYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPTS---GTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKvrgkDISMIFQEPM-----TSLNPIFP--IGKQIAEaltvhqdisssaaKAEVIRLLEKVRIPNakNRFDDYPHQ 168
Cdd:PRK10247 77 EIYRQ----QVSYCAQTPTlfgdtVYDNLIFPwqIRNQQPD-------------PAIFLDDLERFALPD--TILTKNIAE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHD 228
Cdd:PRK10247 138 LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
340-553 |
1.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.09 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTT-LRTMRRSVQMIFQDPFASLDPR 418
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 MSVGTAIMEPfieHRLG-TKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:PRK13649 102 TVLKDVAFGP---QNFGvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 498 SIKAQVCNLLLDLQQNLNLAFLfISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVF 553
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
297-496 |
1.72e-15 |
|
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: 79.99 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 297 SQPVADVKDTVSGGRTPILSVKDLTTRFDIRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIE 376
Cdd:TIGR03796 451 RNPVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 377 PTSGDVMLDGyevLKLDKTTLRTMRRSVQMIFQDPFasldprMSVGT----------AIMEPFIEhrlgtkqQAREKAAd 446
Cdd:TIGR03796 531 PWSGEILFDG---IPREEIPREVLANSVAMVDQDIF------LFEGTvrdnltlwdpTIPDADLV-------RACKDAA- 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 447 LLEKVGLSPDmmrRFPHE-------FSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:TIGR03796 594 IHDVITSRPG---GYDAElaegganLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-256 |
1.74e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.70 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTtsFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEE 97
Cdd:TIGR01842 316 HLSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS----TLARLIVGIWPPTSGSVRLDGADLKQWDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MrkvrGKDISMIFQEPmtslnPIFP--IGKQIA---EALTVHQDISssAAKA----EVIrllekVRIPNAknrFDDY--- 165
Cdd:TIGR01842 390 F----GKHIGYLPQDV-----ELFPgtVAENIArfgENADPEKIIE--AAKLagvhELI-----LRLPDG---YDTVigp 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 -PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVsDRTIVMFR 244
Cdd:TIGR01842 451 gGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPSLLGCV-DKILVLQD 528
|
250
....*....|..
gi 549799341 245 GDVVETGTTDDI 256
Cdd:TIGR01842 529 GRIARFGERDEV 540
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
313-490 |
1.86e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.22 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFDirsglfGRKsgavhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkl 392
Cdd:COG1137 2 MTLEAENLVKSYG------KRT-----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 dkTTLRTMRRSvQM----------IFQdpfasldpRMSVGTAIMEpFIEHRLGTKQQAREKAADLLEKVGLSPdmMRRFP 462
Cdd:COG1137 68 --THLPMHKRA-RLgigylpqeasIFR--------KLTVEDNILA-VLELRKLSKKEREERLEELLEEFGITH--LRKSK 133
|
170 180
....*....|....*....|....*....
gi 549799341 463 -HEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:COG1137 134 aYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
313-556 |
1.90e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKL 392
Cdd:PRK09536 2 PMIDVSDLSVEF-----------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKttlRTMRRSVQMIFQDpfASLDPRMSVGTAIMEPFIEH--RLGTKQQAREKAAD-LLEKVGLSPDMMRRFPhEFSGGQ 469
Cdd:PRK09536 71 SA---RAASRRVASVPQD--TSLSFEFDVRQVVEMGRTPHrsRFDTWTETDRAAVErAMERTGVAQFADRPVT-SLSGGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFIsHDMAVVERVSHRVAVMYLGEIVEIGPR 549
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPP 223
|
....*..
gi 549799341 550 AAVFDNP 556
Cdd:PRK09536 224 ADVLTAD 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
313-543 |
2.04e-15 |
|
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: 74.78 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRfdirsglfgrksgavHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKL 392
Cdd:cd03215 3 PVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DKTTLRtmRRSVQMIFQDpfasldpRMSVGTAIMEPFIEHRLgtkqqarekAADLLekvglspdmmrrfphefSGGQRQR 472
Cdd:cd03215 68 SPRDAI--RAGIAYVPED-------RKREGLVLDLSVAENIA---------LSSLL-----------------SGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEI 543
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEI-YRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-256 |
2.69e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 13 GSVSPV-LSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLggrdlL 91
Cdd:PRK13536 35 GSMSTVaIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKS----TIARMILGMTSPDAGKITV-----L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 ALPEEEMRKVRGKDISMIFQepMTSLNPIFpigkQIAEALTVHQ---DISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQ 168
Cdd:PRK13536 102 GVPVPARARLARARIGVVPQ--FDNLDLEF----TVRENLLVFGryfGMSTREIEAVIPSLLEFARL---ESKADARVSD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
....*...
gi 549799341 249 ETGTTDDI 256
Cdd:PRK13536 252 AEGRPHAL 259
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
37-258 |
3.90e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKktsrIEGKVMLGGRDLLALPEEEMRkvrgKDISMIFQEPMts 116
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV----CGGEIRVNGREIGAYGLRELR----RQFSMIPQDPV-- 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 lnpIFPiGkqiaealTVHQDIS--SSAAKAEVIRLLEKV----RIPNAKNRFDDYPHQ----FSGGMRQRVMIAMALASK 186
Cdd:PTZ00243 1395 ---LFD-G-------TVRQNVDpfLEASSAEVWAALELVglreRVASESEGIDSRVLEggsnYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 187 PKLLI-ADEPTT----ALDVTIQGQILDLIktlqeeEGMSVLFITHDMGVVAEVsDRTIVMFRGDVVETGT-------TD 254
Cdd:PTZ00243 1464 GSGFIlMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSprelvmnRQ 1536
|
....
gi 549799341 255 DIFH 258
Cdd:PTZ00243 1537 SIFH 1540
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-256 |
6.48e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 42 SFEIAPRETVAIVGESGSGKSvTSLSIMrlldKKTSRIEGKVMLGGRDLLALPEEEMRKVRGkdiSMIFQEPMTSLNPIF 121
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKS-TLLARM----AGLLPGSGSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 122 pigkqiaEALTVHQ-DISSSAAKAEVI-RLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMAL-----ASKP--KLLIA 192
Cdd:PRK03695 88 -------QYLTLHQpDKTRTEAVASALnEVAEALGLDDKLGR---SVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 193 DEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-568 |
7.19e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.81 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdKTTLRTMRRSVqmifqdpfasldprMSVGT 423
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW-SPAELARRRAV--------------LPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 AIMEPFIEH---RLG------TKQQAREKAADLLEKVGLSPDMMRRFPhEFSGGQRQRIAIARSLM------LDPKVIVA 488
Cdd:PRK13548 86 SLSFPFTVEevvAMGraphglSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 489 DEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFdnpqhpyTKKLMSAV 568
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-------TPETLRRV 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
341-496 |
7.49e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVML-DGYEVLkldkttlrtmrrsvqmifqdpFASLDPRM 419
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL---------------------FLPQRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGT---AIMEPFIEHRLgtkqqAREKAADLLEKVGLSP-----DMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:COG4178 438 PLGTlreALLYPATAEAF-----SDAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
....*
gi 549799341 492 VSALD 496
Cdd:COG4178 513 TSALD 517
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
314-503 |
9.05e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFdirsglfgrKSGAvHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklD 393
Cdd:PRK13647 4 IIEVEDLHFRY---------KDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDPfaslDPRMSVGTAIME-PFIEHRLG-TKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQ 471
Cdd:PRK13647 71 AENEKWVRSKVGLVFQDP----DDQVFSSTVWDDvAFGPVNMGlDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKK 145
|
170 180 190
....*....|....*....|....*....|..
gi 549799341 472 RIAIARSLMLDPKVIVADEAVSALDVSIKAQV 503
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
344-557 |
9.05e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.09 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLrtmRRSVQMIFQDPFasldprMSVGT 423
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPV------LFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 AI--MEPFIEHRLGTKQQAREKA--ADLLEK--VGLSPDMMRRfPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:PLN03232 1326 VRfnIDPFSEHNDADLWEALERAhiKDVIDRnpFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 498 SIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVShRVAVMYLGEIVEigpraavFDNPQ 557
Cdd:PLN03232 1405 RTDSLI--QRTIREEFKSCTMLVIAHRLNTIIDCD-KILVLSSGQVLE-------YDSPQ 1454
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
344-501 |
1.09e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDkttLRTMRRSVQMIFQDPFasldprMSVGT 423
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPV------LFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 AI--MEPFIEHrlgtkqqareKAADL---LEKVGLSpDMMRRFP-----------HEFSGGQRQRIAIARSLMLDPKVIV 487
Cdd:PLN03130 1329 VRfnLDPFNEH----------NDADLwesLERAHLK-DVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILV 1397
|
170
....*....|....
gi 549799341 488 ADEAVSALDVSIKA 501
Cdd:PLN03130 1398 LDEATAAVDVRTDA 1411
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
337-496 |
1.23e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 337 AVHAVEkvsFDLAEGETLSLVGESGCGKSTTGRSITRLIeptSGD------VMLDGYEVLKLDKTT--LRTMRRSVQMIF 408
Cdd:PRK09984 19 ALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDksagshIELLGRTVQREGRLArdIRKSRANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 409 QDpfASLDPRMSV------GTAIMEPFIEH--RLGTKQQaREKAADLLEKVGlspdmMRRFPHE----FSGGQRQRIAIA 476
Cdd:PRK09984 93 QQ--FNLVNRLSVlenvliGALGSTPFWRTcfSWFTREQ-KQRALQALTRVG-----MVHFAHQrvstLSGGQQQRVAIA 164
|
170 180
....*....|....*....|
gi 549799341 477 RSLMLDPKVIVADEAVSALD 496
Cdd:PRK09984 165 RALMQQAKVILADEPIASLD 184
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
344-553 |
1.24e-14 |
|
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: 73.97 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMldgyEVL--KLDKTTLRTMRRS---VQMIFQDPFaslDPR 418
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFgeRRGGEDVWELRKRiglVSPALQLRF---PRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 MSV-------GTAIMEPFIEHrlgTKQQaREKAADLLEKVGLSPDMMRRFpHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:COG1119 95 ETVldvvlsgFFDSIGLYREP---TDEQ-RERARELLELLGLAHLADRPF-GTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 492 VSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMA-VVERVSHrVAVMYLGEIVEIGPRAAVF 553
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITH-VLLLKDGRVVAAGPKEEVL 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-251 |
1.39e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.84 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsiMRLLDKKTSRIEGKVMLGGRDLlalpEE 96
Cdd:PRK13537 6 APIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTT----LRMLLGLTHPDAGSISLCGEPV----PS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRGKdISMIFQepMTSLNPIFpigkQIAEALTV---HQDISSSAAKAEVIRLLEKVRIpnaKNRFDDYPHQFSGGM 173
Cdd:PRK13537 74 RARHARQR-VGVVPQ--FDNLDPDF----TVRENLLVfgrYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETG 251
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-237 |
1.43e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 15 VSPVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRlldkktsriegkVMLGgrdLLALP 94
Cdd:PRK09544 1 MTSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKS----TLVR------------VVLG---LVAPD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEEMRKVRGKDISMIFQEpmTSLNPIFPigkqiaeaLTVHQ--DISSSAAKAEVIRLLEKVripNAKNRFDDYPHQFSGG 172
Cdd:PRK09544 58 EGVIKRNGKLRIGYVPQK--LYLDTTLP--------LTVNRflRLRPGTKKEDILPALKRV---QAGHLIDAPMQKLSGG 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 173 MRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSD 237
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTD 189
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
325-490 |
1.50e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.03 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 325 DIRSGLFGRksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSV 404
Cdd:PRK11831 9 DMRGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 405 QMIFQDpfASLDPRMSVGTAIMEPFIEHRLGTKQQAREKAADLLEKVGL--SPDMMrrfPHEFSGGQRQRIAIARSLMLD 482
Cdd:PRK11831 87 SMLFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLrgAAKLM---PSELSGGMARRAALARAIALE 161
|
....*...
gi 549799341 483 PKVIVADE 490
Cdd:PRK11831 162 PDLIMFDE 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
39-258 |
1.86e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 39 RNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLLALPEEEmrkvRGkdISMIFQEpmTSLN 118
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKS-TLLRMIAGLEDITS---GDLFIGEKRMNDVPPAE----RG--VGMVFQS--YALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 119 PifpigkqiaeALTVHQDIS-----SSAAKAEVIRLLEKV-RIPNAKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLIA 192
Cdd:PRK11000 88 P----------HLSVAENMSfglklAGAKKEEINQRVNQVaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 193 DEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFH 258
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-255 |
1.95e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGgrdllalpee 96
Cdd:COG0488 314 KVLELEGLSKSY---GD-KTLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLAGELEPDSGTVKLG---------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 emRKVRgkdISMIFQEpMTSLNPifpiGKQIAEALtvhQDISSSAAKAEVIRLLEkvripnaknRF----DD---YPHQF 169
Cdd:COG0488 376 --ETVK---IGYFDQH-QEELDP----DKTVLDEL---RDGAPGGTEQEVRGYLG---------RFlfsgDDafkPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDV-TIQGqildLIKTLQEEEGmSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
....*...
gi 549799341 249 E-TGTTDD 255
Cdd:COG0488 509 EyPGGYDD 516
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-262 |
2.18e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 8 MEQTGGSVSPVLS----VQNLTTSFRVDggwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKV 83
Cdd:PRK10790 326 RQQYGNDDRPLQSgridIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKS----TLASLLMGYYPLTEGEI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 84 MLGGRDLLALPEEEMRkvrgKDISMIFQEPMTSLNPIFpigkqiaEALTVHQDISssaaKAEVIRLLEKVRIPNAKNRFD 163
Cdd:PRK10790 399 RLDGRPLSSLSHSVLR----QGVAMVQQDPVVLADTFL-------ANVTLGRDIS----EEQVWQALETVQLAELARSLP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 164 DYPH--------QFSGGMRQRVMIAMALASKPKLLIADEPTTALDV----TIQgQILDLIKtlqeeEGMSVLFITHDMGV 231
Cdd:PRK10790 464 DGLYtplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteqAIQ-QALAAVR-----EHTTLVVIAHRLST 537
|
250 260 270
....*....|....*....|....*....|..
