|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-623 |
0e+00 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 1201.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 1 MPHSDELDAGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL 80
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 81 RRRSRDVIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQT 160
Cdd:PRK10261 81 RRRSRQVIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
Cdd:PRK10261 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 241 VMYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAPPIEQKTVVDGEPVLRVRNLV 320
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 321 TRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR 400
Cdd:PRK10261 321 TRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 401 RDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALAL 480
Cdd:PRK10261 401 RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 561 RKLLAAVPVAEPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR 623
Cdd:PRK10261 561 RKLMAAVPVADPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR 623
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-571 |
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: 843.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcDKMLLRrrSRDVIEL 90
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPS-GSILFD--GQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLS 170
Cdd:COG4172 82 SE---RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 251 GTVEQIFHAPQHPYTRALLAAVPQLgamkgldyprrfplislehpakQAPPIEQktvvDGEPVLRVRNLVTRFPLRSGLL 330
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAAEPRG----------------------DPRPVPP----DAPPLLEARDLKVWFPIKRGLF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDP 410
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLRRRMQVVFQDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 411 YASLDPRQTIGDSIIEPLRVHGL-LPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:COG4172 372 FGSLSPRMTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPV 569
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
..
gi 1134749654 570 AE 571
Cdd:COG4172 532 LE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-573 |
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: 717.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdKMLLRRRSRDVIELS 91
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI----SGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQsaaqmrhVRGADMAMIFQEPMTSLNPVfTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171
Cdd:COG1123 78 EA-------LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 252 TVEQIFHAPQhpytraLLAAVPQLGAMKGLDYPRRfplislehpakqappieqktvVDGEPVLRVRNLVTRFPLRSGlln 331
Cdd:COG1123 226 PPEEILAAPQ------ALAAVPRLGAARGRAAPAA---------------------AAAEPLLEVRNLSKRYPVRGK--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 332 rvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPY 411
Cdd:COG1123 276 ---GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 412 ASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:COG1123 353 SSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPT 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVAE 571
Cdd:COG1123 433 SALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLD 512
|
..
gi 1134749654 572 PS 573
Cdd:COG1123 513 PA 514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-565 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 560.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrdVIELSE 92
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGES--LLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QsaaQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGG 172
Cdd:PRK15134 84 Q---TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 253 VEQIFHAPQHPYTRALLAAvpqlgamkgldyprrfplisleHPAKQAPPIEQktvvDGEPVLRVRNLVTRFPLRSGLLNR 332
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNS----------------------EPSGDPVPLPE----PASPLLDVEQLQVAFPIRKGILKR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 333 VTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYA 412
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 SLDPRQTIGDSIIEPLRVH-GLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLA 565
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
309-612 |
7.20e-175 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 499.26 E-value: 7.20e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 309 DGEPVLRVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 389 DTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 549 RAVFENPQHPYTRKLLAAVPVAEPSRQRpQRVLLSDDLPSNI--------HLR---GEEVAAVS---LQCVGPGHYVA 612
Cdd:COG4608 243 DELYARPLHPYTQALLSAVPVPDPERRR-ERIVLEGDVPSPLnppsgcrfHTRcpyAQDRCATEeppLREVGPGHQVA 319
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-301 |
8.18e-148 |
|
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: 429.86 E-value: 8.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE---QAGGlvqcdKMLLRrrSRDVI 88
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSG-----EILFD--GEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 ELSEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
Cdd:COG0444 74 KLSE---KELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 249 ETGTVEQIFHAPQHPYTRALLAAVPQLGAMKgldypRRFPLISLEHPAKQAPP 301
Cdd:COG0444 231 EEGPVEELFENPRHPYTRALLSSIPRLDPDG-----RRLIPIPGEPPSLLNPP 278
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
313-612 |
6.44e-147 |
|
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: 427.55 E-value: 6.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG---GEIIFNGQRID 389
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 TLSPGKLQALR-RDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLP--EHAWRYPHEFSG 466
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 547 PRRAVFENPQHPYTRKLLAAVPVAEPSRQRpqRVLLSDDLPSNIHL-----------------RGEEVAavsLQCVGPGH 609
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPDGRR--LIPIPGEPPSLLNPpsgcrfhprcpyamdrcREEEPP---LREVGPGH 308
|
...
gi 1134749654 610 YVA 612
Cdd:COG0444 309 RVA 311
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
309-588 |
8.46e-116 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 348.49 E-value: 8.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 309 DGEPVLRVRNLVTRFPLRSGLLnRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 389 DTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1134749654 549 RAVFENPQHPYTRKLLAAVPVAEPSRQRPqRVLLSDDLPS 588
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPRLNPDDRRE-RIKLTGELPS 278
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
313-546 |
8.28e-113 |
|
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: 336.79 E-value: 8.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWL-LERVGLLPEHAWRYPHEFSGGQRQR 471
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
306-590 |
5.83e-112 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 338.60 E-value: 5.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 306 TVVDGEPVLRVRNLVTRFPLRSG--LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF 383
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 384 NGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRV-HGLLPGKEAVARVAWLLERVGLLPEHAWRYPH 462
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1134749654 543 VEIGPRRAVFENPQHPYTRKLLAAVPVAEPSRQRPQRV-LLSDDLPSNI 590
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqLLEGELPSPI 289
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-277 |
2.76e-109 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 331.69 E-value: 2.76e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrRSRDVIEL 90
Cdd:PRK09473 11 ALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATF----NGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEqsaAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLS 170
Cdd:PRK09473 87 PE---KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260
....*....|....*....|....*..
gi 1134749654 251 GTVEQIFHAPQHPYTRALLAAVPQLGA 277
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGLLNAVPRLDA 270
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-251 |
2.33e-108 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 325.61 E-value: 2.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRDVIELS 91
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-------IFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQsaaqMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMvEAKRMLDQVRIPEAQTILSRYPHQLSG 171
Cdd:cd03257 74 RR----LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEAR-KEAVLLLLVGVGLPEEVLNRYPHELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
309-586 |
2.33e-106 |
|
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: 331.26 E-value: 2.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 309 DGEPVLRVRNLVTRFplRSGllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ----GGEIIFN 384
Cdd:COG4172 2 MSMPLLSVEDLSVAF--GQG-----GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 385 GQRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLlPEHAWR---Y 460
Cdd:COG4172 75 GQDLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERRldaY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1134749654 541 QIVEIGPRRAVFENPQHPYTRKLLAAVPVAEPSRQRP-QRVLLS-DDL 586
Cdd:COG4172 234 EIVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPdAPPLLEaRDL 281
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
314-568 |
8.19e-104 |
|
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: 314.43 E-value: 8.19e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSP 393
Cdd:COG1124 2 LEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLpgkEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRIC 473
Cdd:COG1124 72 RRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*
gi 1134749654 554 NPQHPYTRKLLAAVP 568
Cdd:COG1124 229 GPKHPYTRELLAASL 243
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
311-566 |
3.97e-99 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 303.30 E-value: 3.97e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGLLNRvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidt 390
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
Cdd:COG4167 77 LEYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*.
gi 1134749654 551 VFENPQHPYTRKLLAA 566
Cdd:COG4167 237 VFANPQHEVTKRLIES 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-279 |
3.62e-97 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 300.51 E-value: 3.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlVQCDKmlLRRRSRDVIELS 91
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGR-VMAEK--LEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQsaaQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
Cdd:PRK11022 80 EK---ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
250 260
....*....|....*....|....*...
gi 1134749654 252 TVEQIFHAPQHPYTRALLAAVPQLGAMK 279
Cdd:PRK11022 237 KAHDIFRAPRHPYTQALLRALPEFAQDK 264
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
31-273 |
1.76e-91 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 285.86 E-value: 1.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSEqsaAQMRHVRgADMAMIF 110
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-------GQDITGLSG---RELRPLR-RRMQMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:COG4608 102 QDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEH--ADRYPHEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLA 270
Cdd:COG4608 180 VCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLS 259
|
...
gi 1134749654 271 AVP 273
Cdd:COG4608 260 AVP 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-277 |
1.20e-83 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 262.43 E-value: 1.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRdvielse 92
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsAAQMRHVRgadmaMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEamvEAKRMLDQVRIPEAqtILSRYPHQLSGG 172
Cdd:COG1124 75 --KAFRRRVQ-----MVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPS--FLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250 260
....*....|....*....|....*
gi 1134749654 253 VEQIFHAPQHPYTRALLAAVPQLGA 277
Cdd:COG1124 223 VADLLAGPKHPYTRELLAASLAFER 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-273 |
8.56e-83 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 263.49 E-value: 8.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 22 FMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLLRRrsrdviELSEQSAAQMRHV 101
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV----AWLGK------DLLGMKDDEWRAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 102 RgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQ-NASREEAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMRQRVMIA 180
Cdd:PRK15079 97 R-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLP--NLINRYPHEFSGGQCQRIGIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
250
....*....|...
gi 1134749654 261 QHPYTRALLAAVP 273
Cdd:PRK15079 254 LHPYTKALMSAVP 266
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
31-271 |
2.34e-79 |
|
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: 250.75 E-value: 2.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrrRSRDVIELSeqsaaqmrhVRGADMAMIF 110
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILL---DGRPLLPLS---------IRGRHIATIM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSLNPVFTVGEQIAESIRLHQNASRE--EAMVEAkrmLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:TIGR02770 69 QNPRTAFNPLFTMGNHAIETLRSLGKLSKQarALILEA---LEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRAL 268
Cdd:TIGR02770 146 FLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKL 225
|
...
gi 1134749654 269 LAA 271
Cdd:TIGR02770 226 LSA 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
311-580 |
1.87e-78 |
|
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: 257.91 E-value: 1.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG---GEIIFNGQR 387
Cdd:COG1123 2 TPLLEVRDLSVRYP---------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 388 IDTLSPgklQALRRDIQFIFQDPYASLDPrQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGG 467
Cdd:COG1123 73 LLELSE---ALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGL-SRAEARARVLELLEAVGL-ERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250 260 270
....*....|....*....|....*....|...
gi 1134749654 548 RRAVFENPQhpytrkLLAAVPVAEPSRQRPQRV 580
Cdd:COG1123 227 PEEILAAPQ------ALAAVPRLGAARGRAAPA 253
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-325 |
4.10e-74 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 240.58 E-value: 4.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLrrrsrDVIELSE 92
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW-HVTADRFRW-----NGIDLLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESI-----------RLHQNASReeamveAKRMLDQVRIPEAQTI 161
Cdd:COG4170 78 LSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpswtfkgkwwqRFKWRKKR------AIELLHRVGIKDHKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
Cdd:COG4170 152 MNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 242 MYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLgamkGLDYPRRFPLISLEH--PAKQAPPI----------EQKTVVD 309
Cdd:COG4170 232 LYCGQTVESGPTEQILKSPHHPYTKALLRSMPDF----RQPLPHKSRLNTLPGsiPPLQHLPIgcrlgprcpyAQKKCVE 307
|
330
....*....|....*...