gi 549799341 232 VAEvSDRTIVMFRGDVVETGTTDDIF-HRGRH 262
Cdd:PRK10790 538 IVE-ADTILVLHRGQAVEQGTHQQLLaAQGRY 568
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
338-537 |
2.59e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 338 VHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKldKTTLRTMRRSVQMIFQDpfASLDP 417
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAALAAGVAIIYQE--LHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 418 RMSVGTAIMEPFIEHRLG--TKQQAREKAADLLEKVG--LSPDMMRRfphEFSGGQRQRIAIARSLMLDPKVIVADEAVS 493
Cdd:PRK11288 93 EMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGvdIDPDTPLK---YLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 549799341 494 ALDvSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAV 537
Cdd:PRK11288 170 SLS-AREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-263 |
2.72e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 10 QTGGSVSPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSRIEGKVMLGGRd 89
Cdd:TIGR00955 13 RVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKT-TLMNALAFRSPKGVKGSGSVLLNGM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 llALPEEEMRK----VRGKDI---SMIFQEPMtslnpifpigkQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRF 162
Cdd:TIGR00955 91 --PIDAKEMRAisayVQQDDLfipTLTVREHL-----------MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 163 DDYPHQ---FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHD-MGVVAEVSDR 238
Cdd:TIGR00955 158 IGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDK 236
|
250 260
....*....|....*....|....*...
gi 549799341 239 TIVMFRGDVVETGTTD---DIFHRGRHP 263
Cdd:TIGR00955 237 IILMAEGRVAYLGSPDqavPFFSDLGHP 264
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-252 |
3.19e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.83 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLlalPEEEM 98
Cdd:PRK11176 342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID----EGEILLDGHDL---RDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRgKDISMIFQEPMtslnpIF--PIGKQIAEALTVH---QDISSSAAKAEVIRLLEKVripnaKNRFDDYPHQ----F 169
Cdd:PRK11176 413 ASLR-NQVALVSQNVH-----LFndTIANNIAYARTEQysrEQIEEAARMAYAMDFINKM-----DNGLDTVIGEngvlL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEgmSVLFITHDMGVVaEVSDRTIVMFRGDVVE 249
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTI-EKADEILVVEDGEIVE 558
|
...
gi 549799341 250 TGT 252
Cdd:PRK11176 559 RGT 561
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
17-248 |
3.29e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPee 96
Cdd:PRK11614 4 VMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDWQ-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 emrkvrgkdISMIFQEPMTslnpIFPIGKQIAEALTVHQDISSSAAKAEVIRLLEKVR-----IPNAKNRFDDYPHQFSG 171
Cdd:PRK11614 74 ---------TAKIMREAVA----IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKwvyelFPRLHERRIQRAGTMSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-273 |
4.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 20 SVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPEEEMR 99
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE----KGRIMIDDCDVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 100 KVrgkdISMIFQEPMTSLNPI-FPIgkqiaEALTVHQDisssaakAEVIRLLEKVRIPNA--KNRFD------DYPHQFS 170
Cdd:PLN03232 1310 RV----LSIIPQSPVLFSGTVrFNI-----DPFSEHND-------ADLWEALERAHIKDVidRNPFGldaevsEGGENFS 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILdliKTLQEE-EGMSVLFITHDMGVVAEVsDRTIVMFRGDVVE 249
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ---RTIREEfKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLE 1449
|
250 260
....*....|....*....|....
gi 549799341 250 TGTTDDIFHRGRHPYTRALLSAVP 273
Cdd:PLN03232 1450 YDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
340-556 |
6.79e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkLDKTTLRTMRRSVQMIFQDPFASLdprm 419
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT--GDFSKLQGIRKLVGIVFQNPETQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 sVGTAIMEPFI---EHRLGTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK13644 91 -VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 497 VSiKAQVCNLLLDLQQNLNLAFLFISHDMAVVErVSHRVAVMYLGEIVEIGPRAAVFDNP 556
Cdd:PRK13644 169 PD-SGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-251 |
7.92e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 71.15 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVtslsimrLLDKKTSRIEGKVMLGGRDLLAlpEEE 97
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTT-------LLDAISGRVEGGGTTSGQILFN--GQP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 MRKVRGKD-ISMIFQEpmtslnpifpigKQIAEALTVHQDI-----------SSSAAKAEV-----IRLLEKVRIPNAKN 160
Cdd:cd03234 74 RKPDQFQKcVAYVRQD------------DILLPGLTVRETLtytailrlprkSSDAIRKKRvedvlLRDLALTRIGGNLV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 161 RfddyphQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQgqiLDLIKTLQE--EEGMSVLFITHDMGV-VAEVSD 237
Cdd:cd03234 142 K------GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA---LNLVSTLSQlaRRNRIVILTIHQPRSdLFRLFD 212
|
250
....*....|....
gi 549799341 238 RTIVMFRGDVVETG 251
Cdd:cd03234 213 RILLLSSGEIVYSG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
310-552 |
8.03e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 310 GRTPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV 389
Cdd:PRK13537 3 MSVAPIDFRNVEKRY-----------GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 390 lkldKTTLRTMRRSVQMIFQdpFASLDPRMSVGTAIMePFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFpHEFSGGQ 469
Cdd:PRK13537 72 ----PSRARHARQRVGVVPQ--FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 470 RQRIAIARSLMLDPKVIVADEAVSALDVSIKaQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLG-EIVEIGP 548
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAP 222
|
....
gi 549799341 549 RAAV 552
Cdd:PRK13537 223 HALI 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
314-496 |
8.74e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.66 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDIRSGLfgrksgAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkld 393
Cdd:COG1101 1 MLELKNLSKTFNPGTVN------EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 kTTLRTMRRSvQMI---FQDPFASLDPRMSvgtaimepfIEH--------------RLGTKQQAREKAADLLEKVGLS-P 455
Cdd:COG1101 71 -TKLPEYKRA-KYIgrvFQDPMMGTAPSMT---------IEEnlalayrrgkrrglRRGLTKKRRELFRELLATLGLGlE 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 549799341 456 DMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:COG1101 140 NRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-227 |
8.81e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.49 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktSRI----EGKV-MLGGRDLLAL 93
Cdd:cd03223 1 IELENLS--LATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRAL----AGLwpwgSGRIgMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 94 PEEemrkvrgkdismifqepmtslnPIFPIGkqiaealtvhqdisssaakaeviRLLEKVRipnaknrfddYP--HQFSG 171
Cdd:cd03223 70 PQR----------------------PYLPLG-----------------------TLREQLI----------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKtlqeEEGMSVLFITH 227
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
341-498 |
1.03e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdktTLRTMRRSVQMIFQDPfasLDPRms 420
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML---SSRQLARRLALLPQHH---LTPE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 vGTAIME-------PFIEH--RLGTKQQAREKAAdlLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:PRK11231 90 -GITVRElvaygrsPWLSLwgRLSAEDNARVNQA--MEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
....*..
gi 549799341 492 VSALDVS 498
Cdd:PRK11231 166 TTYLDIN 172
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-256 |
1.36e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 4 AATSMEQTGGSVSPV-LSVQNLTTsFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSrIEGK 82
Cdd:PRK11174 334 HPQQGEKELASNDPVtIEAEDLEI-LSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKT----SLLNALLGFLP-YQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 83 VMLGGRDLLALPEEEMRKvrgkDISMIFQepmtslNPIFPIGkqiaealTVHQDIS---SSAAKAEVIRLLEKVRIPNAK 159
Cdd:PRK11174 406 LKINGIELRELDPESWRK----HLSWVGQ------NPQLPHG-------TLRDNVLlgnPDASDEQLQQALENAWVSEFL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 160 NRFD---DYPHQ-----FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILdliKTLQEE-EGMSVLFITHDMG 230
Cdd:PRK11174 469 PLLPqglDTPIGdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM---QALNAAsRRQTTLMVTHQLE 545
|
250 260
....*....|....*....|....*.
gi 549799341 231 VVAEVsDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK11174 546 DLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-265 |
2.76e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 70.32 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLttSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKktsrIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03288 20 IKIHDL--CVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI----FDGKIVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKvrgkDISMIFQEPMTslnpifpigkqIAEALTVHQDissSAAKAEVIRLLEKVRIPNAKNRFDDYP-----------H 167
Cdd:cd03288 94 RS----RLSIILQDPIL-----------FSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEgmSVLFITHDMGVVAEvSDRTIVMFRGDV 247
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGIL 232
|
250
....*....|....*...
gi 549799341 248 VETGTTDDIFHRGRHPYT 265
Cdd:cd03288 233 VECDTPENLLAQEDGVFA 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-550 |
3.56e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRvdgGWKSVvRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGrdllalpe 95
Cdd:PRK11288 2 SPYLSFDGIGKTFP---GVKAL-DDISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPDA---GSILIDG-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKD-----ISMIFQE----P-MTslnpifpigkqIAEALTVHQ------DISSSAAKAEVIRLLEKVRI---P 156
Cdd:PRK11288 66 QEMRFASTTAalaagVAIIYQElhlvPeMT-----------VAENLYLGQlphkggIVNRRLLNYEAREQLEHLGVdidP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 157 NAKNRFddyphqFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVS 236
Cdd:PRK11288 135 DTPLKY------LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 237 DRTIVmfrgdvvetgttddiFHRGRHPYTRALLSAVPK---LGSMKERllparfPIIDIKTGESQPVADVKDTVSGGRTP 313
Cdd:PRK11288 208 DAITV---------------FKDGRYVATFDDMAQVDRdqlVQAMVGR------EIGDIYGYRPRPLGEVRLRLDGLKGP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSvkdlttrfdirsglfgrksgavhavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVLKLd 393
Cdd:PRK11288 267 GLR-------------------------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-KPIDI- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQD-------PFAS-------------------LDPRMSVGTAimEPFIEhRLGTKQQAREKAADL 447
Cdd:PRK11288 320 RSPRDAIRAGIMLCPEDrkaegiiPVHSvadninisarrhhlragclINNRWEAENA--DRFIR-SLNIKTPSREQLIMN 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 448 LekvglspdmmrrfphefSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAV 527
Cdd:PRK11288 397 L-----------------SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEI-YNVIYELAAQGVAVLFVSSDLPE 458
|
570 580
....*....|....*....|...
gi 549799341 528 VERVSHRVAVMYLGEIVEIGPRA 550
Cdd:PRK11288 459 VLGVADRIVVMREGRIAGELARE 481
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
315-498 |
3.88e-13 |
|
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: 68.54 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFDIRSglfgrksgavhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:TIGR01189 1 LAARNLACSRGERM-----------LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRtmrrsvQMIFQDPFASLDPRMSVGTAIMepFIEHRLGTKQQAREkaaDLLEKVGLSpDMMRRFPHEFSGGQRQRIA 474
Cdd:TIGR01189 70 EPHE------NILYLGHLPGLKPELSALENLH--FWAAIHGGAQRTIE---DALAAVGLT-GFEDLPAAQLSAGQQRRLA 137
|
170 180
....*....|....*....|....
gi 549799341 475 IARSLMLDPKVIVADEAVSALDVS 498
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKA 161
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-252 |
3.97e-13 |
|
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: 73.12 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDLlalpEE 96
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKT-TTLSILTGLLPPTS---GTVLVGGKDI----ET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKVRgKDISMIFQEpmtslNPIFPiGKQIAEALTVHQDI---SSSAAKAEVIRLLEKVRIPNAKNrfdDYPHQFSGGM 173
Cdd:TIGR01257 997 NLDAVR-QSLGMCPQH-----NILFH-HLTVAEHILFYAQLkgrSWEEAQLEMEAMLEDTGLHHKRN---EEAQDLSGGM 1066
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIktLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGT 252
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-257 |
4.12e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSFRvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMrlldkktsrieGKVMLGGRDLLALPE 95
Cdd:PRK15056 4 QAGIVVNDVTVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-----------GFVRLASGKISILGQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDISMIFQEPMTSLNpiFPIgkqIAEALTV-----HQD---ISSSAAKAEVIRLLEKVRIPNAKNRfddYPH 167
Cdd:PRK15056 70 PTRQALQKNLVAYVPQSEEVDWS--FPV---LVEDVVMmgrygHMGwlrRAKKRDRQIVTAALARVDMVEFRHR---QIG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTiVMFRGDV 247
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR-DEGKTMLVSTHNLGSVTEFCDYT-VMVKGTV 219
|
250
....*....|
gi 549799341 248 VETGTTDDIF 257
Cdd:PRK15056 220 LASGPTETTF 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-234 |
4.88e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSfRvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKsvTSLsiMRLLDKKTSRIEGKVMLGGRDLLALPEEe 97
Cdd:PRK13538 1 MLEARNLACE-R---DERILFSGLSFTLNAGELVQIEGPNGAGK--TSL--LRILAGLARPDAGEVLWQGEPIRRQRDE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mrkvrgkdismiFQEPMTSLnpifpiGKQ--IAEALTVH------QDISSSAAKAEVIRLLEKVRIpnakNRFDDYP-HQ 168
Cdd:PRK13538 72 ------------YHQDLLYL------GHQpgIKTELTALenlrfyQRLHGPGDDEALWEALAQVGL----AGFEDVPvRQ 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 169 FSGGMRQRVmiamALA----SKPKLLIADEPTTALDVtiQGqILDLIKTLQE--EEGMSVLFITH-DMGVVAE 234
Cdd:PRK13538 130 LSAGQQRRV----ALArlwlTRAPLWILDEPFTAIDK--QG-VARLEALLAQhaEQGGMVILTTHqDLPVASD 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
340-496 |
5.24e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMldgYEVLKLDKTTLRTMRRSVQMIFQDPFASLDprm 419
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIR---FHDIPLTKLQLDSWRSRLAVVSQTPFLFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTAIMEpfieHRLGTKQQAREKAADLlekVGLSPDMMRrFPHEF-----------SGGQRQRIAIARSLMLDPKVIVA 488
Cdd:PRK10789 404 TVANNIAL----GRPDATQQEIEHVARL---ASVHDDILR-LPQGYdtevgergvmlSGGQKQRISIARALLLNAEILIL 475
|
....*...
gi 549799341 489 DEAVSALD 496
Cdd:PRK10789 476 DDALSAVD 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-257 |
5.32e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRI------------------------------------- 79
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHivfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 80 -------------EGKVMLGGRDLLALPEEEMRKVrgkdISMIFQEPM---TSLNPIFPIGKQIAealtVHQDISSSAAK 143
Cdd:PTZ00265 1263 eggsgedstvfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPMlfnMSIYENIKFGKEDA----TREDVKRACKF 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 144 AEVIRLLEKVripnaKNRFDD----YPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEG 219
Cdd:PTZ00265 1335 AAIDEFIESL-----PNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD 1409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 549799341 220 MSVLFITHDMGVVAEvSDRTIVMFRGD-----VVETGTTDDIF 257
Cdd:PTZ00265 1410 KTIITIAHRIASIKR-SDKIVVFNNPDrtgsfVQAHGTHEELL 1451
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-259 |
5.35e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.64 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrvDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRL---LDKKTSrieGKVMLGGRDLLAL-P 94
Cdd:PRK11650 4 LKLQAVRKSY--DGK-TQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMvagLERITS---GEIWIGGRVVNELeP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 95 EEemrkvrgKDISMIFQEpmTSLNPifpigkqiaeALTVHQDISSS-----AAKAEVIRLLEKV-RIPNAKNRFDDYPHQ 168
Cdd:PRK11650 74 AD-------RDIAMVFQN--YALYP----------HMSVRENMAYGlkirgMPKAEIEERVAEAaRILELEPLLDRKPRE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
250
....*....|.
gi 549799341 249 ETGTTDDIFHR 259
Cdd:PRK11650 215 QIGTPVEVYEK 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-232 |
5.52e-13 |
|
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: 68.15 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSfRvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLlalpeEEM 98
Cdd:TIGR01189 1 LAARNLACS-R---GERMLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILAGLLRPDSGEVRWNGTPL-----AEQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEPmtSLNPIFpigkQIAEALTVHQDISSSAAKAeVIRLLEKVRIpnakNRFDDYP-HQFSGGMRQRV 177
Cdd:TIGR01189 68 RDEPHENILYLGHLP--GLKPEL----SALENLHFWAAIHGGAQRT-IEDALAAVGL----TGFEDLPaAQLSAGQQRRL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 178 MIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVV 232
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
314-548 |
9.79e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 314 ILSVKDLTTRFDIRS----------GLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVM 383
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 384 LDGYEVLKLDKTTLRTM-----RRSvQMIF----QDPFASLdprmsvgTAImepfieHRLgTKQQAREKAADLLEKVGLS 454
Cdd:COG4586 81 VLGYVPFKRRKEFARRIgvvfgQRS-QLWWdlpaIDSFRLL-------KAI------YRI-PDAEYKKRLDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 455 pDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVcnllldlqqnlnLAFL------------FIS 522
Cdd:COG4586 146 -ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI------------REFLkeynrergttilLTS 212
|
250 260
....*....|....*....|....*.
gi 549799341 523 HDMAVVERVSHRVAVMYLGEIVEIGP 548
Cdd:COG4586 213 HDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-256 |
1.18e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVdggwKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLL--------DKKTSRIEGKVMLGGRD 89
Cdd:PRK13547 1 MLTADHLHVARRH----RAILRDLSLRIEPGRVTALLGRNGAGKS----TLLKALagdltgggAPRGARVTGDVTLNGEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 90 LLALPEEEMRKVRgkdiSMIFQEPMT----SLNPIFPIGK----QIAEALTVH-QDISSSA-AKAEVIRLLEKvripnak 159
Cdd:PRK13547 73 LAAIDAPRLARLR----AVLPQAAQPafafSAREIVLLGRyphaRRAGALTHRdGEIAWQAlALAGATALVGR------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 160 nrfdDYPhQFSGGMRQRVMIAMALA---------SKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMG 230
Cdd:PRK13547 142 ----DVT-TLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPN 216
|
250 260
....*....|....*....|....*.
gi 549799341 231 VVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK13547 217 LAARHADRIAMLADGAIVAHGAPADV 242
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-560 |
1.44e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 349 AEGETlSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTT-LRTMRRSVQMIFQDpfASLDPRMSVGTAIme 427
Cdd:PRK11144 23 AQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEKRRIGYVFQD--ARLFPHYKVRGNL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 428 pfiehRLGTKQQAREKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLL 507
Cdd:PRK11144 98 -----RYGMAKSMVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 549799341 508 LDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFDNPQ-HPY 560
Cdd:PRK11144 172 ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-497 |
2.20e-12 |
|
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: 69.96 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKtsrIEGKVMLG-GRDLLALPEE----EMRKVRG------ 103
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDKD---FNGEARPQpGIKVGYLPQEpqldPTKTVREnveegv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 104 ----------KDISMIFQEPMTSLNpifpigkQIAEALTVHQDISSSAAKAEVIRLLEKV----RIPNaknrfDDYP-HQ 168
Cdd:TIGR03719 94 aeikdaldrfNEISAKYAEPDADFD-------KLAAEQAELQEIIDAADAWDLDSQLEIAmdalRCPP-----WDADvTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTiqgQILDLIKTLQEEEGmSVLFITHD-------MGVVAEVsDR-TI 240
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPG-TVVAVTHDryfldnvAGWILEL-DRgRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 241 VMFRGD-----------VVETGTTDDIFHR--------------GRHPYTRALLSAVPKLGSmKERLLPARFPIIDIKTG 295
Cdd:TIGR03719 237 IPWEGNysswleqkqkrLEQEEKEESARQKtlkrelewvrqspkGRQAKSKARLARYEELLS-QEFQKRNETAEIYIPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 296 ESqpvadVKDTVsggrtpiLSVKDLTTRFDIRSgLFgrksgavhavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLI 375
Cdd:TIGR03719 316 PR-----LGDKV-------IEAENLTKAFGDKL-LI----------DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 376 EPTSGDVmldgyevlkldkttlrTMRRSVQMIFQDPF-ASLDPRMSVGTAIMEPFIEHRLGTKQ-QARE-------KAAD 446
Cdd:TIGR03719 373 QPDSGTI----------------EIGETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREiPSRAyvgrfnfKGSD 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 549799341 447 LLEKVGlspdmmrrfphEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:TIGR03719 437 QQKKVG-----------QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-255 |
2.43e-12 |
|
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: 69.47 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTtSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsIMRLLDKKTSRIEGKVMLGGRDL-LALPEE 96
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTEL---VQALFGAYPGKFEGNVFINGKPVdIRNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKvrgkDISMIFQE-PMTSLNPIFPIGKQIA-EALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFDDYP-HQFSGGM 173
Cdd:TIGR02633 333 AIRA----GIAMVPEDrKRHGIVPILGVGKNITlSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVM----FRGDVVE 249
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIgegkLKGDFVN 487
|
....*.
gi 549799341 250 TGTTDD 255
Cdd:TIGR02633 488 HALTQE 493
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
344-496 |
2.89e-12 |
|
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: 66.53 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP---TSGDVMLDGYEVLKldkttlRTMRRSVQMIFQDPFasLDPRMS 420
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP------DQFQKCVAYVRQDDI--LLPGLT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 421 VGTAI--MEPFIEHRLGTKQQAREKAADLLEK-VGLSPDMMRRFPHeFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:cd03234 98 VRETLtyTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-496 |
3.62e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 42 SFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDLLALPEEEMRKVrgkdISMIFQEPMTSLnpIF 121
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS----ALARALAGELPLLSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNTDM--LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 122 P----IGKQIAEaltVHQDISSSAAKAEviRLLEKVRIPNAKNRFDDYphqFSGGMRQRVMIAMALASKPKLLIADEPTT 197
Cdd:PRK10938 93 PgeddTGRTTAE---IIQDEVKDPARCE--QLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 198 ALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFHRgrhpytrallSAVPKLgS 277
Cdd:PRK10938 165 GLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ----------ALVAQL-A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 278 MKERL----LPARF-PIIDIKTGESQPVADVKD-TVSGGRTPILSvkdlttrfdirsglfgrksgavhaveKVSFDLAEG 351
Cdd:PRK10938 233 HSEQLegvqLPEPDePSARHALPANEPRIVLNNgVVSYNDRPILH--------------------------NLSWQVNPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 352 ETLSLVGESGCGKSTTGRSITrlieptsGDvMLDGYEvlklDKTTLRTMRR-SVQMIFQDP----FAS----LDPRMS-- 420
Cdd:PRK10938 287 EHWQIVGPNGAGKSTLLSLIT-------GD-HPQGYS----NDLTLFGRRRgSGETIWDIKkhigYVSsslhLDYRVSts 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTAIMEPFIEhRLGTKQQA----REKAADLLEKVGLSPDMMRRFPHEFSGGQrQRIA-IARSLMLDPKVIVADEAVSAL 495
Cdd:PRK10938 355 VRNVILSGFFD-SIGIYQAVsdrqQKLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGL 432
|
.
gi 549799341 496 D 496
Cdd:PRK10938 433 D 433
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
341-496 |
4.72e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTlrTMRRSVQMIFQDpfASLDPRMS 420
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQE--ASIFRRLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 421 VGTAIMEPF-IEHRLgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK10895 95 VYDNLMAVLqIRDDL-SAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
37-260 |
5.42e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.20 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKtsriEGKVMLGGRDLLALPEEEMRKvrgkDISMIFQEPMTs 116
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA----EGEIIIDGLNIAKIGLHDLRF----KITIIPQDPVL- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 117 lnpifpigkqIAEALTVHQDISSSAAKAEVIRLLEKVRIPN-AKNRFDDYPHQ-------FSGGMRQRVMIAMALASKPK 188
Cdd:TIGR00957 1372 ----------FSGSLRMNLDPFSQYSDEEVWWALELAHLKTfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKTlqEEEGMSVLFITHDMGVVAEVSdRTIVMFRGDVVETGTTDDIF-HRG 260
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLqQRG 1511
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
136-256 |
6.18e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.45 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 136 DISSSAAKAEVIRLLEKVRIPNAKNRfddYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQ 215
Cdd:NF000106 115 DLSRKDARARADELLERFSLTEAAGR---AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 549799341 216 eEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:NF000106 192 -RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-235 |
7.40e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.82 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTtsfrVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRdllalPEEEM 98
Cdd:cd03231 1 LEADELT----CERDGRALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAGLSPPLAGRVLLNGG-----PLDFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEP--MTSLNPIfpigkqiaEALTVHQDISSSAAkaeVIRLLEKVRIpnakNRFDDYP-HQFSGGMRQ 175
Cdd:cd03231 68 RDSIARGLLYLGHAPgiKTTLSVL--------ENLRFWHADHSDEQ---VEEALARVGL----NGFEDRPvAQLSAGQQR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEV 235
Cdd:cd03231 133 RVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAG 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-253 |
8.05e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTtSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKsvTSLsIMRLLDKKTSRIEGKVMLGGRDL-LALPEE 96
Cdd:PRK13549 259 ILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGR--TEL-VQCLFGAYPGRWEGEIFIDGKPVkIRNPQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 EMRKvrgkDISMIFQE-PMTSLNPIFPIGKQIAeaLTVHQDISS----------SAAKAEVIRLleKVRIPNAKNRFDdy 165
Cdd:PRK13549 335 AIAQ----GIAMVPEDrKRDGIVPVMGVGKNIT--LAALDRFTGgsriddaaelKTILESIQRL--KVKTASPELAIA-- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 166 phQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVM--- 242
Cdd:PRK13549 405 --RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGLSDRVLVMheg 481
|
250
....*....|..
gi 549799341 243 -FRGDVVETGTT 253
Cdd:PRK13549 482 kLKGDLINHNLT 493
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
316-496 |
1.18e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 316 SVKDLTTRFDIRSGLFGRKSGAV--HAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEptsgdvmldgyevlkld 393
Cdd:COG2401 19 SVLDLSERVAIVLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 kttlrtmRRSVQMIFQDPFASLDPRMSVgtaimepfIEH--RLGTKQQAREkaadLLEKVGLS-PDMMRRFPHEFSGGQR 470
Cdd:COG2401 82 -------GTPVAGCVDVPDNQFGREASL--------IDAigRKGDFKDAVE----LLNAVGLSdAVLWLRRFKELSTGQK 142
|
170 180
....*....|....*....|....*.