gi 1134749654 310 GEPVLRVRNLVTR--FPL 325
Cdd:COG4170 308 TPRLRKIKGHEFAchFPL 325
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
313-576 |
4.54e-72 |
|
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: 233.16 E-value: 4.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFplRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRI 472
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
250 260
....*....|....*....|....
gi 1134749654 553 ENpQHPYTRKLLAAVPVAEPSRQR 576
Cdd:TIGR02769 240 SF-KHPAGRNLQSAVLPEHPVRRS 262
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
311-568 |
5.45e-72 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 235.00 E-value: 5.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG---GEIIFNGQR 387
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 388 IDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLlPEHAWR---YPHE 463
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRmkmYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260
....*....|....*....|....*
gi 1134749654 544 EIGPRRAVFENPQHPYTRKLLAAVP 568
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-275 |
1.73e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 231.01 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 22 FMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmlLRRRSRDVIELSEQSAAQMRHv 101
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGE-------LYYQGQDLLKADPEAQKLLRQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 102 rgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRI-PEAQTilsRYPHQLSGGMRQRVMIA 180
Cdd:PRK11308 93 ---KIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYD---RYPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
250
....*....|....*
gi 1134749654 261 QHPYTRALLAAVPQL 275
Cdd:PRK11308 247 RHPYTQALLSATPRL 261
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
314-580 |
9.32e-70 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 229.19 E-value: 9.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRID 389
Cdd:COG1135 2 IELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInlleRPTSGSVLVDGVDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 TLSPGKLQALRRDIQFIFQDpyASLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQR 469
Cdd:COG1135 71 ALSERELRAARRKIGMIFQH--FNLLSSRTVAENVALPLEIAGV-PKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250 260 270
....*....|....*....|....*....|.
gi 1134749654 550 AVFENPQHPYTRKLLAAVPVAEPSRQRPQRV 580
Cdd:COG1135 227 DVFANPQSELTRRFLPTVLNDELPEELLARL 257
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
312-576 |
4.26e-69 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 225.34 E-value: 4.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPLRSGLLNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHQHQTV--LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQR 471
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE---IGPR 548
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDK 239
|
250 260
....*....|....*....|....*...
gi 1134749654 549 RAVfenpQHPYTRKLLAAVPVAEPSRQR 576
Cdd:PRK10419 240 LTF----SSPAGRVLQNAVLPAFPVRRR 263
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
311-566 |
1.52e-68 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 223.90 E-value: 1.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGLLNRvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidt 390
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
Cdd:PRK15112 77 LHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*.
gi 1134749654 551 VFENPQHPYTRKLLAA 566
Cdd:PRK15112 237 VLASPLHELTKRLIAG 252
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
12-272 |
6.07e-64 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 211.60 E-value: 6.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM--RLLEQAGglvqcdKMLLRRRSRDVIE 89
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS-TLLKCLyfDLAPTSG------SVYYRDRDGGPRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 LSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAEsiRL------HQNASREEAmveaKRMLDQVRIPeaqtiLS 163
Cdd:COG4107 81 LFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAE--RLmaagerHYGDIRARA----LEWLERVEIP-----LE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 R---YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
Cdd:COG4107 150 RiddLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTM 229
|
250 260 270
....*....|....*....|....*....|..
gi 1134749654 241 VMYQGEAVETGTVEQIFHAPQHPYTRALLAAV 272
Cdd:COG4107 230 VMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-271 |
1.36e-62 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 207.63 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIafmqdQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL----EQAGGLVQCDKMllrrrsrdv 87
Cdd:PRK10418 4 QIELRNIAL-----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGK--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 ielsEQSAAQmrhVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAkrmLDQVRIPEAQTILSRYPH 167
Cdd:PRK10418 70 ----PVAPCA---LRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAA---LEAVGLENAARVLKLYPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
250 260
....*....|....*....|....
gi 1134749654 248 VETGTVEQIFHAPQHPYTRALLAA 271
Cdd:PRK10418 220 VEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-556 |
3.72e-61 |
|
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: 203.20 E-value: 3.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVE----SQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDp 410
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINglerPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 411 YASLDPRqTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:cd03258 91 FNLLSSR-TVFENVALPLEIAGV-PKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:cd03258 168 TSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
13-286 |
1.29e-60 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 202.76 E-value: 1.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAF-----MQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdKMLLRRRsrdv 87
Cdd:COG4167 5 LEVRNLSKTFkyrtgLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSG-----EILINGH---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 iELSEQSAAQM-RHVRgadmaMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRI-PEAQTIlsrY 165
Cdd:COG4167 76 -KLEYGDYKYRcKHIR-----MIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHANF---Y 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1134749654 246 EAVETGTVEQIFHAPQHPYTRALLAAvpQLGAMKGLDYPRR 286
Cdd:COG4167 227 EVVEYGKTAEVFANPQHEVTKRLIES--HFGEALTADAWRR 265
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-596 |
4.92e-60 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 203.43 E-value: 4.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQRIDTLSPG-KLQALRRDIQFIFQDPYAS 413
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKeRRNLVGAEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 LDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLlPEHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVP-- 568
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPef 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1134749654 569 VAEPSR------------QRPQRVLLSDDLP-SNIHLRGEE 596
Cdd:PRK11022 261 AQDKARlaslpgvvpgkyDRPNGCLLNPRCPyATDRCRAEE 301
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
334-567 |
1.04e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 203.11 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYAS 413
Cdd:PRK11153 15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQ--HFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 LDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:PRK11153 93 LLSSRTVFDNVALPLELAGT-PKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAV 567
Cdd:PRK11153 171 LDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQST 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
309-561 |
5.60e-59 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 197.51 E-value: 5.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 309 DGEPVLRVRNLVTRFplrsGllnrvTREVHavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
Cdd:COG1127 1 MSEPMIEVRNLTKSF----G-----DRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 389 DTLSPGKLQALRRDIQFIFQDP--YASLdprqTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGlLPEHAWRYPHEFSG 466
Cdd:COG1127 70 TGLSEKELYELRRRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
250
....*....|....*
gi 1134749654 547 PRRAVFENPqHPYTR 561
Cdd:COG1127 225 TPEELLASD-DPWVR 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-270 |
6.16e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 206.09 E-value: 6.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 8 DAGNVLAVENLNIAF---------MQDQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLeQAGGLVQCDKM 78
Cdd:PRK15134 271 PASPLLDVEQLQVAFpirkgilkrTVDHN--VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 79 LLRRRSRdvielseqsaAQMRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQN----ASREEAMVEAkrmLDQVR 154
Cdd:PRK15134 348 PLHNLNR----------RQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtlsaAQREQQVIAV---MEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 155 I-PEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVA 233
Cdd:PRK15134 414 LdPETR---HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVR 490
|
250 260 270
....*....|....*....|....*....|....*..
gi 1134749654 234 EIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLA 270
Cdd:PRK15134 491 ALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
312-572 |
6.35e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 206.09 E-value: 6.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFplRSGllnRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL-----VESQGGEIIFNGQ 386
Cdd:PRK15134 4 PLLAIENLSVAF--RQQ---QTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 387 RIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLlpEHAWR----YP 461
Cdd:PRK15134 77 SLLHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGI--RQAAKrltdYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|.
gi 1134749654 542 IVEIGPRRAVFENPQHPYTRKLLAAVPVAEP 572
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQKLLNSEPSGDP 265
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
312-559 |
2.36e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 196.86 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:COG3842 4 PALELENVSKRYG-----------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKlqalrRDIQFIFQDpYAsLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQR 471
Cdd:COG3842 73 PPEK-----RNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGV-PKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD----MAvverISHRVAVMYLGQIVEIGP 547
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGT 219
|
250
....*....|..
gi 1134749654 548 RRAVFENPQHPY 559
Cdd:COG3842 220 PEEIYERPATRF 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
313-567 |
1.39e-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: 190.98 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFplrsGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLS 392
Cdd:COG1126 1 MIEIENLHKSF----G-------DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PGKLQALRRDIQFIFQDpyASLDPRQTIGDSIIE-PLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQR 471
Cdd:COG1126 69 KKDINKLRRKVGMVFQQ--FNLFPHLTVLENVTLaPIKVKKM-SKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
250
....*....|....*.
gi 1134749654 552 FENPQHPYTRKLLAAV 567
Cdd:COG1126 224 FENPQHERTRAFLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
311-544 |
2.48e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 189.87 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQ 386
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILggldRPTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 387 RIDTLSPGKLQALRRD-IQFIFQDPYasLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFS 465
Cdd:COG1136 71 DISSLSERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGV-SRKERRERARELLERVGL-GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-551 |
2.53e-56 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 198.32 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCD--KMLLRRRsrdVIELSEQSAAQMRHVrgadmAM 108
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS-T---LMKIL---SGVYQPDsgEILLDGE---PVRFRSPRDAQAAGI-----AI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPmtSLNPVFTVgeqiAESIRLHQNASR-----EEAMV-EAKRMLDQVRIPE-AQTILSRyphqLSGGMRQRVMIAM 181
Cdd:COG1129 84 IHQEL--NLVPNLSV----AENIFLGREPRRgglidWRAMRrRARELLARLGLDIdPDTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIfhapq 261
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 262 hpyTRALLAAvpqlgAMKGLDYPRRFPlislehpakqappieQKTVVDGEPVLRVRNLVTRfplrsgllnrvtrevHAVE 341
Cdd:COG1129 228 ---TEDELVR-----LMVGRELEDLFP---------------KRAAAPGEVVLEVEGLSVG---------------GVVR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQF---------IFQDpya 412
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR--DAIRAGIAYvpedrkgegLVLD--- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 sldprQTIGD----SIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
Cdd:COG1129 345 -----LSIREnitlASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 489 EAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
314-542 |
2.66e-56 |
|
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: 189.62 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRID 389
Cdd:cd03255 1 IELKNLSKTYGGGG-------EKVQALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILggldRPTSGEVRVDGTDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 TLSPGKLQALRRD-IQFIFQDPYasLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQ 468
Cdd:cd03255 70 KLSEKELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGL-GDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQI 542
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-325 |
1.06e-55 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 191.94 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQaGGLVQCDKMLLrrrsrDVIELS 91
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD-NWRVTADRMRF-----DDIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESI-----------RLHQNASReeamveAKRMLDQVRIPEAQT 160
Cdd:PRK15093 77 RLSPRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwqRFGWRKRR------AIELLHRVGIKDHKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
Cdd:PRK15093 151 AMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKIN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 241 VMYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLGamKGLDYPRRFPLI-----SLEH---PAKQAP--PIEQKTVVDG 310
Cdd:PRK15093 231 VLYCGQTVETAPSKELVTTPHHPYTQALIRAIPDFG--SAMPHKSRLNTLpgaipLLEHlpiGCRLGPrcPYAQRECIET 308
|
330
....*....|....*..