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
544-580 |
1.19e-11 |
|
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: 60.11 E-value: 1.19e-11
10 20 30
....*....|....*....|....*....|....*..
gi 549799341 544 VEIGPRAAVFDNPQHPYTKKLMSAVPVPDPARRQIKR 580
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYT 37
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
52-258 |
1.34e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 52 AIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGRDL------LALPEEEMRkvrgkdISMIFQEPMtslnpIFP--- 122
Cdd:PRK11144 28 AIFGRSGAGKT----SLINAISGLTRPQKGRIVLNGRVLfdaekgICLPPEKRR------IGYVFQDAR-----LFPhyk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 123 ------IGkqIAEALTVHQDisssaakaEVIRLL--EKVripnaknrFDDYPHQFSGGMRQRVMIAMALASKPKLLIADE 194
Cdd:PRK11144 93 vrgnlrYG--MAKSMVAQFD--------KIVALLgiEPL--------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 195 PTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDIFH 258
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWA 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
329-503 |
1.60e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 329 GLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEP---TSGDVMLDGYEVlkldktTLRTMRRSVQ 405
Cdd:TIGR00955 29 GCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI------DAKEMRAISA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 406 MIFQDPFasLDPRMSVGTAIMepFIEH-RLG---TKQQAREKAADLLEKVGL---------SPDMMRrfphEFSGGQRQR 472
Cdd:TIGR00955 103 YVQQDDL--FIPTLTVREHLM--FQAHlRMPrrvTKKEKRERVDEVLQALGLrkcantrigVPGRVK----GLSGGERKR 174
|
170 180 190
....*....|....*....|....*....|.
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQV 503
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
143-537 |
2.18e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 143 KAEVIRLLEKVripNAKNRFDDYPHQF-------------SGGMRQRVMIAMALASKPKLLIADEPTTALDVtiqGQILD 209
Cdd:PRK13409 177 KGKVRELLKKV---DERGKLDEVVERLglenildrdiselSGGELQRVAIAAALLRDADFYFFDEPTSYLDI---RQRLN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 210 LIKTLQEE-EGMSVLFITHDMGVVAEVSDrTIVMFRGD-----VVEtgttddifhrgrHPY-TR----ALLSAVPKLGSM 278
Cdd:PRK13409 251 VARLIRELaEGKYVLVVEHDLAVLDYLAD-NVHIAYGEpgaygVVS------------KPKgVRvginEYLKGYLPEENM 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 279 KERLLPARFpiidiktgESQPVADVKDtvsggRTPILSVKDLTTRFdirsGLFgrkSGAVHAVEkvsfdLAEGETLSLVG 358
Cdd:PRK13409 318 RIRPEPIEF--------EERPPRDESE-----RETLVEYPDLTKKL----GDF---SLEVEGGE-----IYEGEVIGIVG 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 359 ESGCGKSTTGRSITRLIEPTSGDVMLDgyevLKLdkttlrtmrrSV--QMIFQDPFASL-DPRMSVGTAIMEPFIEHrlg 435
Cdd:PRK13409 373 PNGIGKTTFAKLLAGVLKPDEGEVDPE----LKI----------SYkpQYIKPDYDGTVeDLLRSITDDLGSSYYKS--- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 436 tkqqarekaaDLLEKVGLsPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLN 515
Cdd:PRK13409 436 ----------EIIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERE 504
|
410 420
....*....|....*....|..
gi 549799341 516 LAFLFISHDMAVVERVSHRVAV 537
Cdd:PRK13409 505 ATALVVDHDIYMIDYISDRLMV 526
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
336-535 |
2.87e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.02 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVL-------KLDKTTLRTMRRSVQMif 408
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVayvpqrsEVPDSLPLTVRDLVAM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 409 qdpfaSLDPRMSvgtaimePFIEHRlgtkQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVA 488
Cdd:NF040873 81 -----GRWARRG-------LWRRLT----RDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 549799341 489 DEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRV 535
Cdd:NF040873 144 DEPTTGLDAESRERI-IALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-252 |
3.31e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIegkvMLGGRDLLALPEEEMRKVrgkdISMIFQEPMT- 115
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI----LIDGCDISKFGLMDLRKV----LGIIPQAPVLf 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 116 ------SLNPifpigkqiaeaLTVHQDisssaakAEVIRLLEKVRIPNA--KNRF------DDYPHQFSGGMRQRVMIAM 181
Cdd:PLN03130 1326 sgtvrfNLDP-----------FNEHND-------ADLWESLERAHLKDVirRNSLgldaevSEAGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 182 ALASKPKLLIADEPTTALDVTIQGQILdliKTLQEE-EGMSVLFITHDMGVVAEvSDRTIVMFRGDVVETGT 252
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQ---KTIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDT 1455
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-552 |
4.40e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldKTTLRTMRRSVQMIFQdpFASLDPRMS 420
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTAIMEPFIEHRLGTKqQAREKAADLLEKVGLSPDMMRRFPhEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIK 500
Cdd:PRK13536 131 VRENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 549799341 501 aQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLG-EIVEIGPRAAV 552
Cdd:PRK13536 209 -HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALI 260
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-204 |
5.03e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 63.72 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFrVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDkktsrIEGKVMLGGRDLLALPEEEM 98
Cdd:cd03289 3 MTVKDLTAKY-TEGG-NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-----TEGDIQIDGVSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGKDISMIFQEPMTSLNPIFPIGKqiaealtvHQDisssaakAEVIRLLEKVRIpnaKNRFDDYPHQ---------- 168
Cdd:cd03289 76 RKAFGVIPQKVFIFSGTFRKNLDPYGK--------WSD-------EEIWKVAEEVGL---KSVIEQFPGQldfvlvdggc 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 549799341 169 -FSGGMRQRVMIAMALASKPKLLIADEPTTALD-VTIQ 204
Cdd:cd03289 138 vLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
344-501 |
5.45e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkttlrtmrrsvqmIFQDPFAS--------- 414
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-----------------DDPDVAEAchylghrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 415 LDPRMSVGTAIMepFIEHRLGTkqqAREKAADLLEKVGLSPDMMRRFpHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK13539 84 MKPALTVAENLE--FWAAFLGG---EELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
....*..
gi 549799341 495 LDVSIKA 501
Cdd:PRK13539 158 LDAAAVA 164
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
315-549 |
5.84e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRfdirsglfgrkSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRL--IEPTSGDVMLDGYEVLKL 392
Cdd:cd03217 1 LEIKDLHVS-----------VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 393 DkTTLRTmRRSVQMIFQDPfasldPRMSvgtaimepfiehrlGTKqqarekAADLLEKVGLSpdmmrrfpheFSGGQRQR 472
Cdd:cd03217 70 P-PEERA-RLGIFLAFQYP-----PEIP--------------GVK------NADFLRYVNEG----------FSGGEKKR 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 473 IAIARSLMLDPKVIVADEAVSALDVSIKAQVCnLLLDLQQNLNLAFLFISHDMAVVERV-SHRVAVMYLGEIVEIGPR 549
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVA-EVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
331-547 |
1.04e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMrrsvqmifqd 410
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA---------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 pfasldprMSVgtaimepfIEHR-------------LGTKQQAREKAADLLEKVGLSP-------------DMMRrfphE 464
Cdd:PRK11160 416 --------ISV--------VSQRvhlfsatlrdnllLAAPNASDEALIEVLQQVGLEKlleddkglnawlgEGGR----Q 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 465 FSGGQRQRIAIARSLMLDPKVIVADEAVSALD-------VSIKAQVCnllldlqqnLNLAFLFISHDMAVVERVShRVAV 537
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaeterqiLELLAEHA---------QNKTVLMITHRLTGLEQFD-RICV 545
|
250
....*....|
gi 549799341 538 MYLGEIVEIG 547
Cdd:PRK11160 546 MDNGQIIEQG 555
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-253 |
1.08e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.72 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFRVDGGWKSVVRNmsfeIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSRIEGKVMLGGRDL-----LA 92
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLN----IHHGEMVALLGPSGSGKS-TLLRHLSGLITGDKSAGSHIELLGRTVqregrLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 93 lpeEEMRKVRGKdISMIFQE-----PMTSLNPIF-------PIGKQIAEALTVHQdisssaaKAEVIRLLEKVRIPNakn 160
Cdd:PRK09984 79 ---RDIRKSRAN-TGYIFQQfnlvnRLSVLENVLigalgstPFWRTCFSWFTREQ-------KQRALQALTRVGMVH--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 161 rfddYPHQ----FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVS 236
Cdd:PRK09984 145 ----FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYC 220
|
250
....*....|....*..
gi 549799341 237 DRTIVMFRGDVVETGTT 253
Cdd:PRK09984 221 ERIVALRQGHVFYDGSS 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
331-552 |
1.47e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 331 FGRKSGAvhavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQD 410
Cdd:PRK10253 17 YGKYTVA----ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 411 pfASLDPRMSVGTAIMEPFIEHR-LGT--KQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIV 487
Cdd:PRK10253 90 --ATTPGDITVQELVARGRYPHQpLFTrwRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 488 ADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG-PRAAV 552
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGaPKEIV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-255 |
1.72e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 6 TSMEQTGGSVS--PVLSVQNLTtsfRVDGGwksVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKV 83
Cdd:PRK09700 251 NAMKENVSNLAheTVFEVRNVT---SRDRK---KVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEI 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 84 MLGGRDLLalPEEEMRKVRgKDISMIFQEPMTslNPIFPiGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNRFD 163
Cdd:PRK09700 321 RLNGKDIS--PRSPLDAVK-KGMAYITESRRD--NGFFP-NFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 164 DYP----------HQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVA 233
Cdd:PRK09700 395 LLAlkchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEII 473
|
250 260
....*....|....*....|..
gi 549799341 234 EVSDRTIVMFRGDVVETGTTDD 255
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQILTNRD 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
35-243 |
1.89e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktsriegkvmlggrdllalpEEEMRKVRGKDISMIFQEPm 114
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL----------------------AGALKGTPVAGCVDVPDNQ- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 tslnpiFPIGKQIAEALTVHQDIsssaakAEVIRLLEKVRIPNA---KNRFDDYphqfSGGMRQRVMIAMALASKPKLLI 191
Cdd:COG2401 96 ------FGREASLIDAIGRKGDF------KDAVELLNAVGLSDAvlwLRRFKEL----STGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 549799341 192 ADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVMF 243
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
333-551 |
2.37e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRsITRLIEPT---SGDVMLDGYEvlkLDKTTLR-TMRRSVQMIF 408
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSP---LKASNIRdTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 409 QDpfASLDPRMSVGTAI-MEPFIEHRLGTKQQAR--EKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKV 485
Cdd:TIGR02633 85 QE--LTLVPELSVAENIfLGNEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 486 IVADEAVSALDVSiKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEivEIGPRAA 551
Cdd:TIGR02633 163 LILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKDM 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-496 |
2.53e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.88 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 310 GRTPILSVKDLTTRFDIrsglFGRKsgavhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV 389
Cdd:TIGR01257 924 GLVPGVCVKNLVKIFEP----SGRP-----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 390 lkldKTTLRTMRRSVQMIFQDPFasLDPRMSVGTAIMepFIEHRLG-TKQQAREKAADLLEKVGLSPDMMRRfPHEFSGG 468
Cdd:TIGR01257 995 ----ETNLDAVRQSLGMCPQHNI--LFHHLTVAEHIL--FYAQLKGrSWEEAQLEMEAMLEDTGLHHKRNEE-AQDLSGG 1065
|
170 180
....*....|....*....|....*...
gi 549799341 469 QRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:TIGR01257 1066 MQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
135-245 |
2.71e-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: 63.26 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 135 QDISSSAAKAEVIRLLEKVRIpnaknrFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTL 214
Cdd:COG1245 428 DDFGSSYYKTEIIKPLGLEKL------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
90 100 110
....*....|....*....|....*....|.
gi 549799341 215 QEEEGMSVLFITHDMGVVAEVSDRTIVmFRG 245
Cdd:COG1245 502 AENRGKTAMVVDHDIYLIDYISDRLMV-FEG 531
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-503 |
2.74e-10 |
|
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: 59.47 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDV-MLDGYEVLkldkttlrtmrrsvqMIFQDPFasldprM 419
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLL---------------FLPQRPY------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTaimepfiehrlgtkqqarekaadLLEKVglspdmmrRFP--HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:cd03223 76 PLGT-----------------------LREQL--------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
....*.
gi 549799341 498 SIKAQV 503
Cdd:cd03223 125 ESEDRL 130
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
351-547 |
2.98e-10 |
|
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: 63.43 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDkttLRTMRRSVQMIFQDP-FASLDPRMSvgtaiMEPF 429
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPvLFSGSLRMN-----LDPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 430 IEHRLGTKQQAREkAADLLEKVGLSPDmmrRFPHE-------FSGGQRQRIAIARSLMLDPKVIVADEAVSALDV----- 497
Cdd:TIGR00957 1384 SQYSDEEVWWALE-LAHLKTFVSALPD---KLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnl 1459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 549799341 498 ---SIKAQVcnllldlqqnLNLAFLFISHDMAVVERVShRVAVMYLGEIVEIG 547
Cdd:TIGR00957 1460 iqsTIRTQF----------EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
355-496 |
3.38e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 355 SLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDPF---ASLDPRMSVGTAIMEpfie 431
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR---QGVAMVQQDPVvlaDTFLANVTLGRDISE---- 443
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 432 hrlgtkqqarEKAADLLEKVGLSpDMMRRFP-----------HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:PRK10790 444 ----------EQVWQALETVQLA-ELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
284-541 |
3.41e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.49 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 284 PARFPIIDiktgESQPVADVKDTV-SGG-RTPILSVKDLTTrfdIRSGlfgrksGAVHAVEKVSFDLAEGETLSLVGESG 361
Cdd:TIGR01257 1909 PAKEPIFD----EDDDVAEERQRIiSGGnKTDILRLNELTK---VYSG------TSSPAVDRLCVGVRPGECFGLLGVNG 1975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 362 CGKSTTGRSITRLIEPTSGDVMLDGYEVLkldkTTLRTMRRSvqMIFQDPFASLDPRMsvgTAIMEPFIEHRL-GTKQQA 440
Cdd:TIGR01257 1976 AGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQN--MGYCPQFDAIDDLL---TGREHLYLYARLrGVPAEE 2046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 441 REKAADL-LEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKaQVCNLLLDLQQNLNLAFL 519
Cdd:TIGR01257 2047 IEKVANWsIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR-RMLWNTIVSIIREGRAVV 2124
|
250 260
....*....|....*....|..
gi 549799341 520 FISHDMAVVERVSHRVAVMYLG 541
Cdd:TIGR01257 2125 LTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-248 |
4.76e-10 |
|
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: 59.58 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTS---RIEGKVMLGGrdllaLPEEEMRKVRGKDISMIFQ 111
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCS----TLLKALANRTEgnvSVEGDIHYNG-----IPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 112 EPMtslnpifpigkQIAEaLTVHQDISSSAakaevirllekvripnaKNRFDDYPHQFSGGMRQRVMIAMALASKPKLLI 191
Cdd:cd03233 91 EDV-----------HFPT-LTVRETLDFAL-----------------RCKGNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 192 ADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVA-EVSDRTIVMFRGDVV 248
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQI 199
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
542-593 |
5.25e-10 |
|
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: 56.22 E-value: 5.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 549799341 542 EIVEIGPRAAVFDNPQHPYTKKLMSAVPVP-DPARRQIKrnmATDEIRSPIRP 593
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRDRKLIS---IPGEVPSLINL 50
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-254 |
6.07e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 16 SPVLSVQNLTTSfrVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSvtSLSIMRLLDKKTSRIEGKVMLGGRDLLALpE 95
Cdd:CHL00131 5 KPILEIKNLHAS--VNE--NEILKGLNLSINKGEIHAIMGPNGSGKS--TLSKVIAGHPAYKILEGDILFKGESILDL-E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGkdISMIFQEP------------MTSLNpifpiGKQIAEALTVHQDISSsaakAEVIRllEKVRIPNAKNRF- 162
Cdd:CHL00131 78 PEERAHLG--IFLAFQYPieipgvsnadflRLAYN-----SKRKFQGLPELDPLEF----LEIIN--EKLKLVGMDPSFl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 163 -DDYPHQFSGGMRQRVMI-AMALaSKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGmSVLFITHDMGVVAEVS-DRT 239
Cdd:CHL00131 145 sRNVNEGFSGGEKKRNEIlQMAL-LDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYV 222
|
250
....*....|....*
gi 549799341 240 IVMFRGDVVETGTTD 254
Cdd:CHL00131 223 HVMQNGKIIKTGDAE 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
344-528 |
6.37e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLD-----GY--EVLKLDKTTLRTMRRsvqmifqdpFASLD 416
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgklriGYvpQKLYLDTTLPLTVNR---------FLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 417 PrmSVGTAIMEPFIEhrlgtkqqaREKAADLLEkvglspdmmrrFP-HEFSGGQRQRIAIARSLMLDPKVIVADEAVSAL 495
Cdd:PRK09544 94 P--GTKKEDILPALK---------RVQAGHLID-----------APmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190
....*....|....*....|....*....|...
gi 549799341 496 DVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVV 528
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-245 |
6.55e-10 |
|
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: 58.79 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVtslsimrLLD-----KKTSRIEGKVMLGGRDLl 91
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT-------LLDvlagrKTAGVITGEILINGRPL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 alpEEEMRKVRGkdismiFQEPMTSLNPifpigkqiaeALTVHQDISSSAAkaevIRLLekvripnaknrfddyphqfSG 171
Cdd:cd03232 74 ---DKNFQRSTG------YVEQQDVHSP----------NLTVREALRFSAL----LRGL-------------------SV 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 172 GMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHD-MGVVAEVSDRTIVMFRG 245
Cdd:cd03232 112 EQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
313-551 |
7.73e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRsITRLIEPT---SGDVMLDGyEV 389
Cdd:PRK13549 4 YLLEMKNITKTF-----------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEG-EE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 390 LKLdKTTLRTMRRSVQMIFQDpfASLDPRMSVGTAIM---EPFIEHRLGTKQQAREkAADLLEKVGLSPDMMRRFpHEFS 466
Cdd:PRK13549 71 LQA-SNIRDTERAGIAIIHQE--LALVKELSVLENIFlgnEITPGGIMDYDAMYLR-AQKLLAQLKLDINPATPV-GNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 467 GGQRQRIAIARSLMLDPKVIVADEAVSALDVSiKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEivEI 546
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HI 222
|
....*
gi 549799341 547 GPRAA 551
Cdd:PRK13549 223 GTRPA 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
342-502 |
9.62e-10 |
|
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: 58.66 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 342 EKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyevlkldkTTLRTMRRSVQ--MIFQDPFASLDPRM 419
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--------GPLDFQRDSIArgLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 420 SVGTAIMepfIEHRLGtkqqAREKAADLLEKVGLSPDMMRRFpHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSI 499
Cdd:cd03231 89 SVLENLR---FWHADH----SDEQVEEALARVGLNGFEDRPV-AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
...
gi 549799341 500 KAQ 502
Cdd:cd03231 161 VAR 163
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
341-496 |
1.37e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.94 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQDPfaSLDPRMS 420
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV---ATTPSRELAKRLAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 421 VGTAIM---EPFIEHRLgtKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:COG4604 92 VRELVAfgrFPYSKGRL--TAEDREIIDEAIAYLDLE-DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
136-245 |
1.49e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 136 DISSSAAKAEVIRLLEKVRIpnaknrFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQ 215
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQLERL------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
90 100 110
....*....|....*....|....*....|
gi 549799341 216 EEEGMSVLFITHDMGVVAEVSDRTIVmFRG 245
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYISDRLMV-FEG 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-248 |
1.84e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 29 RVDGGWKS-----VVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGgRDLLA--LPEEEMRKV 101
Cdd:PRK11147 5 SIHGAWLSfsdapLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNGEVLLDDGRIIYE-QDLIVarLQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 102 RGKDISMIFQepmtslnpifpiG-KQIAEALTVHQDIS-------SSAAKAEVIRLLEKVRIPNAKnRFDDYPHQ----- 168
Cdd:PRK11147 80 EGTVYDFVAE------------GiEEQAEYLKRYHDIShlvetdpSEKNLNELAKLQEQLDHHNLW-QLENRINEvlaql 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 ----------FSGGMRQRVMIAMALASKPKLLIADEPTTALDV-TIQGqildLIKTLQEEEGmSVLFITHDMGVVAEVSD 237
Cdd:PRK11147 147 gldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIeTIEW----LEGFLKTFQG-SIIFISHDRSFIRNMAT 221
|
250
....*....|.
gi 549799341 238 RTIVMFRGDVV 248
Cdd:PRK11147 222 RIVDLDRGKLV 232
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
248-291 |
2.08e-09 |
|
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: 53.94 E-value: 2.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 549799341 248 VETGTTDDIFHRGRHPYTRALLSAVPKLGSMKERL--LPARFPIID 291
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLytIPGNVPSLL 46
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-537 |
2.10e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 347 DLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkldkttlrtmrrsvqmIFQDPFASLDPRMSVGTAIM 426
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------------SYKPQYIKADYEGTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 427 EpfIEHRLGTKQQARekaADLLEKVGLSPDMMRRFPhEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNL 506
Cdd:cd03237 84 S--ITKDFYTHPYFK---TEIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|.
gi 549799341 507 LLDLQQNLNLAFLFISHDMAVVERVSHRVAV 537
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
333-558 |
2.73e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 333 RKSGAVhaVEKVSFDLAEGETLSLVGESGCGKSTTGRSIT-RLIEPT-------SGDVMLDGYEVLKLDKTTLRTMRRSV 404
Cdd:PRK13547 11 RRHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 405 QMIFQDPFA-SLDPRMSVGTAimePFIEHRLGTKQQAREKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSL---- 479
Cdd:PRK13547 89 PQAAQPAFAfSAREIVLLGRY---PHARRAGALTHRDGEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 480 -----MLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAVFd 554
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL- 243
|
....
gi 549799341 555 NPQH 558
Cdd:PRK13547 244 TPAH 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-204 |
2.76e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.31 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSFRVDGgwKSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKktsriEGKVMLGGRDLLALPEEEM 98
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-----EGEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 99 RKVRGkdisMIFQEpmtslnpIFPIGKQIAEALTVHQDISSSaakaEVIRLLEKVRIPNAKNRF--------DDYPHQFS 170
Cdd:TIGR01271 1291 RKAFG----VIPQK-------VFIFSGTFRKNLDPYEQWSDE----EIWKVAEEVGLKSVIEQFpdkldfvlVDGGYVLS 1355
|
170 180 190
....*....|....*....|....*....|....*
gi 549799341 171 GGMRQRVMIAMALASKPKLLIADEPTTALD-VTIQ 204
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
170-537 |
3.67e-09 |
|
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: 59.41 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVtiqGQILDLIKTLQE--EEGMSVLFITHDMGVVAEVSDrTIVMFRGD- 246
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDI---YQRLNVARLIRElaEEGKYVLVVEHDLAILDYLAD-YVHILYGEp 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 247 ----VVEtgttddifhrgrHPY-TR----ALLSAVPKLGSMKERLLPARFpiidiktgESQPVADVKDtvsggRTPILSV 317
Cdd:COG1245 290 gvygVVS------------KPKsVRvginQYLDGYLPEENVRIRDEPIEF--------EVHAPRREKE-----EETLVEY 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 318 KDLTTRFDirsglfGRK----SGAVHavekvsfdlaEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLD-------G 386
Cdd:COG1245 345 PDLTKSYG------GFSleveGGEIR----------EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 387 YEVLKLDKTtlrtmrrsVQMIFqdpfasldpRMSVGTAIMEPFIEHrlgtkqqarekaaDLLEKVGLSPdMMRRFPHEFS 466
Cdd:COG1245 409 YISPDYDGT--------VEEFL---------RSANTDDFGSSYYKT-------------EIIKPLGLEK-LLDKNVKDLS 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 467 GGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAV 537
Cdd:COG1245 458 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
247-283 |
4.67e-09 |
|
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: 53.52 E-value: 4.67e-09
10 20 30
....*....|....*....|....*....|....*..
gi 549799341 247 VVETGTTDDIFHRGRHPYTRALLSAVPKLGSMKERLL 283
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLI 38
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
315-497 |
7.59e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFDIRSgLFgrksgavhavEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDK 394
Cdd:PRK13538 2 LEARNLACERDERI-LF----------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 395 TTLRTMRrsvqmifqdpfasldprmsvgtaimepFIEHRLGTK-----------------QQAREKAADLLEKVGLspdm 457
Cdd:PRK13538 71 EYHQDLL---------------------------YLGHQPGIKteltalenlrfyqrlhgPGDDEALWEALAQVGL---- 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 549799341 458 mRRF---P-HEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:PRK13538 120 -AGFedvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
342-537 |
8.76e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 342 EKVSFDLAEGETLSLVGESGCGKSTTgrsitrlIEPTSGDVMLDGYEVLKLDkttLRTMRRSVQMIFQDPfasldprMSV 421
Cdd:PTZ00265 1246 EEQNVGMKNVNEFSLTKEGGSGEDST-------VFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEP-------MLF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 GTAIMEPFiehRLGTKQQAREKAADLLeKVGLSPDMMRRFPHEF-----------SGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PTZ00265 1309 NMSIYENI---KFGKEDATREDVKRAC-KFAAIDEFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDE 1384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 549799341 491 AVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERvSHRVAV 537
Cdd:PTZ00265 1385 ATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
308-496 |
9.22e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 308 SGGRtpiLSVKDLTTRFdirsglfgrKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEpTSGDVMLDGy 387
Cdd:TIGR01271 1214 SGGQ---MDVQGLTAKY---------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG- 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 evLKLDKTTLRTMRRSVQMIFQDPFA-SLDPRMSvgtaiMEPFiehrlgtKQQAREKAADLLEKVGLSpDMMRRFPHE-- 464
Cdd:TIGR01271 1280 --VSWNSVTLQTWRKAFGVIPQKVFIfSGTFRKN-----LDPY-------EQWSDEEIWKVAEEVGLK-SVIEQFPDKld 1344
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 549799341 465 ---------FSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:TIGR01271 1345 fvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
343-557 |
1.02e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 343 KVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQDPFAsLDP--RMS 420
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI---GAYGLRELRRQFSMIPQDPVL-FDGtvRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VgtaimEPFIEhrlgtKQQAREKAAdlLEKVGLSpdmmRRFPHE--------------FSGGQRQRIAIARSLM-LDPKV 485
Cdd:PTZ00243 1404 V-----DPFLE-----ASSAEVWAA--LELVGLR----ERVASEsegidsrvleggsnYSVGQRQLMCMARALLkKGSGF 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 486 IVADEAVS----ALDVSIKAQVcnllldlqqnlNLAF-----LFISHDMAVVERVShRVAVMYLGEIVEIG-PRAAVFdN 555
Cdd:PTZ00243 1468 ILMDEATAnidpALDRQIQATV-----------MSAFsaytvITIAHRLHTVAQYD-KIIVMDHGAVAEMGsPRELVM-N 1534
|
..