gi 1134749654 311 EPVLRVRN--LVTRFPL 325
Cdd:PRK15093 309 PRLTGAKNhlYACHFPL 325
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
31-551 |
4.14e-54 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 192.16 E-value: 4.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCDK--MLLR------RRSRDVIELseqsaaqmrhvr 102
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKS-T---LMKIL---YGLYQPDSgeILIDgkpvriRSPRDAIAL------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 103 GadMAMIFQEPMtsLNPVFTVGEQIA----ESIRLHQNASREEAMVE--AKRM---LDqvripeaqtiLSRYPHQLSGGM 173
Cdd:COG3845 81 G--IGMVHQHFM--LVPNLTVAENIVlglePTKGGRLDRKAARARIRelSERYgldVD----------PDAKVEDLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 174 RQRVMIAMALSCRPAVLIADEPTTALdvTIQaQILQLIKVLQ--KEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVL--TPQ-EADELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 252 TVEQIfhapqhpyTRALLAAvpqlgAMKGldyprrfplislehpAKQAPPIEQKTVVDGEPVLRVRNLVTRFPlrsglln 331
Cdd:COG3845 224 DTAET--------SEEELAE-----LMVG---------------REVLLRVEKAPAEPGEVVLEVENLSVRDD------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 332 rvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRrdIQFIFQDPY 411
Cdd:COG3845 269 ---RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG--VAYIPEDRL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 412 AS-LDPRQTIGDSII------EPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
Cdd:COG3845 344 GRgLVPDMSVAENLIlgryrrPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 485 IIADEAVSALDVS----IRGQIINLlldlqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:COG3845 424 LIAAQPTRGLDVGaiefIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-553 |
4.81e-53 |
|
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: 190.01 E-value: 4.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLL------EQAGGLV-----QCDKML-L 80
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVLrgmdqyEPTSGRIiyhvaLCEKCGyV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 81 RRRSRD--------------VIELSEQSAAQMRHVRgADMAMIFQEPMtSLNPVFTVGEQIAESirLHQ-NASREEAMVE 145
Cdd:TIGR03269 73 ERPSKVgepcpvcggtlepeEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEA--LEEiGYEGKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 146 AKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFI 225
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 226 THDMGVVAEIADRVLVMYQGEAVETGTVEQIFHapqhpytrallaavpqlgamkgldyprRFplislehpAKQAPPIEQK 305
Cdd:TIGR03269 226 SHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA---------------------------VF--------MEGVSEVEKE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 306 TVVD-GEPVLRVRNLVTRF-PLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF 383
Cdd:TIGR03269 271 CEVEvGEPIIKVRNVSKRYiSVDRGV-------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 384 --NGQRIDTLSPGKLQALR--RDIQFIFQDpyASLDPRQTIGDSIIEPLRVHglLPGKEAVARVAWLLERVGLLPEHAW- 458
Cdd:TIGR03269 344 rvGDEWVDMTKPGPDGRGRakRYIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEEKAEe 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 459 ---RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVA 535
Cdd:TIGR03269 420 ildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAA 499
|
570
....*....|....*...
gi 1134749654 536 VMYLGQIVEIGPRRAVFE 553
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEIVE 517
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
339-570 |
2.56e-52 |
|
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: 180.92 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASLDPR 417
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlpeHAW--RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:cd03294 117 RTVLENVAFGLEVQGV-PRAEREERAAEALELVGL---EGWehKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVA 570
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRA 267
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
312-568 |
3.22e-52 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 182.41 E-value: 3.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGgeII------FNG 385
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGR-------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--HVtadrfrWNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 386 QRIDTLSPGKLQAL-RRDIQFIFQDPYASLDPRQTIGDSIIEPLRvHGLLPG------KEAVARVAWLLERVGLL-PEHA 457
Cdd:COG4170 73 IDLLKLSPRERRKIiGREIAMIFQEPSSCLDPSAKIGDQLIEAIP-SWTFKGkwwqrfKWRKKRAIELLHRVGIKdHKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 458 WR-YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
Cdd:COG4170 152 MNsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
250 260 270
....*....|....*....|....*....|..
gi 1134749654 537 MYLGQIVEIGPRRAVFENPQHPYTRKLLAAVP 568
Cdd:COG4170 232 LYCGQTVESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
314-561 |
5.95e-52 |
|
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: 178.46 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFplrsGllnrvTREVHavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03261 1 IELRGLTKSF----G-----GRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLQALRRDIQFIFQDP--YASLdprqTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAwRYPHEFSGGQRQR 471
Cdd:cd03261 70 AELYRLRRRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAED-LYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|
gi 1134749654 552 FeNPQHPYTR 561
Cdd:cd03261 225 R-ASDDPLVR 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-546 |
4.61e-51 |
|
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: 175.40 E-value: 4.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQD 409
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 410 PyaSLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:cd03259 81 Y--ALFPHLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-274 |
5.30e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 179.50 E-value: 5.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKmllrrrsRDVIELSEq 93
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLERPtSGSVLVDG-------VDLTALSE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 saAQMRHVRgADMAMIFQEP--MTSLnpvfTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPE-AQtilsRYPHQLS 170
Cdd:COG1135 75 --RELRAAR-RKIGMIFQHFnlLSSR----TVAENVALPLEI-AGVPKAEIRKRVAELLELVGLSDkAD----AYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|....
gi 1134749654 251 GTVEQIFHAPQHPYTRALLAAVPQ 274
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLPTVLN 246
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
314-537 |
1.97e-50 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 173.81 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gklqalrrDIQFIFQDPyaSLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRIC 473
Cdd:cd03293 74 --------DRGYVFQQD--ALLPWLTVLDNVALGLELQGV-PKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM--AVveRISHRVAVM 537
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
314-556 |
2.67e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 174.06 E-value: 2.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gkLQALRRDIQFIFQDPyaslDpRQTIGDSIIE----PLRVHGlLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQR 469
Cdd:COG1122 70 --LRELRRKVGLVFQNP----D-DQLFAPTVEEdvafGPENLG-LPREEIRERVEEALELVGLE-HLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
....*..
gi 1134749654 550 AVFENPQ 556
Cdd:COG1122 220 EVFSDYE 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
312-551 |
7.36e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 7.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPlrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKLQALRRDIQFIFQDPYasLDPRQTIGDSIIeplrvHGLLP------------GKEAVARVAWLLERVGLLpEHAWR 459
Cdd:COG3638 71 RGRALRRLRRRIGMIFQQFN--LVPRLSVLTNVL-----AGRLGrtstwrsllglfPPEDRERALEALERVGLA-DKAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 1134749654 540 GQIVEIGPRRAV 551
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
330-551 |
7.77e-50 |
|
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: 172.75 E-value: 7.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG-----GEIIFNGQRIDTLSPGKLqALRRDIQ 404
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVL-ELRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 405 FIFQDPYasldP-RQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWR-YPHEFSGGQRQRICIARALALNP 482
Cdd:cd03260 85 MVFQKPN----PfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 483 KVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
311-567 |
1.18e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 173.35 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQ 386
Cdd:COG1116 5 APALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIagleKPTSGEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 387 RIDTLSPgklqalrrDIQFIFQDPyaSLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSG 466
Cdd:COG1116 74 PVTGPGP--------DRGVVFQEP--ALLPWLTVLDNVALGLELRGV-PKAERRERARELLELVGLA-GFEDAYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM--AVveRISHRVAVM--YLGQI 542
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAV--FLADRVVVLsaRPGRI 219
|
250 260 270
....*....|....*....|....*....|...
gi 1134749654 543 VEI------GPR-RAVFENPQ-HPYTRKLLAAV 567
Cdd:COG1116 220 VEEidvdlpRPRdRELRTSPEfAALRAEILDLL 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-261 |
2.05e-49 |
|
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: 171.61 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDkmllrrrSRDVIELSEq 93
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERpTSGSVLVD-------GTDLTLLSG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 saAQMRHVRgADMAMIFQE--PMTSLnpvfTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
Cdd:cd03258 75 --KELRKAR-RRIGMIFQHfnLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKA---DAYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
250
....*....|
gi 1134749654 252 TVEQIFHAPQ 261
Cdd:cd03258 224 TVEEVFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-272 |
3.23e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 171.33 E-value: 3.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKMLLRRRSRDViel 90
Cdd:COG1126 1 MIEIENLHKSF-GDLE---VLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLEEPdSGTITVDGEDLTDSKKDI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 seqsaaqmRHVRgADMAMIFQepmtSLN--PVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQ 168
Cdd:COG1126 73 --------NKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADK---ADAYPAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKE-MSMgvIFITHDMGVVAEIADRVLVMYQGEA 247
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTM--VVVTHEMGFAREVADRVVFMDGGRI 214
|
250 260
....*....|....*....|....*
gi 1134749654 248 VETGTVEQIFHAPQHPYTRALLAAV 272
Cdd:COG1126 215 VEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-246 |
5.26e-48 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 167.28 E-value: 5.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDkmllrrrsRDVIEL 90
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRptSGEVRVDG--------TDISKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEqsaAQMRHVRGADMAMIFQEPmtSLNPVFTVGEQIAESIRLHQNaSREEAMVEAKRMLDQVRIPEaqtILSRYPHQLS 170
Cdd:cd03255 72 SE---KELAAFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGLGD---RLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMgVVAEIADRVLVMYQGE 246
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
337-548 |
5.73e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 167.54 E-value: 5.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDP 416
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIGDSIIEPLRVHGlLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:COG2884 93 DRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 497 SIRGQIINLLLDLQRdFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
Cdd:COG2884 171 ETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-269 |
1.53e-47 |
|
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: 166.69 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 8 DAGNVLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDV 87
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-------GQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 IELSEqsaAQMRHVRgADMAMIFQEP--MTSLnpvfTVGEQIAESIRLHQNASREEA--MVEAKrmLDQVRIPEAQtilS 163
Cdd:COG1127 70 TGLSE---KELYELR-RRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIreLVLEK--LELVGLPGAA---D 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY 243
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250 260
....*....|....*....|....*.
gi 1134749654 244 QGEAVETGTVEQIFHAPqHPYTRALL 269
Cdd:COG1127 217 DGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-566 |
1.54e-47 |
|
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: 167.09 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDpyASLDPRQ 418
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKIGYVIQQ--IGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIieplrvhGLLPG------KEAVARVAWLLERVGLLPEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:cd03295 91 TVEENI-------ALVPKllkwpkEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAA 566
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
13-274 |
2.55e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 167.03 E-value: 2.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM--RLLEQAGglvqcdKMLLRRRSRDVIEL 90
Cdd:PRK11701 7 LSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKT-TLLNALsaRLAPDAG------EVHYRMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAEsiRL------HQNASREEAMveakRMLDQVRIPEAQtiLSR 164
Cdd:PRK11701 76 YALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGE--RLmavgarHYGDIRATAG----DWLERVEIDAAR--IDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260 270
....*....|....*....|....*....|
gi 1134749654 245 GEAVETGTVEQIFHAPQHPYTRALLAAVPQ 274
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYTQLLVSSVLQ 257
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
338-556 |
6.85e-47 |
|
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: 164.72 E-value: 6.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPR 417
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK-----RPVNTVFQN-YA-LFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:cd03300 87 LTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
314-564 |
7.39e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.40 E-value: 7.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLR----LVESQGGEIIFNGQRID 389
Cdd:COG1118 3 IEVRNISKRFG-----------SFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRiiagLETPDSGRIVLNGRDLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 T-LSPGKlqalrRDIQFIFQDpYAsLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQ 468
Cdd:COG1118 68 TnLPPRE-----RRVGFVFQH-YA-LFPHMTVAENIAFGLRVRPP-SKAEIRARVEELLELVQL-EGLADRYPSQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTP 218
|
250
....*....|....*.
gi 1134749654 549 RAVFENPQHPYTRKLL 564
Cdd:COG1118 219 DEVYDRPATPFVARFL 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-266 |
1.49e-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: 164.21 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqaGGLVQCDKMLLRRRSRDVIELSEqs 94
Cdd:cd03261 3 LRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKST----LLRLI---VGLLRPDSGEVLIDGEDISGLSE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 aAQMRHVRgADMAMIFQEP--MTSLnpvfTVGEQIAESIRLHQNASREE--AMVEAKrmLDQVRIPEAQtilSRYPHQLS 170
Cdd:cd03261 70 -AELYRLR-RRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEEirEIVLEK--LEAVGLRGAE---DLYPAELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
250
....*....|....*.
gi 1134749654 251 GTVEQIFHApQHPYTR 266
Cdd:cd03261 219 GTPEELRAS-DDPLVR 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-316 |
2.68e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 166.90 E-value: 2.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 16 ENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDkmllrrrSRDVIELSEQS 94
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERpTSGRVLVD-------GQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 AAQMRHvrgaDMAMIFQEpmtslnpvF------TVGEQIAESIRLhQNASREEamVEAK--RMLDQVRIPEAQtilSRYP 166
Cdd:PRK11153 77 LRKARR----QIGMIFQH--------FnllssrTVFDNVALPLEL-AGTPKAE--IKARvtELLELVGLSDKA---DRYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 247 AVETGTVEQIFHAPQHPYTRALLAAVpqlgamkgldyprrfplISLEHPAKQAPPIEQKTVVDGEPVLRV 316
Cdd:PRK11153 219 LVEQGTVSEVFSHPKHPLTREFIQST-----------------LHLDLPEDYLARLQAEPTTGSGPLLRL 271
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-249 |
4.10e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.52 E-value: 4.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCDKMLLRRRSRDVIEL 90
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-T---LLNIL---GGLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEqsaAQMRHVRGADMAMIFQEPmtSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLS 170
Cdd:COG1136 76 SE---RELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMgVVAEIADRVLVMYQGEAVE 249
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
305-561 |
3.14e-45 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 161.36 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 305 KTVVDGEPVLRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG-----G 379
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 380 EIIFNGQriDTLSPG-KLQALRRDIQFIFQDPyaslDP-RQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPE-- 455
Cdd:COG1117 72 EILLDGE--DIYDPDvDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEvk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 456 ---HawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISH 532
Cdd:COG1117 146 drlK--KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVTHNMQQAARVSD 221
|
250 260
....*....|....*....|....*....
gi 1134749654 533 RVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
314-551 |
5.49e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.84 E-value: 5.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gklqALRRDIQFIFQDPyaSLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRIC 473
Cdd:COG1131 70 ----EVRRRIGYVPQEP--ALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-272 |
1.56e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 159.85 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLEqagGLVQCDKMLLRRRSRDVIELSEqsaAQMRHVRGaDMAMIFQ 111
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKST----LARLLV---GLESPSQGNVSWRGEPLAKLNR---AQRKAFRR-DIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PRK10419 97 DSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDS--VLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHApQHPYTRALLAA 271
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGRVLQNA 253
|
.
gi 1134749654 272 V 272
Cdd:PRK10419 254 V 254
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
314-551 |
1.61e-44 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 158.89 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03256 1 IEVENLSKTYP----------NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLQALRRDIQFIFQDPyaSLDPRQTIGDSIIeplrvHGLLP------------GKEAVARVAWLLERVGLLpEHAWRYP 461
Cdd:cd03256 71 KALRQLRRQIGMIFQQF--NLIERLSVLENVL-----SGRLGrrstwrslfglfPKEEKQRALAALERVGLL-DKAYQRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
250
....*....|
gi 1134749654 542 IVEIGPRRAV 551
Cdd:cd03256 223 IVFDGPPAEL 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
338-542 |
1.91e-44 |
|
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: 157.69 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQDpyASLDPR 417
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQ--FNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIE-PLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:cd03262 91 LTVLENITLaPIKVKGM-SKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1134749654 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03262 169 ELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
314-542 |
2.44e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.29 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSGLLNrvtrevhavekVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:COG4619 1 LELEGLSFRVGGKPILSP-----------VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gklQALRRDIQFIFQDPYAsldPRQTIGDSIIEPLRVHGLLPGKEAVARvawLLERVGLlPEHAWRYP-HEFSGGQRQRI 472
Cdd:COG4619 70 ---PEWRRQVAYVPQEPAL---WGGTVRDNLPFPFQLRERKFDRERALE---LLERLGL-PPDILDKPvERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
311-567 |
5.70e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 157.78 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGLLNrvtrevhavekVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF---NGQR 387
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRD-----------VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 388 ID--TLSPGKLQAL-RRDIQFIFQDPYASLDPRQTIGDSIIEPL-----RVHGLLpgkEAVArVAWLlERVGLLPEHAWR 459
Cdd:PRK11701 73 RDlyALSEAERRRLlRTEWGFVHQHPRDGLRMQVSAGGNIGERLmavgaRHYGDI---RATA-GDWL-ERVEIDAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260
....*....|....*....|....*...
gi 1134749654 540 GQIVEIGPRRAVFENPQHPYTRKLLAAV 567
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
314-541 |
5.81e-44 |
|
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: 155.04 E-value: 5.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
Cdd:cd03229 1 LELKNVSKRYG-----------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLQALRRDIQFIFQDPyaSLDPRQTIGDSIIEPLrvhgllpgkeavarvawllervgllpehawryphefSGGQRQRIC 473
Cdd:cd03229 69 DELPPLRRRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-261 |
7.95e-44 |
|
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: 156.34 E-value: 7.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrdviELSE 92
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK----------DITK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHvrgaDMAMIFQEPMTSL-NPvfTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSG 171
Cdd:COG1122 68 KNLRELRR----KVGLVFQNPDDQLfAP--TVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEH---LADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
250
....*....|
gi 1134749654 252 TVEQIFHAPQ 261
Cdd:COG1122 217 TPREVFSDYE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
315-541 |
9.21e-44 |
|
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: 155.70 E-value: 9.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 315 RVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG 394
Cdd:cd03225 1 ELKNLSFSYP---------DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 395 KLqalRRDIQFIFQDPyaslDpRQTIGDSIIE----PLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQ 470
Cdd:cd03225 72 EL---RRKVGLVFQNP----D-DQFFGPTVEEevafGLENLGL-PEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-272 |
1.02e-42 |
|
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: 154.22 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALM-RLLEQAGglvqcdKMLLRRRSRDVIELSEQSAAQMRHVRGADMA 107
Cdd:TIGR02323 16 GKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHG------TATYIMRSGAELELYQLSEAERRRLMRTEWG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEPMTSLNPVFTVGEQIAEsiRLHQNASREEAMV--EAKRMLDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:TIGR02323 90 FVHQNPRDGLRMRVSAGANIGE--RLMAIGARHYGNIraTAQDWLEEVEIDPTR--IDDLPRAFSGGMQQRLQIARNLVT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYT 265
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYT 245
|
....*..
gi 1134749654 266 RALLAAV 272
Cdd:TIGR02323 246 QLLVSSI 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
330-557 |
7.87e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 154.85 E-value: 7.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 LNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFI 406
Cdd:COG3839 6 LENVSKsygGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 407 FQDpYAsLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVII 486
Cdd:COG3839 81 FQS-YA-LYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD----MAvverISHRVAVMYLGQIVEIGPRRAVFENPQH 557
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
336-552 |
1.06e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.81 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKLQALRRDIQFIFQDPyaslD 415
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVFQNP----D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 pRQTIGdSIIEPLRVHGL----LPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:TIGR04520 88 -NQFVG-ATVEDDVAFGLenlgVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVF 552
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-257 |
1.60e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 151.71 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 8 DAGNVLAVENLNiaFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrdv 87
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 iELSEQSAAQMRHVRGadmaMIFQEPmtslNPVF---TVGEQIAESIRlHQNASREEaMVE-AKRMLDQVRIpeaQTILS 163
Cdd:PRK13635 70 -VLSEETVWDVRRQVG----MVFQNP----DNQFvgaTVQDDVAFGLE-NIGVPREE-MVErVDQALRQVGM---EDFLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMY 243
Cdd:PRK13635 136 REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMN 214
|
250
....*....|....