gi 549799341 556 PQ 557
Cdd:PTZ00243 1535 RQ 1536
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
174-546 |
1.22e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 174 RQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEeGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTT 253
Cdd:PRK10982 140 MQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 254 DDifhrgrhpytralLSAVPKLGSMKERLLPARFPIIDIKTGESqpvadvkdtvsggrtpILSVKDLTtrfdirsglfgr 333
Cdd:PRK10982 219 AG-------------LTMDKIIAMMVGRSLTQRFPDKENKPGEV----------------ILEVRNLT------------ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 334 kSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlkLDKTTLRTMRRSVQMIFQDP-- 411
Cdd:PRK10982 258 -SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI--NNHNANEAINHGFALVTEERrs 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 ---FASLDPRMSVGTAIMEPFIEhRLGTKQQAREKAadlleKVGLSPDMMR-RFPHE------FSGGQRQRIAIARSLML 481
Cdd:PRK10982 335 tgiYAYLDIGFNSLISNIRNYKN-KVGLLDNSRMKS-----DTQWVIDSMRvKTPGHrtqigsLSGGNQQKVIIGRWLLT 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 482 DPKVIVADEAVSALDVSIKAQVcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEI 546
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEI-YQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
344-552 |
1.26e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKttlRTMRRSVQMIFQD-PFASldpRMSVG 422
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQlPAAE---GMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 423 TAI-MEPFIEH----RLGtkQQAREKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:PRK10575 104 ELVaIGRYPWHgalgRFG--AADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 498 SIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIGPRAAV 552
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
325-497 |
1.27e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 325 DIRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSIT-RLIE--PTSGDVMLDGYEVLKLDKTTL---- 397
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILHVEQEVVGDDTTALqcvl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 398 -------RTMRRSVQMIFQD-----PFASLDPRMSVGTAIMEPFIEHRLGT---------KQQAREKAADLLEKVGLSPD 456
Cdd:PLN03073 257 ntdiertQLLEEEAQLVAQQrelefETETGKGKGANKDGVDKDAVSQRLEEiykrlelidAYTAEARAASILAGLSFTPE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 549799341 457 MMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
336-490 |
1.28e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 336 GAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLklDKTTLRTMRRSVQMIFQDpfASL 415
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMREAVAIVPEG--RRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 416 DPRMSVGTAI-MEPFIEHRlgtkQQAREKaadlLEKV-GLSPDMMRRFPHE---FSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PRK11614 92 FSRMTVEENLaMGGFFAER----DQFQER----IKWVyELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-246 |
2.88e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 47 PRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIegkVMLGGRDLLALPEEEMRKVrgkdismifqepmtslnpifpigkq 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDILEEVLDQLLLI------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 127 iaealtvhqdisssaakaevirllekvripnaknRFDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQ 206
Cdd:smart00382 53 ----------------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 549799341 207 ILDLIKT-----LQEEEGMSVLFITHDMGVVAE-----VSDRTIVMFRGD 246
Cdd:smart00382 99 LLLLEELrllllLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLIL 148
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
315-496 |
3.34e-08 |
|
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: 55.25 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 315 LSVKDLTTRFdirsglfgrkSGAVHAV-EKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEpTSGDVMLDGyevLKLD 393
Cdd:cd03289 3 MTVKDLTAKY----------TEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG---VSWN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 394 KTTLRTMRRSVQMIFQDPFASLDP-RMSvgtaiMEPFiehrlgtKQQAREKAADLLEKVGLSpDMMRRFPHE-------- 464
Cdd:cd03289 69 SVPLQKWRKAFGVIPQKVFIFSGTfRKN-----LDPY-------GKWSDEEIWKVAEEVGLK-SVIEQFPGQldfvlvdg 135
|
170 180 190
....*....|....*....|....*....|....*
gi 549799341 465 ---FSGGQRQRIAIARSLMLDPKVIVADEAVSALD 496
Cdd:cd03289 136 gcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
326-499 |
3.60e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 54.26 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 326 IRSGLFGRKSGaVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRR-SV 404
Cdd:cd03290 3 VTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 405 QMIFQDPF---ASLDPRMSVGTaimePFiehrlgTKQqaREKAadLLEKVGLSPDMmRRFPH-----------EFSGGQR 470
Cdd:cd03290 82 AYAAQKPWllnATVEENITFGS----PF------NKQ--RYKA--VTDACSLQPDI-DLLPFgdqteigergiNLSGGQR 146
|
170 180
....*....|....*....|....*....
gi 549799341 471 QRIAIARSLMLDPKVIVADEAVSALDVSI 499
Cdd:cd03290 147 QRICVARALYQNTNIVFLDDPFSALDIHL 175
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
313-555 |
5.97e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 313 PILSVKDLttrfdirsgLFGRKSGAVH-AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK 391
Cdd:PRK13545 20 PFDKLKDL---------FFRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 392 LDKTTLRTMRRSVQMIfqdpfaSLDPRMsvgtaimepfiehrLG-TKQQAREKAADLLEKVGLSpdmmrRFPHE----FS 466
Cdd:PRK13545 91 AISSGLNGQLTGIENI------ELKGLM--------------MGlTKEKIKEIIPEIIEFADIG-----KFIYQpvktYS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 467 GGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQvCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEI 546
Cdd:PRK13545 146 SGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK-CLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEY 224
|
....*....
gi 549799341 547 GPRAAVFDN 555
Cdd:PRK13545 225 GDIKEVVDH 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
312-547 |
7.84e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 312 TPILSVKDLTTRFDIRSGLFGrksgavhavekVSFDLAEGETLSLVGESGCGKSTTGRSITRliEP----TSGDVMLDGY 387
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKG-----------LNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 388 EVLKLDkTTLRTmRRSVQMIFQDPFASldPRMSvgtaiMEPFIEHRLGTKQQAREKA-----------ADLLEKVGLSPD 456
Cdd:CHL00131 72 SILDLE-PEERA-HLGIFLAFQYPIEI--PGVS-----NADFLRLAYNSKRKFQGLPeldplefleiiNEKLKLVGMDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 457 MMRRFPHE-FSGGQRQRIAIARSLMLDPKVIVADEAVSALDvsIKA-QVCNLLLDLQQNLNLAFLFISHDMAVVERVS-H 533
Cdd:CHL00131 143 FLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLD--IDAlKIIAEGINKLMTSENSIILITHYQRLLDYIKpD 220
|
250
....*....|....
gi 549799341 534 RVAVMYLGEIVEIG 547
Cdd:CHL00131 221 YVHVMQNGKIIKTG 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-289 |
9.51e-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: 55.40 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 11 TGGSVSPVLSVQNLTTSFrvDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTslsiMRLLDKKTSRIEGKVMLGGRDL 90
Cdd:TIGR01257 1930 SGGNKTDILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKSI 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 91 LAlpeeemrkvrgkDISMIFQEpmTSLNPIFpigKQIAEALTVHQDISSSAAKAEV-IRLLEKVRIPNAKN-----RFDD 164
Cdd:TIGR01257 2004 LT------------NISDVHQN--MGYCPQF---DAIDDLLTGREHLYLYARLRGVpAEEIEKVANWSIQSlglslYADR 2066
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 165 YPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFR 244
Cdd:TIGR01257 2067 LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVK 2145
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 549799341 245 GDVVETGTTDDIFHRGRHPYTRALlsavpKLGSMKERLLPARFPI 289
Cdd:TIGR01257 2146 GAFQCLGTIQHLKSKFGDGYIVTM-----KIKSPKDDLLPDLNPV 2185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-227 |
1.18e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTsfrVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSIMRLLDKKTSrieGKVMLGGRDL-LALPE 95
Cdd:PRK13539 1 MMLEGEDLAC---VRGG-RVLFSGLSFTLAAGEALVLTGPNGSGKT-TLLRLIAGLLPPAA---GTIKLDGGDIdDPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 96 EEMRKVRGKDismifqepmtSLNPifpigkqiaeALTVHQDISSSAAkaevIRLLEKVRIPNAKNRFD-----DYPHQF- 169
Cdd:PRK13539 73 EACHYLGHRN----------AMKP----------ALTVAENLEFWAA----FLGGEELDIAAALEAVGlaplaHLPFGYl 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMsVLFITH 227
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATH 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-259 |
1.34e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 41 MSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGGrDLLALPEEEMRKVRGKDISMIFQEPmtsLNPi 120
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKS----SLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSLRENILFGKA---LNE- 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 121 fPIGKQIAEALTVHQDIsssaakaEVIRLLEKVRIpnaknrfDDYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALD 200
Cdd:TIGR00957 728 -KYYQQVLEACALLPDL-------EILPSGDRTEI-------GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 201 VTIQGQILD-LIKTLQEEEGMSVLFITHDMGVVAEVsDRTIVMFRGDVVETGTTDDIFHR 259
Cdd:TIGR00957 793 AHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-232 |
1.43e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKVMLGgrDLLALPEEEMRKVRGKdISMIFQEPMT- 115
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSK-IGVVSQDPLLf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 116 -------------SLNPIFPIGKQIAEALTVHQDISSSAAK---------------------------------AEVIRL 149
Cdd:PTZ00265 473 snsiknnikyslySLKDLEALSNYYNEDGNDSQENKNKRNScrakcagdlndmsnttdsneliemrknyqtikdSEVVDV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 150 LEKVRIPNAKNRFDDY--------PHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMS 221
Cdd:PTZ00265 553 SKKVLIHDFVSALPDKyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
250
....*....|.
gi 549799341 222 VLFITHDMGVV 232
Cdd:PTZ00265 633 TIIIAHRLSTI 643
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-241 |
1.92e-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: 51.42 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 143 KAEVIRLLEKVRIPNAKNRFDD-----YPHQF---SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTL 214
Cdd:cd03222 38 KTTAVKILAGQLIPNGDNDEWDgitpvYKPQYidlSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
90 100
....*....|....*....|....*..
gi 549799341 215 QEEEGMSVLFITHDMGVVAEVSDRTIV 241
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
346-535 |
2.63e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 346 FDLAEGETLSLVGESGCGKSTtgrsitrLIEPTSGDVMLD-GYEVLKLDKTTLRtmrrsVQmifQDPfasldPRMSVGT- 423
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKST-------LMKILNGEVLLDdGRIIYEQDLIVAR-----LQ---QDP-----PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 ------------AIMEPF--IEHRLGT-------KQQAR--------------EKAADLLEKVGLSPDMMRRfphEFSGG 468
Cdd:PRK11147 84 ydfvaegieeqaEYLKRYhdISHLVETdpseknlNELAKlqeqldhhnlwqleNRINEVLAQLGLDPDAALS---SLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 469 QRQRIAIARSLMLDPKVIVADEAVSALDVSikaqvcnllldlQQNLNLAFL--------FISHDMAVVERVSHRV 535
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIE------------TIEWLEGFLktfqgsiiFISHDRSFIRNMATRI 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-547 |
2.69e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.70 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTtgrsitrLIE------PTSGDVMLDGYEVLKLDKTTLRtmrRSVQMIFQDPfaSLdP 417
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTS-------LLNallgflPYQGSLKINGIELRELDPESWR---KHLSWVGQNP--QL-P 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 418 RMSVGTAImepfiehRLGTKQQAREKAADLLEKVGLSpDMMRRFPH-----------EFSGGQRQRIAIARSLMLDPKVI 486
Cdd:PRK11174 436 HGTLRDNV-------LLGNPDASDEQLQQALENAWVS-EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799341 487 VADEAVSALDVSIKAQVcnLLLDLQQNLNLAFLFISHDMAVVERVShRVAVMYLGEIVEIG 547
Cdd:PRK11174 508 LLDEPTASLDAHSEQLV--MQALNAASRRQTTLMVTHQLEDLAQWD-QIWVMQDGQIVQQG 565
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
332-547 |
2.81e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 332 GRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGyEVlkldkttlrtmrrSVQMIfqdp 411
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EV-------------SVIAI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 412 FASLDPRMSvGTAIMEpFIEHRLGTKQQAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:PRK13546 93 SAGLSGQLT-GIENIE-FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 492 VSALDVSIkAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMYLGEIVEIG 547
Cdd:PRK13546 171 LSVGDQTF-AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
326-554 |
3.34e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 326 IRSGLFGRKSGAVHAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVmldgyevlkldkttlrTMRRSVQ 405
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------------HMKGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 406 MIFQDPF---ASLDPRMSVGTAIMEPFIehrlgtkqQAREKAADLLEKVGLSPDMMRRFPHE----FSGGQRQRIAIARS 478
Cdd:TIGR00957 703 YVPQQAWiqnDSLRENILFGKALNEKYY--------QQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARA 774
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799341 479 LMLDPKVIVADEAVSALDVSIKAQVCNLLL-DLQQNLNLAFLFISHDMAVVERVSHrVAVMYLGEIVEIGPRAAVFD 554
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAHVGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELLQ 850
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
341-497 |
3.44e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 341 VEKVSFDLAEGETLSLVGESGCGKSTTGRSIT--------RLIEPTSGDVmldgYEVLKLDKTTLRTMRRsvQMIFqdPF 412
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKL----FYVPQRPYMTLGTLRD--QIIY--PD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 413 ASLDPRM-SVGTAIMEPFIEHRlgtkqqareKAADLLEKVGlSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEA 491
Cdd:TIGR00954 540 SSEDMKRrGLSDKDLEQILDNV---------QLTHILEREG-GWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
....*.
gi 549799341 492 VSALDV 497
Cdd:TIGR00954 610 TSAVSV 615
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
136-243 |
4.03e-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: 51.60 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 136 DISSSAAKAEVIRLLEKVripNAKNRFDDYPHQ-------------FSGGMRQRVMIAMALASKPKLLIADEPTTALDVt 202
Cdd:cd03236 97 DLIPKAVKGKVGELLKKK---DERGKLDELVDQlelrhvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDI- 172
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 549799341 203 iqGQILDLIKTLQE--EEGMSVLFITHDMGVVAEVSDRTIVMF 243
Cdd:cd03236 173 --KQRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
170-254 |
4.50e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDV-- 247
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNGLVag 471
|
....*...