gi 1134749654 244 QGEAVETGTVEQIF 257
Cdd:PRK13635 215 KGEILEEGTPEEIF 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-246 |
2.95e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 148.77 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrSRDVIELSeqsaaqm 98
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHVrgadmAMIFQEPMTSL-NPvfTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRV 177
Cdd:cd03225 75 RKV-----GLVFQNPDDQFfGP--TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
340-566 |
5.87e-41 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 149.46 E-value: 5.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL----VESQGGEIIFNGQRIdtlSPGKLQAlrRDIQFIFQDPYASLD 415
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPV---APCALRG--RKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGDSIIEPLRVHGLLPgkeAVARVAWLLERVGLlpEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPA---DDATLTAALEAVGL--ENAARvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAA 566
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-551 |
1.37e-40 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 154.82 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVIELSEQSAAQMrhvrgaDMAMIFQE 112
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKS----TLMKII---AGIVPPDSGTLEIGGNPCARLTPAKAHQL------GIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 PMtsLNPVFTVGEQIAesIRLHQNASREEAMVEAKRMLDQVRIPEAQTILsryphqLSGGMRQRVMIAMALSCRPAVLIA 192
Cdd:PRK15439 95 PL--LFPNLSVKENIL--FGLPKRQASMQKMKQLLAALGCQLDLDSSAGS------LEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 193 DEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHApqhpytrALLAAV 272
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD-------DIIQAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 273 PQLGAMKGLDYPRRFPLislehpakqAPPIEQKTVVDGEPVLRVRNLVTRfplrsGLLNrvtrevhavekVSFDLWPGET 352
Cdd:PRK15439 237 TPAAREKSLSASQKLWL---------ELPGNRRQQAAGAPVLTVEDLTGE-----GFRN-----------ISLEVRAGEI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyasldpRQTIGDSIIEPLR--- 429
Cdd:PRK15439 292 LGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA--QRLARGLVYLPED-------RQSSGLYLDAPLAwnv 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 430 ---VHGLLPGKEAVARVAWLLER----VGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
Cdd:PRK15439 363 calTHNRRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1134749654 503 INLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:PRK15439 443 YQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-271 |
2.34e-40 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 148.01 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAF-----MQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRd 86
Cdd:PRK15112 4 LLEVRNLSKTFryrtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 87 vielseqsaaqmrHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNAS---REEAMVEAKRMLDQvrIPEAqtiLS 163
Cdd:PRK15112 83 -------------SYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEpeqREKQIIETLRQVGL--LPDH---AS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY 243
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 224
|
250 260
....*....|....*....|....*...
gi 1134749654 244 QGEAVETGTVEQIFHAPQHPYTRALLAA 271
Cdd:PRK15112 225 QGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-273 |
2.63e-40 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 148.18 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrdviELSEQSAAQMRHVRGADMAMI 109
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ----------DIAAMSRKELRELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEpmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIpEAQtiLSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03294 108 FQS--FALLPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL-EGW--EHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALL 269
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
....
gi 1134749654 270 AAVP 273
Cdd:cd03294 262 RGVD 265
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-256 |
4.06e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVielse 92
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsaaqMRHVrgadmAMIFQEPmtSLNPVFTVGEQIAESIRLHQNaSREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGG 172
Cdd:COG1131 72 -----RRRI-----GYVPQEP--ALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDA---ADRKVGTLSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:COG1131 136 MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
....
gi 1134749654 253 VEQI 256
Cdd:COG1131 215 PDEL 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
343-490 |
6.34e-40 |
|
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: 142.79 E-value: 6.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyaSLDPRQTIGD 422
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 423 SIIEPLRVHGLLpGKEAVARVAWLLERVGL---LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:pfam00005 79 NLRLGLLLKGLS-KREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-242 |
7.24e-40 |
|
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: 145.31 E-value: 7.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqAGglvqcdkmlLRRRSRDVIELSE 92
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-T---LLRII--AG---------LERPTSGEVLVDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQmrhvRGADMAMIFQEPmtSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGG 172
Cdd:cd03293 66 EPVTG----PGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGF---ENAYPHQLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-257 |
9.21e-40 |
|
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: 146.83 E-value: 9.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDkmllrrrSRDVIELSEQSAAQMRHVRGadmaMI 109
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNgLLKPTSGTVTID-------GRDITAKKKKKLKDLRKKVG----LV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMTSLnpvF--TVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:TIGR04521 88 FQFPEHQL---FeeTVYKDIAFGPK-NLGLSEEEAEERVKEALELVGLDE--EYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIF 257
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
311-567 |
1.81e-39 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 145.36 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGLLNrvtrevhavekVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF---NGQR 387
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRD-----------VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 388 ID--TLSPGKLQAL-RRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLP-GKEAVARVAWLlERVGLLPEHAWRYPHE 463
Cdd:TIGR02323 70 LElyQLSEAERRRLmRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWL-EEVEIDPTRIDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
250 260
....*....|....*....|....
gi 1134749654 544 EIGPRRAVFENPQHPYTRKLLAAV 567
Cdd:TIGR02323 229 ESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
314-546 |
3.29e-39 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 143.16 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03301 1 VELENVTKRFG-----------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKlqalrRDIQFIFQDpYAsLDPRQTIGDSIIEPLRVHGLLPG--KEAVARVAWLLERVGLLPehawRYPHEFSGGQRQR 471
Cdd:cd03301 70 KD-----RDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEHLLD----RKPKQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-242 |
3.80e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.46 E-value: 3.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 9 AGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCDKMLLRRRSRDVI 88
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-T---LLRLI---AGLEKPTSGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 ELseqsaaqmrhvrGADMAMIFQEPmtSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQ 168
Cdd:COG1116 77 GP------------GPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGF---EDAYPHQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDV----TIQAQILQLIKVLQKemsmGVIFITHDmgvVAE---IADRVLV 241
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQETGK----TVLFVTHD---VDEavfLADRVVV 211
|
.
gi 1134749654 242 M 242
Cdd:COG1116 212 L 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-251 |
6.22e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 142.27 E-value: 6.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRDVIELse 92
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG-------RDVTGV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsAAQMRHVrgadmAMIFQEPmtSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGG 172
Cdd:cd03259 68 --PPERRNI-----GMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEG---LLNRYPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
31-264 |
1.25e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.01 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCD--KMLLRrrSRDVIELseqsAAQMRHVrgadmAM 108
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKT-T---LLRMI---AGFETPDsgRILLD--GRDVTGL----PPEKRNV-----GM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPmtSLNPVFTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:COG3842 82 VFQDY--ALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEG---LADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPY 264
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
314-559 |
1.44e-38 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 142.48 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsp 393
Cdd:cd03296 3 IEVRNVSKRFG-----------DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLQALRRDIQFIFQDpYAsLDPRQTIGDSIIEPLRV---HGLLPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:cd03296 67 TDVPVQERNVGFVFQH-YA-LFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*....
gi 1134749654 551 VFENPQHPY 559
Cdd:cd03296 224 VYDHPASPF 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
313-546 |
4.38e-38 |
|
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: 141.15 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PgklqALRRDIQFIFQDPYasLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRI 472
Cdd:COG4555 70 R----EARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-272 |
4.84e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 141.33 E-value: 4.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTAL-ALMRLLEQAGGLVQCDkmllrrrSRDVIEL 90
Cdd:COG1120 1 MLEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKPSSGEVLLD-------GRDLASL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAQMrhvrgadMAMIFQEPMTSLNpvFTVgeqiAESIRL----HQNA-----SREEAMVEakRMLDQVRIpeaQTI 161
Cdd:COG1120 69 SRRELARR-------IAYVPQEPPAPFG--LTV----RELVALgrypHLGLfgrpsAEDREAVE--EALERTGL---EHL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
Cdd:COG1120 131 ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
250 260 270
....*....|....*....|....*....|.
gi 1134749654 242 MYQGEAVETGTVEQIFhapqhpyTRALLAAV 272
Cdd:COG1120 211 LKDGRIVAQGPPEEVL-------TPELLEEV 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
343-564 |
5.70e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.04 E-value: 5.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP-----GKLQALRRDIQFIFQDpyASLDPR 417
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkGLIRQLRQHVGFVFQN--FNLFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIE-PLRVHGLlPGKEAVARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:PRK11264 100 RTVLENIIEgPVIVKGE-PKEEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLL 564
Cdd:PRK11264 178 ELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
343-556 |
1.24e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID---TLSPGKLQALRRDIQFIFQDpYaSLDPRQT 419
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRELRRNVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIE-PLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
Cdd:PRK11124 99 VQQNLIEaPCRVLGL-SKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 499 RGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAvFENPQ 556
Cdd:PRK11124 177 TAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-271 |
2.39e-37 |
|
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: 138.97 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRHvrgaDMAMIF 110
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG----------EDIREQDPVELRR----KIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQtILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03295 82 QQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAE-FADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLA 270
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
.
gi 1134749654 271 A 271
Cdd:cd03295 238 A 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
309-566 |
2.70e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.15 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 309 DGEPVLRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQri 388
Cdd:PRK13635 1 MKEEIIRVEHISFRYP---------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 389 dTLSPGKLQALRRDIQFIFQDPyaslDPR---QTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFS 465
Cdd:PRK13635 70 -VLSEETVWDVRRQVGMVFQNP----DNQfvgATVQDDVAFGLENIGV-PREEMVERVDQALRQVGME-DFLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEI 545
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
250 260
....*....|....*....|....*....
gi 1134749654 546 GPRRAVFENPQH--------PYTRKLLAA 566
Cdd:PRK13635 222 GTPEEIFKSGHMlqeigldvPFSVKLKEL 250
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
312-568 |
5.55e-37 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 140.71 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ----GGEIIFNGQR 387
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDG-------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 388 IDTLSPGKLQAL-RRDIQFIFQDPYASLDPRQTIGDSIIEPLrvhgllPG----KEAVARVAW-------LLERVGLL-P 454
Cdd:PRK15093 75 LLRLSPRERRKLvGHNVSMIFQEPQSCLDPSERVGRQLMQNI------PGwtykGRWWQRFGWrkrraieLLHRVGIKdH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 455 EHAWR-YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHR 533
Cdd:PRK15093 149 KDAMRsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
250 260 270
....*....|....*....|....*....|....*
gi 1134749654 534 VAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVP 568
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-556 |
6.39e-37 |
|
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: 137.47 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQT 419
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-----RDISYVPQN-YA-LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIEPLRvHGLLPGKEAVARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
Cdd:cd03299 88 VYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI--DHLLnRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
339-556 |
7.12e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.84 E-value: 7.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID---TLSPGKLQALRRDIQFIFQDpYaSLD 415
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLRQKVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGDSIIE-PLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:COG4161 95 PHLTVMENLIEaPCKVLGL-SKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 495 DVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGpRRAVFENPQ 556
Cdd:COG4161 173 DPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQ 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-257 |
1.05e-36 |
|
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: 137.95 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrdvieLSEQSAAQM 98
Cdd:TIGR04520 5 NVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT---------LDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHVRGadmaMIFQepmtslNP--VF---TVGEQIA---ESIRLhqnaSREEaMVEakrmldqvRIPEA------QTILSR 164
Cdd:TIGR04520 76 RKKVG----MVFQ------NPdnQFvgaTVEDDVAfglENLGV----PREE-MRK--------RVDEAlklvgmEDFRDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQ 244
Cdd:TIGR04520 133 EPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNK 211
|
250
....*....|...
gi 1134749654 245 GEAVETGTVEQIF 257
Cdd:TIGR04520 212 GKIVAEGTPREIF 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-562 |
1.35e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 137.35 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP 410
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMD---VIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 411 YASldPRQTIGDSIIEPLRVHGLLPGK-EAVARVAWLLERVGLLPEHAWRY---PHEFSGGQRQRICIARALALNPKVII 486
Cdd:PRK14247 92 NPI--PNLSIFENVALGLKLNRLVKSKkELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRK 562
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-246 |
2.11e-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: 134.24 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSE 92
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------GEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHVRgadmaMIFQEPmtSLNPVFTVGEQIAESirlhqnasreeamveakrmldqvripeaqtilsryphqLSGG 172
Cdd:cd03229 70 ELPPLRRRIG-----MVFQDF--ALFPHLTVLENIALG--------------------------------------LSGG 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd03229 105 QQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-567 |
3.43e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 136.13 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 353 LSLVGESGSGKSTTGRALLRLVESQG-----GEIIFNGQRIDTLSPGKLQaLRRDIQFIFQdpYASLDPRQTIGDSIIEP 427
Cdd:PRK14267 33 FALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIE-VRREVGMVFQ--YPNPFPHLTIYDNVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 428 LRVHGLLPGKEAV-ARVAWLLERVGLLPEHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
Cdd:PRK14267 110 VKLNGLVKSKKELdERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 504 NLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAV 567
Cdd:PRK14267 190 ELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-256 |
4.42e-36 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 135.00 E-value: 4.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQ-----AGGLVQCDKMLLRRRSRDV 87
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 IELSEQsaaqmrhvrgadMAMIFQEPmtslNPV-FTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtILSR-Y 165
Cdd:cd03260 77 LELRRR------------VGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDE--VKDRlH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:cd03260 139 ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT--IVIVTHNMQQAARVADRTAFLLNG 216
|
250
....*....|.
gi 1134749654 246 EAVETGTVEQI 256
Cdd:cd03260 217 RLVEFGPTEQI 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-261 |
5.02e-36 |
|
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: 135.16 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqqKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRDVIELSe 92
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSV-------LLETIAGFIKPDSGKILLNGKDITNLP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsaAQMRhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGG 172
Cdd:cd03299 68 ---PEKR-----DISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:cd03299 134 EQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
....*....
gi 1134749654 253 VEQIFHAPQ 261
Cdd:cd03299 214 PEEVFKKPK 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
314-556 |
5.97e-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: 5.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03219 1 LEVRGLTKRF-----------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLqaLRRDIQFIFQDP--YASLDPRQTI--------GDSIIEPLRVHGLlpgKEAVARVAWLLERVGlLPEHAWRYPHE 463
Cdd:cd03219 70 HEI--ARLGIGRTFQIPrlFPELTVLENVmvaaqartGSGLLLARARREE---REARERAEELLERVG-LADLADRPAGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
250
....*....|...
gi 1134749654 544 EIGPRRAVFENPQ 556
Cdd:cd03219 223 AEGTPDEVRNNPR 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-246 |
9.69e-36 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 133.42 E-value: 9.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKMLLRRRSRDVIELSEQ 93
Cdd:cd03262 3 IKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEEPdSGTIIIDGLKLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 saaqmrhvrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGM 173
Cdd:cd03262 78 ------------VGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKAD---AYPAQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKE-MSMgvIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTM--VVVTHEMGFAREVADRVIFMDDGR 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
313-567 |
1.44e-35 |
|
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: 134.40 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPlrsgllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
Cdd:COG1120 1 MLEAENLSVGYG---------GRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PgklQALRRDIQFIFQDPYASldprqtigdsiiEPLRV-----------HGLL--PGKEAVARVAWLLERVGLLpEHAWR 459
Cdd:COG1120 70 R---RELARRIAYVPQEPPAP------------FGLTVrelvalgryphLGLFgrPSAEDREAVEEALERTGLE-HLADR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
Cdd:COG1120 134 PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
250 260
....*....|....*....|....*...
gi 1134749654 540 GQIVEIGPRRAVFenpqhpyTRKLLAAV 567
Cdd:COG1120 214 GRIVAQGPPEEVL-------TPELLEEV 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
314-546 |
3.46e-35 |
|
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: 132.24 E-value: 3.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlsp 393
Cdd:cd03263 1 LQIRNLTKTYK---------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gKLQALRRDIQFIFQDpyASLDPRQTIGDSIIEPLRVHGlLPGKEAVARVAWLLERVGLLPeHAWRYPHEFSGGQRQRIC 473
Cdd:cd03263 69 -DRKAARQSLGYCPQF--DALFDELTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
355-581 |
3.50e-35 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 135.31 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPgklqALRRDIQFIFQDpYAsLDPRQTIGDSIIEPLRVHGLl 434
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVP----PHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 435 PGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFG 514
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 515 IAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVAEPS---RQRPQRVL 581
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATvieRKSEQVVL 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-197 |
6.41e-35 |
|
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: 129.30 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRdvielseqsaaqmrHVRGADMAMIFQ 111
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER--------------KSLRKEIGYVFQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EPmtSLNPVFTVGEQIAESIRLHQNASREEAmVEAKRMLDQVRIPE-AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:pfam00005 67 DP--QLFPRLTVRENLRLGLLLKGLSKREKD-ARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 1134749654 191 IADEPTT 197
Cdd:pfam00005 144 LLDEPTA 150
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
339-555 |
8.59e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 135.46 E-value: 8.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsL 414
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-----RHVNTVFQS-YA-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK09452 98 FPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
330-541 |
1.08e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 128.90 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQd 409
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL---EELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 410 pyasldprqtigdsiieplrvhgllpgkeavarvawllervgllpehawrypheFSGGQRQRICIARALALNPKVIIADE 489
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
311-537 |
1.19e-34 |
|
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: 131.02 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN--GQRI 388
Cdd:COG4778 2 TTLLEVENLSKTFTLH----LQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 389 D--TLSPGKLQALRRDI-----QFifqdpyasLD--PRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWR 459
Cdd:COG4778 78 DlaQASPREILALRRRTigyvsQF--------LRviPRVSALDVVAEPLLERGV-DREEARARARELLARLNL-PERLWD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 460 -YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVM 537
Cdd:COG4778 148 lPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
314-541 |
1.53e-34 |
|
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: 128.65 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
Cdd:cd03228 1 IEFKNVSFSYP---------GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gkLQALRRDIQFIFQDPYasLDPRqTIGDSIieplrvhgllpgkeavarvawllervgllpehawrypheFSGGQRQRIC 473
Cdd:cd03228 71 --LESLRKNIAYVPQDPF--LFSG-TIRENI---------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQ 541
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-245 |
1.54e-34 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 130.55 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLvqcDKmllrRRSRDVI--- 88
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS----TLLHLL---GGL---DN----PTSGEVLfng 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 -ELSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPH 167
Cdd:TIGR02211 67 qSLSKLSSNERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPL-LIGKKSVKEAKERAYEMLEKVGLEHR---INHRPS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
Cdd:TIGR02211 141 ELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDG 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-597 |
1.67e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 134.96 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPLRsgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:PRK11607 18 PLLEIRNLTKSFDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPgklqaLRRDIQFIFQDpYAsLDPRQTIGDSIIEPLRvHGLLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQR 471
Cdd:PRK11607 87 PP-----YQRPINMMFQS-YA-LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 552 FENPQHPYTRKLLAAVPVAE---------------PSRQRPQRVL----LSDDLPSNIHLRGEEV 597
Cdd:PRK11607 238 YEHPTTRYSAEFIGSVNVFEgvlkerqedglvidsPGLVHPLKVDadasVVDNVPVHVALRPEKI 302
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-261 |
1.94e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.90 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLE--QAGGLVQCDkmllrrrsrDVIELSE 92
Cdd:PRK11124 5 LNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEmpRSGTLNIAG---------NHFDFSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 Q-SAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSG 171
Cdd:PRK11124 71 TpSDKAIRELR-RNVGMVFQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKP---YADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
250
....*....|
gi 1134749654 252 TVEQiFHAPQ 261
Cdd:PRK11124 224 DASC-FTQPQ 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-256 |
2.07e-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: 130.75 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqAGglvqcdkmLLRRRSRDVIELSEQS 94
Cdd:COG4555 4 VENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKT-T---LLRML--AG--------LLKPDSGSILIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 AAQMRHVRgADMAMIFQEPMtsLNPVFTVGEQIAESIRLHQNaSREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMR 174
Cdd:COG4555 66 RKEPREAR-RQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLEE---FLDRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGTVE 254
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
..
gi 1134749654 255 QI 256
Cdd:COG4555 218 EL 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
311-560 |
3.81e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 130.28 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGLLNrvtrevhavekVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNG 385
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNS-----------VSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 386 Q-----RIDTLSpgklqaLRRDIQFIFQDPyaslDP-RQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWR 459
Cdd:PRK14239 72 HniyspRTDTVD------LRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 460 YpHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVA 535
Cdd:PRK14239 142 L-HDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|....*
gi 1134749654 536 VMYLGQIVEIGPRRAVFENPQHPYT 560
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
342-546 |
4.61e-34 |
|
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: 128.95 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 342 KVSFDLwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-DTLSPGKLQALRRDIQFIFQDpyASLDPRQTI 420
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQRKIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIIEPLRVHGLLPGKEavaRVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:cd03297 93 RENLAFGLKRKRNREDRI---SVDELLDLLGL--DHlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1134749654 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-252 |
1.14e-33 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 128.32 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 8 DAGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDkmllrrrSRD 86
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPtSGTVRLA-------GQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 87 VIELSEQSAAQmrhVRGADMAMIFQEPMtsLNPVFTVGEQIAESIRLhqnASREEAMVEAKRMLDQV----RipeaqtiL 162
Cdd:COG4181 76 LFALDEDARAR---LRARHVGFVFQSFQ--LLPTLTALENVMLPLEL---AGRRDARARARALLERVglghR-------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVM 242
Cdd:COG4181 141 DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRL 219
|
250
....*....|
gi 1134749654 243 YQGEAVETGT 252
Cdd:COG4181 220 RAGRLVEDTA 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
30-265 |
1.30e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqaGGLVQCDkmllrrrsRDVIELSEQSAAQMRHVRGADMAMI 109
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTT----LLRII---AGLETPD--------SGRIVLNGRDLFTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMtsLNPVFTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:COG1118 81 FQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEG---LADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYT 265
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-542 |
1.45e-33 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 134.57 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMllrrrSRDVI-ELSEQSAAQMRHVRGADMA 107
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKS----TLMKIL---SGVYPHGTW-----DGEIYwSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEPMtsLNPVFTVGEQI--AESIRLHQNASREEAMV-EAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALS 184
Cdd:TIGR02633 82 IIHQELT--LVPELSVAENIflGNEITLPGGRMAYNAMYlRAKNLLRELQLDADNV--TRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETgtveqifhapqhpy 264
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT-------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 265 trallaavpqlGAMKGLDYPRRFPLIsLEHPAKQAPPIEQKTVvdGEPVLRVRNLVTRFPlrsgllnrVTREVHAVEKVS 344
Cdd:TIGR02633 223 -----------KDMSTMSEDDIITMM-VGREITSLYPHEPHEI--GDVILEARNLTCWDV--------INPHRKRVDDVS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIDTLSPgkLQALRRDIQFIFQD-PYASLDPRQTIGD 422
Cdd:TIGR02633 281 FSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNP--AQAIRAGIAMVPEDrKRHGIVPILGVGK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SIIepLRVHGLLPGKEAVARVAWL------LERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:TIGR02633 359 NIT--LSVLKSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1134749654 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
314-542 |
1.65e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 125.97 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03230 1 IEVRNLSKRY-----------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gklqALRRDIQFIFQDP--YASLDPRQTIgdsiieplrvhgllpgkeavarvawllervgllpehawryphEFSGGQRQR 471
Cdd:cd03230 70 ----EVKRRIGYLPEEPslYENLTVRENL------------------------------------------KLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
311-550 |
2.08e-33 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 127.55 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQ 386
Cdd:COG4181 6 APIIELRGLTKTVGTGAG-------ELTILKGISLEVEAGESVAIVGASGSGKST----LLGLLagldRPTSGTVRLAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 387 RIDTLSPGKLQALRRD-IQFIFQdpyaS--LDPRQTIGDSIIEPLRVHGLlpgKEAVARVAWLLERVGL--LPEHawrYP 461
Cdd:COG4181 75 DLFALDEDARARLRARhVGFVFQ----SfqLLPTLTALENVMLPLELAGR---RDARARARALLERVGLghRLDH---YP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQ 541
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*....