gi 549799341 248 -VETGTTD 254
Cdd:PRK10982 472 iVDTKTTT 479
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-503 |
5.19e-07 |
|
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: 50.24 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKST-----TGRsitRLIEPTSGDVMLDGYevlkldKTTLRTMRRSVQMIFQDPFasLDPR 418
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTllnalAGR---RTGLGVSGEVLINGR------PLDKRSFRKIIGYVPQDDI--LHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 MSVgtaimepfiehrlgtkQQAREKAADLLekvGLSpdmmrrfphefsGGQRQRIAIARSLMLDPKVIVADEAVSALDVS 498
Cdd:cd03213 97 LTV----------------RETLMFAAKLR---GLS------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
....*
gi 549799341 499 IKAQV 503
Cdd:cd03213 146 SALQV 150
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
304-547 |
6.32e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 304 KDTVSGGRTPILSVKDLTTRFdirsglfgrksGAVHAVEKVSFDLAEGETLSLVGESGCGKSTtGRSITRLIEPTSGDVM 383
Cdd:NF000106 3 RKTISNGARNAVEVRGLVKHF-----------GEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 384 LDGYEVLKLDKTTLRTM--RRSVQMIFQDPFASLDPRMSVGTAIMEpfiehrlgTKQQAREKAADLLEKVGLSpDMMRRF 461
Cdd:NF000106 71 WRF*TWCANRRALRRTIg*HRPVR*GRRESFSGRENLYMIGR*LDL--------SRKDARARADELLERFSLT-EAAGRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 462 PHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHdMAVVERVSHRVAVMYLG 541
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY-MEEAEQLAHELTVIDRG 220
|
....*.
gi 549799341 542 EIVEIG 547
Cdd:NF000106 221 RVIADG 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
36-229 |
1.02e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 36 SVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKktsrIEGKVMLGGRDLLALPEEEMRKVRGKDISMIFQEP-- 113
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT----LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPwl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 114 ---MTSLNPIF--PIGKQIAEALTvhqDISSSAAKAEVIRLLEKVRIpnaknrfDDYPHQFSGGMRQRVMIAMALASKPK 188
Cdd:cd03290 91 lnaTVEENITFgsPFNKQRYKAVT---DACSLQPDIDLLPFGDQTEI-------GERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 549799341 189 LLIADEPTTALDVTIQGQILD--LIKTLQEEEgMSVLFITHDM 229
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-539 |
1.25e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 349 AEGETLSLVGESGCGKSTTGR--------SITRLIEPTSGDVMLDGYEVLKLDKTTLRTMRRSVQMIFQDPFASLDPRMS 420
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKilagklkpNLGKFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 421 VGTAImepfiehRLGTKQQAREKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS-- 498
Cdd:cd03236 104 KGKVG-------ELLKKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqr 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 549799341 499 IKAqvcNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMY 539
Cdd:cd03236 176 LNA---ARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-260 |
1.35e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 17 PVLSVQNLTTSFRVDGGwKSVVRNMSFEIAPRETVAIVGESGSGKsvTSLsIMRLLDKKTSRIEGKVMLGGRdLLALPEe 96
Cdd:PLN03130 613 PAISIKNGYFSWDSKAE-RPTLSNINLDVPVGSLVAIVGSTGEGK--TSL-ISAMLGELPPRSDASVVIRGT-VAYVPQ- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 97 emrkvrgkdISMIFQEpmtslnpifpigkqiaealTVHQDISSsAAKAEVIRLLEKVRIPNAKNRFDDYPH--------- 167
Cdd:PLN03130 687 ---------VSWIFNA-------------------TVRDNILF-GSPFDPERYERAIDVTALQHDLDLLPGgdlteiger 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 --QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDliKTLQEE-EGMSVLFITHDMGVVAEVsDRTIVMFR 244
Cdd:PLN03130 738 gvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHE 814
|
250
....*....|....*.
gi 549799341 245 GDVVETGTTDDIFHRG 260
Cdd:PLN03130 815 GMIKEEGTYEELSNNG 830
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
168-497 |
1.61e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVT----IQGQILDLIKTL------QEEEGMSVLFITHDMGvvaevsd 237
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKWPKTFivvshaREFLNTVVTDILHLHG------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 238 RTIVMFRGDVvetgttdDIFHRGRHPY-------------TRALLSA-VPKLGSMKER--LLPARFPIIDIKTGESQPVA 301
Cdd:PLN03073 417 QKLVTYKGDY-------DTFERTREEQlknqqkafesnerSRSHMQAfIDKFRYNAKRasLVQSRIKALDRLGHVDAVVN 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 302 D--------VKDTVSGGrtPILSVKDLTtrfdirsglFGRKSGAVhAVEKVSFDLAEGETLSLVGESGCGKSTTGRSITR 373
Cdd:PLN03073 490 DpdykfefpTPDDRPGP--PIISFSDAS---------FGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 374 LIEPTSGdvmldgyevlkldkTTLRTMRRSVQMIFQDPFASLDPRMSVGTAIMEPFIehrlGTKQQareKAADLLEKVGL 453
Cdd:PLN03073 558 ELQPSSG--------------TVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFP----GVPEQ---KLRAHLGSFGV 616
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 549799341 454 SPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:PLN03073 617 TGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
340-503 |
1.69e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.88 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLK-LDKTTLRTMRRSVQMIFQDPFASLDPR 418
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 419 MsVGTAIMEPFIEHrlgTKQQAREKAADLLEKVGLSpDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS 498
Cdd:PRK15056 102 M-MGRYGHMGWLRR---AKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
....*
gi 549799341 499 IKAQV 503
Cdd:PRK15056 177 TEARI 181
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-254 |
1.70e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 27 SFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLS-IMRLLDKKtsriEGKVMLGGRDLLALPEEEMRKvrgkD 105
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSlIQRHFDVS----EGDIRFHDIPLTKLQLDSWRS----R 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 106 ISMIFQEPM----TSLNPIfPIGK------QIAEAL---TVHQDIsssaakaevirllekVRIPNAknrfddYPHQ---- 168
Cdd:PRK10789 391 LAVVSQTPFlfsdTVANNI-ALGRpdatqqEIEHVArlaSVHDDI---------------LRLPQG------YDTEvger 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 ---FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKtlQEEEGMSVLFITHDMGVVAEvSDRTIVMFRG 245
Cdd:PRK10789 449 gvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHG 525
|
....*....
gi 549799341 246 DVVETGTTD 254
Cdd:PRK10789 526 HIAQRGNHD 534
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-256 |
1.71e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 29 RVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVTSlsimRLLDKKTSRIEGKV-MLGGRDLLAlpeeemrkvrgkdIS 107
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLS----NLIAGVTMPNKGTVdIKGSAALIA-------------IS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 108 MIFQEPMTSLNPIfpigkqiaEALTVHQDISSSAAKAEVIRLLEKVRIpnakNRFDDYP-HQFSGGMRQRVMIAMALASK 186
Cdd:PRK13545 94 SGLNGQLTGIENI--------ELKGLMMGLTKEKIKEIIPEIIEFADI----GKFIYQPvKTYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 187 PKLLIADEPTTALDVTIQGQILDLIKTLQEEeGMSVLFITHDMGVVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
170-248 |
2.45e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 2.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
351-498 |
2.91e-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: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVLKLdktTLRTMRRSVQMIFQDPFA-------SLDPRmsvgt 423
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPILfsgsirfNLDPE----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 424 aimepfiehrlgtKQQAREKAADLLEKVGLSpDMMRRFP-----------HEFSGGQRQRIAIARSLMLDPKVIVADEAV 492
Cdd:cd03288 119 -------------CKCTDDRLWEALEIAQLK-NMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
....*.
gi 549799341 493 SALDVS 498
Cdd:cd03288 185 ASIDMA 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
169-500 |
4.05e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 169 FSGGMRQRVMIAMALASKPKLLIADEPTTALDVTiqgQILDLIKTLQEEEGMSVLfITHDMGVVAEVSDRTIVMFRGDVV 248
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLIL-ISHDRDFLDPIVDKIIHIEQQSLF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 249 E-TGT----------------------TDDIFH------RGRHPYTRA--LLSAVPKLGSMkERLLPA------RFpiiD 291
Cdd:PRK10636 226 EyTGNyssfevqratrlaqqqamyesqQERVAHlqsyidRFRAKATKAkqAQSRIKMLERM-ELIAPAhvdnpfHF---S 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 292 IKTGESQPvadvkdtvsggrTPILSVKDLTTRFDIRSGLfgrksgavhavEKVSFDLAEGETLSLVGESGCGKSTTGRSI 371
Cdd:PRK10636 302 FRAPESLP------------NPLLKMEKVSAGYGDRIIL-----------DSIKLNLVPGSRIGLLGRNGAGKSTLIKLL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 372 TRLIEPTSGDVMLD-----GY------EVLKLDKTTLRTMRRsvqmifqdpfasLDPRMsvgtaimepfiehrlgTKQQA 440
Cdd:PRK10636 359 AGELAPVSGEIGLAkgiklGYfaqhqlEFLRADESPLQHLAR------------LAPQE----------------LEQKL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 441 RekaaDLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIK 500
Cdd:PRK10636 411 R----DYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-245 |
4.11e-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: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 44 EIAPRETVAIVGESGSGKSvtslSIMRLLDKKTSRIEGKvmlggrdllalPEEEMRKVRGKDISMIFQEPMTSLNPIFPI 123
Cdd:cd03237 21 SISESEVIGILGPNGIGKT----TFIKMLAGVLKPDEGD-----------IEIELDTVSYKPQYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 124 gkqIAEALTVHQDISSSAAKAEVIRLLEKvRIPNaknrfddyphqFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTI 203
Cdd:cd03237 86 ---TKDFYTHPYFKTEIAKPLQIEQILDR-EVPE-----------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 549799341 204 QGQILDLIKTLQEEEGMSVLFITHDMGVVAEVSDRTIVmFRG 245
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEG 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
340-490 |
8.62e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 340 AVEKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVlklDKTTLRTMRRSVQMIFQD--PFASL-- 415
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLFSAVFTDfhLFDQLlg 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799341 416 DPRMSVGTAIMEPFIEhRLGTKQQAREKAADLLEKvglspdmmrrfphEFSGGQRQRIAIARSLMLDPKVIVADE 490
Cdd:PRK10522 415 PEGKPANPALVEKWLE-RLKMAHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
170-251 |
9.61e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIA--MALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVaEVSDRTIVM----- 242
Cdd:cd03238 89 SGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLI-DLGNTVILIEHNLDVL-SSADWIIDFgpgsg 166
|
90
....*....|
gi 549799341 243 -FRGDVVETG 251
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-538 |
1.40e-05 |
|
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: 45.13 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 342 EKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVmldgyevlkldkttlrtmrrsvqmifqdpfaSLDPRMSV 421
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------------------TWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 GTaimepfiehrlgtkqqarekaadllekvglspdmmrrFPHeFSGGQRQRIAIARSLMLDPKVIVADE--------AVS 493
Cdd:cd03221 66 GY-------------------------------------FEQ-LSGGEKMRLALAKLLLENPNLLLLDEptnhldleSIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 549799341 494 ALDVSIKAQvcnllldlqqnlNLAFLFISHDMAVVERVSHRVAVM 538
Cdd:cd03221 108 ALEEALKEY------------PGTVILVSHDRYFLDQVATKIIEL 140
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
131-256 |
1.62e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.20 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 131 LTVHQ---------DISSSAAKAEVIRLLEkvripnaknRFD--DYPHQFSG----GMRQRVMIAMALASKPKLLIADEP 195
Cdd:NF033858 354 LTVRQnlelharlfHLPAAEIAARVAEMLE---------RFDlaDVADALPDslplGIRQRLSLAVAVIHKPELLILDEP 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 196 TTALDVTIQGQILDLIKTLQEEEGMSVlFI-THDMGvVAEVSDRTIVMFRGDVVETGTTDDI 256
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTI-FIsTHFMN-EAERCDRISLMHAGRVLASDTPAAL 484
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-498 |
1.78e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTS--GDVMLDGyevlklDKTTLRTMRRSvQMIFQDPFasLDPRMSV-GTAIME 427
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN------RKPTKQILKRT-GFVTQDDI--LYPHLTVrETLVFC 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 428 PFIE-HRLGTKQQAREKAADLLEKVGLSP----DMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS 498
Cdd:PLN03211 165 SLLRlPKSLTKQEKILVAESVISELGLTKcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-243 |
2.02e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 8 MEQTGGSVSPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSVtslsimrLLDKKTSRIE-----GK 82
Cdd:PLN03211 54 MKNKGSNIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKST-------LLNALAGRIQgnnftGT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 83 VMLGGRDLLALPEEEMRKVRGKDIsmIFQEPMTSLNPIFPIGKQIAEALTvhQDISSSAAKAEVIRL-LEKVRIPNAKNR 161
Cdd:PLN03211 127 ILANNRKPTKQILKRTGFVTQDDI--LYPHLTVRETLVFCSLLRLPKSLT--KQEKILVAESVISELgLTKCENTIIGNS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 162 FddyPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHdmgvvaEVSDRTIV 241
Cdd:PLN03211 203 F---IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMH------QPSSRVYQ 272
|
..
gi 549799341 242 MF 243
Cdd:PLN03211 273 MF 274
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
53-228 |
2.15e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 53 IVGESGSGKSvTSLSIMRLLDKKtsrIEGKVMLG-GRDLLALPEE----EMRKVRG----------------KDISMIFQ 111
Cdd:PRK11819 38 VLGLNGAGKS-TLLRIMAGVDKE---FEGEARPApGIKVGYLPQEpqldPEKTVREnveegvaevkaaldrfNEIYAAYA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 112 EPMTSLNpifpigkQIAEALTVHQDISSSAAKAEVIRLLEK----VRIPNaknrfDDYP-HQFSGGMRQRVMIAMALASK 186
Cdd:PRK11819 114 EPDADFD-------ALAAEQGELQEIIDAADAWDLDSQLEIamdaLRCPP-----WDAKvTKLSGGERRRVALCRLLLEK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 549799341 187 PKLLIADEPTTALDVTiqgQILDLIKTLQEEEGmSVLFITHD 228
Cdd:PRK11819 182 PDMLLLDEPTNHLDAE---SVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
170-260 |
2.78e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILD-LIKtlQEEEGMSVLFITHDMGVVAEVsDRTIVMFRGDVV 248
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMK--DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
90
....*....|..
gi 549799341 249 ETGTTDDIFHRG 260
Cdd:PLN03232 819 EEGTFAELSKSG 830
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-228 |
3.36e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.85 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 18 VLSVQNLTTSFrvdgGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLL------DKKTSRIEGKVMLGGRDll 91
Cdd:TIGR03719 322 VIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKS----TLFRMItgqeqpDSGTIEIGETVKLAYVD-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 92 alpeeEMRKvrgkdismifqepmtSLNPifpiGKqiaealTVHQDISSSAakaEVIRLlEKVRIPNAK--NRFD------ 163
Cdd:TIGR03719 392 -----QSRD---------------ALDP----NK------TVWEEISGGL---DIIKL-GKREIPSRAyvGRFNfkgsdq 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799341 164 -DYPHQFSGGMRQRVMIAMALASKPKLLIADEPTTALDVtiqgqildliKTLQE-EEGM-----SVLFITHD 228
Cdd:TIGR03719 438 qKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----------ETLRAlEEALlnfagCAVVISHD 499
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
466-497 |
5.50e-05 |
|
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: 44.38 E-value: 5.50e-05
10 20 30
....*....|....*....|....*....|..
gi 549799341 466 SGGQRQRIAIARSLMLDPKVIVADEAVSALDV 497
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-245 |
1.06e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 13 GSVSPVLSVQNLTTSFRVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvTSLSImrLLDKKTSRI--EGKVMLGGRDL 90
Cdd:TIGR00956 754 ESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKT-TLLNV--LAERVTTGVitGGDRLVNGRPL 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 91 LALPEEEMRKVRGKDISMifqepmtslnpifpigkqiaEALTVHQDISSSAA--------KAE-------VIRLLEkvri 155
Cdd:TIGR00956 831 DSSFQRSIGYVQQQDLHL--------------------PTSTVRESLRFSAYlrqpksvsKSEkmeyveeVIKLLE---- 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 156 pnaknrFDDYPHQFSG----GM----RQRVMIAMALASKPKLLI-ADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFIT 226
Cdd:TIGR00956 887 ------MESYADAVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTI 959
|
250 260
....*....|....*....|
gi 549799341 227 HD-MGVVAEVSDRTIVMFRG 245
Cdd:TIGR00956 960 HQpSAILFEEFDRLLLLQKG 979
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-227 |
1.20e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.12 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 37 VVRNMSFEIAPRETVAIVGESGSGKSvtslSIMRLLdkktsrieGKV--MLGGRdlLALPEEemrkvrGKdISMIFQEPM 114
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKS----SLFRIL--------GELwpVYGGR--LTKPAK------GK-LFYVPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 TSLNPIfpiGKQIAEALTVHQDISSSAAKAEVIRLLEKVRIPNAKNR---FD---DYPHQFSGGMRQRVMIAMALASKPK 188
Cdd:TIGR00954 526 MTLGTL---RDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReggWSavqDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 549799341 189 LLIADEPTTALDVTIQGQILDLIKtlqeEEGMSVLFITH 227
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-245 |
1.27e-04 |
|
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: 43.61 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 19 LSVQNLTTSF-RVDGGWKSVVRNMSFEIAPRETVAIVGESGSGKSvtSLsIMRLLdKKTSRIEGKVMLGGRdllalpeee 97
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKS--SL-LSALL-GELEKLSGSVSVPGS--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 98 mrkvrgkdISMIFQEPM---TSL--NPIFpiGKQIAE----------ALTvhQDISSSAA--KAEV----IRLlekvrip 156
Cdd:cd03250 68 --------IAYVSQEPWiqnGTIreNILF--GKPFDEeryekvikacALE--PDLEILPDgdLTEIgekgINL------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 157 naknrfddyphqfSGGMRQRVMIAMALASKPKLLIADEPTTALDV---------TIQGQILDLiKTlqeeegmsVLFITH 227
Cdd:cd03250 129 -------------SGGQKQRISLARAVYSDADIYLLDDPLSAVDAhvgrhifenCILGLLLNN-KT--------RILVTH 186
|
250
....*....|....*...
gi 549799341 228 DMGVVAEVsDRTIVMFRG 245
Cdd:cd03250 187 QLQLLPHA-DQIVVLDNG 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
176-228 |
1.41e-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: 43.36 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDV-TIQGQILDLIKTLQEEEGMSVLFITHD 228
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
167-242 |
1.47e-04 |
|
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: 42.73 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 167 HQFSGGMRQRVMIAMALAS---KPK-LLIADEPTTALDVTIQGQILDLIK-TLQeeEGMSVLFITHDMGvVAEVSDRTIV 241
Cdd:cd03227 76 LQLSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILeHLV--KGAQVIVITHLPE-LAELADKLIH 152
|
.
gi 549799341 242 M 242
Cdd:cd03227 153 I 153
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
170-252 |
1.48e-04 |
|
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: 43.76 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 170 SGGMRQRVMIAMAL---ASKPKLLIADEPTTAL---DVTiqgQILDLIKTLQeEEGMSVLFITHDMGVVAeVSDRTIVM- 242
Cdd:cd03271 171 SGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDVK---KLLEVLQRLV-DKGNTVVVIEHNLDVIK-CADWIIDLg 245
|
90
....*....|....*
gi 549799341 243 -----FRGDVVETGT 252
Cdd:cd03271 246 peggdGGGQVVASGT 260
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
170-240 |
1.64e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 170 SGGMRQRVMIAMALAS---KPKLLIADEPTTALDVTiqgQILDLIKTLQE--EEGMSVLFITHDMGVVaEVSDRTI 240
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTH---DIKALIYVLQSltHQGHTVVIIEHNMHVV-KVADYVL 882
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
344-389 |
2.45e-04 |
|
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: 44.02 E-value: 2.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEV 389
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
441-542 |
3.76e-04 |
|
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: 43.62 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 441 REKAADLLEKVGLSPdMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS--IKAqvcNLLLDLQQNLNLAF 518
Cdd:COG1245 190 RGKLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrLNV---ARLIRELAEEGKYV 265
|
90 100
....*....|....*....|....
gi 549799341 519 LFISHDMAVVERVSHRVAVMYlGE 542
Cdd:COG1245 266 LVVEHDLAILDYLADYVHILY-GE 288
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
344-547 |
4.44e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 344 VSFDLAEGETLSLVGESGCGKSTTGRSIT--RLIEPTSGDVMLDGYEVLKLDKTtlRTMRRSVQMIFQDPFASldPRMSv 421
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPE--DRAGEGIFMAFQYPVEI--PGVS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 422 gtaiMEPFIEHRLGTKQQAREKA-------ADLLEK----VGLSPDMMRRFPHE-FSGGQRQRIAIARSLMLDPKVIVAD 489
Cdd:PRK09580 95 ----NQFFLQTALNAVRSYRGQEpldrfdfQDLMEEkialLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 490 EAVSALDVSiKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVS-HRVAVMYLGEIVEIG 547
Cdd:PRK09580 171 ESDSGLDID-ALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
464-539 |
8.02e-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: 40.63 E-value: 8.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799341 464 EFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQVCNLLLDLQQNLNLAFLFISHDMAVVERVSHRVAVMY 539
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-497 |
9.90e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 342 EKVSFDLAEGETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDGYEVL-KL--------DKTTLRT-MRRSVQM----- 406
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLgKLrqdqfafeEFTVLDTvIMGHTELwevkq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 407 ----IFQDPFASLDPRMSVGTAIMEpFIEHRlGTKQQARekAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLD 482
Cdd:PRK15064 98 erdrIYALPEMSEEDGMKVADLEVK-FAEMD-GYTAEAR--AGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSN 173
|
170
....*....|....*
gi 549799341 483 PKVIVADEAVSALDV 497
Cdd:PRK15064 174 PDILLLDEPTNNLDI 188
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
170-232 |
1.03e-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: 42.31 E-value: 1.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 170 SGGMRQRVMIAMALASK---PKLLIADEPTTAL---DVTiqgQILDLIKTLQeEEGMSVLFITHDMGVV 232
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK---KLLEVLQRLV-DKGNTVVVIEHNLDVI 895
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
351-537 |
1.11e-03 |
|
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: 39.66 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTSGDVMldgyeVLKLDKTTLRTMRRSVQMIFqdpfasldprmsvgtaimepfi 430
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-----YIDGEDILEEVLDQLLLIIV---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 431 ehrlgtkqqarekaadllekvglspdmmRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDVS-----IKAQVCN 505
Cdd:smart00382 55 ----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELR 106
|
170 180 190
....*....|....*....|....*....|....*...
gi 549799341 506 LLLDLQQNLNLAFLFISH------DMAVVERVSHRVAV 537
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVL 144
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
441-542 |
1.16e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 441 REKAADLLEKVGLSPDMMRRFpHEFSGGQRQRIAIARSLMLDPKVIVADEAVSALDvsIKAQVCNLLLDLQQNLNLAFLF 520
Cdd:PRK13409 190 RGKLDEVVERLGLENILDRDI-SELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNVARLIRELAEGKYVLV 266
|
90 100
....*....|....*....|..
gi 549799341 521 ISHDMAVVERVSHRVAVMYlGE 542
Cdd:PRK13409 267 VEHDLAVLDYLADNVHIAY-GE 287
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
168-256 |
1.29e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQeEEGMSVLFITHDMGVVAEVSDRTIVMFRGDV 247
Cdd:PRK13546 143 KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
....*....
gi 549799341 248 VETGTTDDI 256
Cdd:PRK13546 222 KDYGELDDV 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
466-503 |
1.68e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|....*...
gi 549799341 466 SGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQV 503
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
354-436 |
1.77e-03 |
|
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.
Pssm-ID: 238984 [Multi-domain] Cd Length: 273 Bit Score: 40.78 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 354 LSLVGESGCGKSTTGRSITRL-IEPTSGDVMLDGYevLKLDkttlRTMRRSVQMIFQDPFASLDPRMS-------VGTAI 425
Cdd:cd02026 2 IGVAGDSGCGKSTFLRRLTSLfGSDLVTVICLDDY--HSLD----RKGRKETGITALDPRANNFDLMYeqlkalkEGQAI 75
|
90
....*....|.
gi 549799341 426 MEPFIEHRLGT 436
Cdd:cd02026 76 EKPIYNHVTGL 86
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
170-228 |
3.05e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 3.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 549799341 170 SGGMRQRVMIAMALASKPKLLIADEPTTALDVtiqgQILDLIKTLQEEEGMSVLFITHD 228
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-254 |
3.84e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 35 KSVVRNMSFEIAPRETVAIVGESGSGKSVTSLSIMRLLDKKTSRIEGKVMLGGrdllaLPEEEMRKVRGKDISMIFQepm 114
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDG-----ITPEEIKKHYRGDVVYNAE--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 115 tsLNPIFPIgkqiaeaLTVHQDISSSAA-KAEVIRLLEKVRIPNAKNRFD------------------DYPHQFSGGMRQ 175
Cdd:TIGR00956 146 --TDVHFPH-------LTVGETLDFAARcKTPQNRPDGVSREEYAKHIADvymatyglshtrntkvgnDFVRGVSGGERK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 176 RVMIAMALASKPKLLIADEPTTALDVTIQGQILDLIKTLQEEEGMSVLFITHDMGVVA-EVSDRTIVMFRGDVVETGTTD 254
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAyELFDKVIVLYEGYQIYFGPAD 296
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
354-436 |
4.37e-03 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 39.61 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 354 LSLVGESGCGKSTTGRSITRLIEPtsgDVM----LDGYEvlKLDkttlRTMRRsvqmifQDPFASLDPR----------- 418
Cdd:PRK07429 11 LGVAGDSGCGKTTFLRGLADLLGE---ELVtvicTDDYH--SYD----RKQRK------ELGITALDPRannldimyehl 75
|
90 100
....*....|....*....|
gi 549799341 419 --MSVGTAIMEPFIEHRLGT 436
Cdd:PRK07429 76 kaLKTGQPILKPIYNHETGT 95
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
351-497 |
5.63e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 351 GETLSLVGESGCGKSTTGRSITRLIEPTSGDVMLDG--------YEVLKLDKTTLRTM------RRSVQMIFQDPFASLD 416
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEYVidgdreYRQLEAQLHDANERND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799341 417 prmsvGTAIMEpfIEHRLGTKQ--QAREKAADLLEKVGLSPDMMRRFPHEFSGGQRQRIAIARSLMLDPKVIVADEAVSA 494
Cdd:PRK10636 107 -----GHAIAT--IHGKLDAIDawTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
...
gi 549799341 495 LDV 497
Cdd:PRK10636 180 LDL 182
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
168-237 |
6.13e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 6.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799341 168 QFSGGMRQRVMIAMALASKPKLLIADEPTTALDvtiqgqiLDLIKTLQEE----EGMSVLfITHDMGVVAEVSD 237
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-------LDMRQALTEAlidfEGALVV-VSHDRHLLRSTTD 495
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
466-503 |
7.61e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 7.61e-03
10 20 30
....*....|....*....|....*....|....*...
gi 549799341 466 SGGQRQRIAIARSLMLDPKVIVADEAVSALDVSIKAQV 503
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
|
|