gi 1134749654 542 IVEIGPRRA 550
Cdd:COG4181 224 LVEDTAATA 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
339-571 |
3.31e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPR 417
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:PRK10070 121 MTVLDNTAFGMELAGI-NAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVAE 571
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQ 272
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-269 |
3.52e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.56 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFmQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQC-DKMLLRRRSrdvieLSE 92
Cdd:PRK11264 6 VKNLVKKF-HGQT---VLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQpEAGTIRVgDITIDTARS-----LSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAaQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGG 172
Cdd:PRK11264 76 QKG-LIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|....*..
gi 1134749654 253 VEQIFHAPQHPYTRALL 269
Cdd:PRK11264 228 AKALFADPQQPRTRQFL 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
344-564 |
3.93e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.79 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 344 SFDLW--PGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDP--YASLD 415
Cdd:COG3840 17 RFDLTiaAGERVAILGPSGAGKST----LLNLIagflPPDSGRILWNGQDLTALPPAE-----RPVSMLFQENnlFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGdsiiepLRVH-GLLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:COG3840 88 VAQNIG------LGLRpGLKLTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLL 564
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-559 |
5.71e-33 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 134.58 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 292 LEHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL 371
Cdd:COG2274 452 LDLPPEREEGRSKLSLPRLKGDIELENVSFRYP---------GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 372 RLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYasldprqTIGDSIIEPLRVHGLLPGKEAV---ARVAWLLE 448
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDP---ASLRRQIGVVLQDVF-------LFSGTIRENITLGDPDATDEEIieaARLAGLHD 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 449 RVGLLP--------EHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFI 520
Cdd:COG2274 593 FIEALPmgydtvvgEGG----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--III 666
|
250 260 270
....*....|....*....|....*....|....*....
gi 1134749654 521 SHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
Cdd:COG2274 667 AHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-261 |
7.36e-33 |
|
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: 126.20 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqaGGLVQCDKMLLRRRSRDVIELSeqsaAQMRHVRgadmaMIF 110
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLI---AGFETPTSGEILLDGKDITNLP----PHKRPVN-----TVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03300 79 QN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEG---YANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQ 261
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-552 |
1.35e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.77 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtLSPGKLQALRRDIQFIFQDPyaslD 415
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRHKIGMVFQNP----D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PR---QTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:PRK13650 92 NQfvgATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAVF 552
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
311-559 |
1.38e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridt 390
Cdd:COG1121 4 MPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 lspgKLQALRRDIQFIFQdpYASLDPRQtigdsiiePLRVH-----------GLL--PGKEAVARVAWLLERVGLLpEHA 457
Cdd:COG1121 69 ----PPRRARRRIGYVPQ--RAEVDWDF--------PITVRdvvlmgrygrrGLFrrPSRADREAVDEALERVGLE-DLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 458 WRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVM 537
Cdd:COG1121 134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL 212
|
250 260
....*....|....*....|....
gi 1134749654 538 yLGQIVEIGPRRAVF--ENPQHPY 559
Cdd:COG1121 213 -NRGLVAHGPPEEVLtpENLSRAY 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
292-546 |
1.69e-32 |
|
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: 132.19 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 292 LEHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPLRSGLLNrvtrevhaveKVSFDLWPGETLSLVGESGSGKSTTGRALL 371
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALD----------GLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 372 RLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYasldprqTIGDSIIEPLRVHGLLPGKEAVARVawlLERVG 451
Cdd:COG4988 385 GFLPPYSGSILINGVDLSDLDP---ASWRRQIAWVPQNPY-------LFAGTIRENLRLGRPDASDEELEAA---LEAAG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 452 L------LP--------EHAWRypheFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAY 517
Cdd:COG4988 452 LdefvaaLPdgldtplgEGGRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTV 525
|
250 260
....*....|....*....|....*....
gi 1134749654 518 LFISHDMAVVERISHRVaVMYLGQIVEIG 546
Cdd:COG4988 526 ILITHRLALLAQADRIL-VLDDGRIVEQG 553
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-246 |
1.77e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrdviELSE 92
Cdd:COG4619 1 LELEGLSFRV--GGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK----------PLSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHvrgaDMAMIFQEPmtslnPVF--TVGEQIAESIRLHQNASREEamvEAKRMLDQVRIPEAqtILSRYPHQLS 170
Cdd:COG4619 67 MPPPEWRR----QVAYVPQEP-----ALWggTVRDNLPFPFQLRERKFDRE---RALELLERLGLPPD--ILDKPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-267 |
1.99e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.53 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 4 SDELDAGNVLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTAL-ALMRLLE-----QAGGLVQCDK 77
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKS-TLLrCLNRMNDlipgaRVEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 78 MLLRRRSRDVIELSeqsaaqmRHVrgadmAMIFQEPmtslNPvF--TVGEQIAESIRLHQNASREE--AMVEakRMLDQV 153
Cdd:COG1117 78 EDIYDPDVDVVELR-------RRV-----GMVFQKP----NP-FpkSIYDNVAYGLRLHGIKSKSEldEIVE--ESLRKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 154 RI-PEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVV 232
Cdd:COG1117 139 ALwDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT--IVIVTHNMQQA 216
|
250 260 270
....*....|....*....|....*....|....*
gi 1134749654 233 AEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRA 267
Cdd:COG1117 217 ARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
343-567 |
3.32e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPG-KLQALRRDIQFIFQDPYasLDPRQTIG 421
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvDERLIRQEAGMVFQQFY--LFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 422 DSII-EPLRVHGLlpGKEAVARVAW-LLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:PRK09493 96 ENVMfGPLRVRGA--SKEEAEKQAReLLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 500 GQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAV 567
Cdd:PRK09493 173 HEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
15-261 |
4.20e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.35 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLE--QAGGLVQCDKMLlrrrsrdviELSE 92
Cdd:COG4161 5 LKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLEtpDSGQLNIAGHQF---------DFSQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 Q-SAAQMRHVRGaDMAMIFQEpmTSLNPVFTVGEQIAES-IRLhQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLS 170
Cdd:COG4161 71 KpSEKAIRLLRQ-KVGMVFQQ--YNLWPHLTVMENLIEApCKV-LGLSKEQAREKAMKLLARLRL---TDKADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
250
....*....|.
gi 1134749654 251 GTVEqIFHAPQ 261
Cdd:COG4161 223 GDAS-HFTQPQ 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
311-551 |
4.27e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsGllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
Cdd:COG1129 2 EPLLEMRGISKSFG---G--------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPgkLQALRRDIQFIFQDPyaSLDPRQTIGDSI---IEPLRvHGLLPGKEAVARVAWLLERVGlLPEHAWRYPHEFSGG 467
Cdd:COG1129 71 RSP--RDAQAAGIAIIHQEL--NLVPNLSVAENIflgREPRR-GGLIDWRAMRRRARELLARLG-LDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
....
gi 1134749654 548 RRAV 551
Cdd:COG1129 224 VAEL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-542 |
4.52e-32 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 130.05 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqAG----GLVQCDKmllrrrsrdVIELSEQSAAQMRHVRGADM 106
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKST----LMKVL--SGvyphGTYEGEI---------IFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 107 AMIFQEPMtsLNPVFTVGEQI--AESIRLHQNASREEAMVEAKRMLDQVR--IPEAQTILsryphQLSGGMRQRVMIAMA 182
Cdd:PRK13549 85 AIIHQELA--LVKELSVLENIflGNEITPGGIMDYDAMYLRAQKLLAQLKldINPATPVG-----NLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG-----TVEQIf 257
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRpaagmTEDDI- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 258 hapqhpytrallaavpqLGAMKGLDYPRRFPliSLEHPAkqappieqktvvdGEPVLRVRNLVTRFPlrsgllnrVTREV 337
Cdd:PRK13549 236 -----------------ITMMVGRELTALYP--REPHTI-------------GEVILEVRNLTAWDP--------VNPHI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRIDTLSPgkLQALRRDIQFIFQD------- 409
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNP--QQAIAQGIAMVPEDrkrdgiv 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 410 ---------PYASLDpRQTIGDSIIEPLRVHGLLpgkEAVARV----AWLLERVGLLpehawryphefSGGQRQRICIAR 476
Cdd:PRK13549 354 pvmgvgkniTLAALD-RFTGGSRIDDAAELKTIL---ESIQRLkvktASPELAIARL-----------SGGNQQKAVLAK 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 477 ALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-246 |
6.61e-32 |
|
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: 121.35 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIElse 92
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsaaqmrhvrgaDMAMIFQEPmtSLNPVFTVGEQIaesirlhqnasreeamveakrmldqvripeaqtilsryphQLSGG 172
Cdd:cd03230 74 ------------RIGYLPEEP--SLYENLTVRENL----------------------------------------KLSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
314-543 |
1.07e-31 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 120.61 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GklQALRRDIQFIFQdpyasldprqtigdsiieplrvhgllpgkeavarvawllervgllpehawrypheFSGGQRQRIC 473
Cdd:cd03216 70 R--DARRAGIAMVYQ-------------------------------------------------------LSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-264 |
1.53e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 122.83 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRDVIELSEQSAAQMrHVRGADMAMIF 110
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKT----TLLRLI--AG---------LERPDSGTILFGGEDATDV-PVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03296 81 QH--YALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPY 264
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-556 |
1.79e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.32 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDPyasldPRQ 418
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRKHIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGdSIIEPLRVHGL----LPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK13648 96 FVG-SIVKYDVAFGLenhaVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
312-534 |
2.34e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.85 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPlRSGLLNRVTREVhavekvSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:PRK11629 4 ILLQCDNLCKRYQ-EGSVQTDVLHNV------SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKLQALR-RDIQFIFQdpYASLDPRQTIGDSIIEPLRVHGLLPgKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQ 470
Cdd:PRK11629 77 SSAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLAAVGL-EHRANHRPSELSGGERQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
337-542 |
2.56e-31 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 121.36 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDP 416
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlpEHAWR-YPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:cd03292 92 DRNVYENVAFALEVTGV-PPREIRKRVPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1134749654 496 VSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03292 169 PDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-288 |
4.43e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 125.53 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRHVRGADMAMIF 110
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----------VDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLHQNASREEAmveaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK10070 113 QS--FALMPHMTVLDNTAFGMELAGINAEERR----EKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLA 270
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
250
....*....|....*...
gi 1134749654 271 AVPQLGAMKGLDYPRRFP 288
Cdd:PRK10070 267 GVDISQVFSAKDIARRTP 284
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
316-546 |
7.07e-31 |
|
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: 120.17 E-value: 7.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 316 VRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGK 395
Cdd:cd03265 3 VENLVKKY-----------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 396 LqalRRDIQFIFQDPyaSLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIA 475
Cdd:cd03265 71 V---RRRIGIVFQDL--SVDDELTGWENLYIHARLYGV-PGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 476 RALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-257 |
8.41e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.08 E-value: 8.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQ--QKIAaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSE 92
Cdd:PRK13637 5 IENLTHIYMEGTpfEKKA-LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----------VDITD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAaQMRHVRgADMAMIFQEPMTSLnpvF--TVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLS 170
Cdd:PRK13637 74 KKV-KLSDIR-KKVGLVFQYPEYQL---FeeTIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
....*..
gi 1134749654 251 GTVEQIF 257
Cdd:PRK13637 227 GTPREVF 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-287 |
1.47e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrdviel 90
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEK-YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAQMRHVRGadmaMIFQEPMTSLNPVfTVGEQIAESIRlHQNASREEaMVEakRMLDQVRIPEAQTILSRYPHQLS 170
Cdd:PRK13650 72 TEENVWDIRHKIG----MVFQNPDNQFVGA-TVEDDVAFGLE-NKGIPHEE-MKE--RVNEALELVGMQDFKEREPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAeIADRVLVMYQGEAVET 250
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVEST 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1134749654 251 GTVEQIFHAPQH--------PYTRALLAAVPQlgamKGLDYPRRF 287
Cdd:PRK13650 222 STPRELFSRGNDllqlgldiPFTTSLVQSLRQ----NGYDLPEGY 262
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
31-275 |
1.48e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 119.90 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqaGGLVQCDKMLLRRRSRDVIELseqsaaqmrHVRGADMAMIF 110
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKST----LLRII---AGLEQPDSGRIRLNGQDATRV---------HARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLHQ-NASREEAMVEakRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:TIGR00968 79 QH--YALFKHLTVRDNIAFGLEIRKhPKAKIKARVE--ELLELVQLEGLG---DRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALL 269
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
....*.
gi 1134749654 270 AAVPQL 275
Cdd:TIGR00968 232 GEVNVL 237
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
12-245 |
1.63e-30 |
|
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: 119.35 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqaGGLVQCDKMLLRRRSRDVIELS 91
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLI------GGLRSVQEGSLKVLGQELHGAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHVRGadmaMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSG 171
Cdd:TIGR02982 74 KKQLVQLRRRIG----YIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDH---LNYYPHNLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQG 245
Cdd:TIGR02982 145 GQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRIL-DVADRILQMEDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
336-554 |
2.28e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.92 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQDPYASLD 415
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 pRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK13637 98 -EETIEKDIAFGPINLGL-SEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-251 |
2.44e-30 |
|
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: 118.51 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqaGGLVQCDKMLLRRRSRDVIELSeqsaAQMRhvrgaDMAMIF 110
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMI---AGLEEPTSGRIYIGGRDVTDLP----PKDR-----DIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLHqNASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03301 79 QN--YALYPHMTVYDNIAFGLKLR-KVPKDEI---DERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-251 |
2.58e-30 |
|
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: 117.15 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 14 AVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTAL-ALMRLLEQAGGLVQCDKMLLRRRSRdvIELSE 92
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSSGEILLDGKDLASLSP--KELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QsaaqmrhvrgadMAMIFQepmtslnpvftvgeqiaesirlhqnasreeamveakrMLDQVRIpeaQTILSRYPHQLSGG 172
Cdd:cd03214 74 K------------IAYVPQ-------------------------------------ALELLGL---AHLADRPFNELSGG 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03214 102 ERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-256 |
3.88e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.01 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSvTAL-ALMRLLEQAGGLVQCDKmllrrrsrdvIEL 90
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVEPTSGEILVDG----------QDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAQMRHVRgADMAMIFQEP-----MTSLNPVFTvGeqiaesiRLHQNAS--------REEAMVEAKRMLDQVRIpe 157
Cdd:COG3638 68 TALRGRALRRLR-RRIGMIFQQFnlvprLSVLTNVLA-G-------RLGRTSTwrsllglfPPEDRERALEALERVGL-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 158 AQTILSRyPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIAD 237
Cdd:COG3638 137 ADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYAD 215
|
250
....*....|....*....
gi 1134749654 238 RVLVMYQGEAVETGTVEQI 256
Cdd:COG3638 216 RIIGLRDGRVVFDGPPAEL 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
338-565 |
4.32e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 119.30 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL----------SPGKLQALRRDIQFI 406
Cdd:PRK10619 18 HEVLKgVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 407 FQdpYASLDPRQTIGDSIIE-PLRVHGLlPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:PRK10619 98 FQ--HFNLWSHMTVLENVMEaPIQVLGL-SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLA 565
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-261 |
4.67e-30 |
|
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: 118.31 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCDKMLLRRRSRDVIELSE 92
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-T---LFNLI---SGFLRPTSGSVLFDGEDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRhvrgadMAMIFQEP-----MTSLNPVfTVGEQIA--ESIRLHQNASREEAMVE-AKRMLDQVRIPEaqtILSR 164
Cdd:cd03219 70 HEIARLG------IGRTFQIPrlfpeLTVLENV-MVAAQARtgSGLLLARARREEREARErAEELLERVGLAD---LADR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
Cdd:cd03219 140 PAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
250
....*....|....*..
gi 1134749654 245 GEAVETGTVEQIFHAPQ 261
Cdd:cd03219 219 GRVIAEGTPDEVRNNPR 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-546 |
6.43e-30 |
|
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: 116.00 E-value: 6.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQdpyasldprqt 419
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP---KELARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 igdsiieplrvhgllpgkeavarvawLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:cd03214 81 --------------------------ALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1134749654 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-257 |
8.78e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.96 E-value: 8.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 7 LDAGNVLAVENLNIAFMQDQ-QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQC------DKML 79
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 80 LRRRSRDVIELSEQSAAQMRHVrgadMAMIFQEPMTSLnpvF--TVGEQIA-ESIRLHQnaSREEAMVEAKRMLDQVRIP 156
Cdd:PRK13631 96 NHELITNPYSKKIKNFKELRRR----VSMVFQFPEYQL---FkdTIEKDIMfGPVALGV--KKSEAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 157 EaqTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIA 236
Cdd:PRK13631 167 D--SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVA 243
|
250 260
....*....|....*....|.
gi 1134749654 237 DRVLVMYQGEAVETGTVEQIF 257
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
338-543 |
9.74e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.90 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDpr 417
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHGlLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:PRK10908 94 RTVYDNVAIPLIIAG-ASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1134749654 498 IRGQIINLLLDLQRdFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK10908 172 LSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-257 |
1.16e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 14 AVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQ 93
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG----------ITISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 SAAQMRHVRGadmaMIFQEPmtslNPVF---TVGEQIAESIrlhqnasrEEAMVEAKRMLD-------QVRIPEaqtILS 163
Cdd:PRK13632 77 NLKEIRKKIG----IIFQNP----DNQFigaTVEDDIAFGL--------ENKKVPPKKMKDiiddlakKVGMED---YLD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAeIADRVLVMY 243
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFS 216
|
250
....*....|....
gi 1134749654 244 QGEAVETGTVEQIF 257
Cdd:PRK13632 217 EGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-261 |
1.41e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.58 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRdVIElSEQSAAQMRHVRgADMAMIF 110
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKST-------LLQHLNGLLQPTSGTVTIGER-VIT-AGKKNKKLKPLR-KKVGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSLnpvF--TVGEQIAESirlHQN--ASREEAMVEAKRMLDQVRIPEAqtILSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:PRK13634 92 QFPEHQL---FeeTVEKDICFG---PMNfgVSEEDAKQKAREMIELVGLPEE--LLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQ 261
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
29-273 |
1.41e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 120.98 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTAL-ALMRLLEQAGGLVQCDkmllrrrSRDVIELSEqsaAQMRHVRGADMA 107
Cdd:COG4175 40 TVGVNDASFDVEEGEIFVIMGLSGSGKS-TLVrCLNRLIEPTAGEVLID-------GEDITKLSK---KELRELRRKKMS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEpmtslnpvF------TVGEQIAESIRLhQNASREEAMVEAKRMLDQVRipeaqtiLS----RYPHQLSGGMRQRV 177
Cdd:COG4175 109 MVFQH--------FallphrTVLENVAFGLEI-QGVPKAERRERAREALELVG-------LAgwedSYPDELSGGMQQRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 178 MIAMALSCRPAVLIADEPTTALDVTIQAQiLQ--LIKvLQKEMSMGVIFITHDMgvvAE---IADRVLVMYQGEAVETGT 252
Cdd:COG4175 173 GLARALATDPDILLMDEAFSALDPLIRRE-MQdeLLE-LQAKLKKTIVFITHDL---DEalrLGDRIAIMKDGRIVQIGT 247
|
250 260
....*....|....*....|.
gi 1134749654 253 VEQIFHAPQHPYTRALLAAVP 273
Cdd:COG4175 248 PEEILTNPANDYVADFVEDVD 268
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
32-356 |
1.50e-29 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 120.10 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKML--LRRRSRDVIELSEqsaaqmrHVRGadMAMI 109
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTT-------LLRAIAGFVKAAGLTgrIAIADRDLTHAPP-------HKRG--LALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEpmTSLNPVFTVGEQIAESIRlhqnASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:TIGR03258 85 FQN--YALFPHLKVEDNVAFGLR----AQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEM-SMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRAL 268
Cdd:TIGR03258 159 LLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 269 LAAVPQLGAMK-GLDYPRRFPLISLEHPAKQAPPIEQKTVVDGEPVLRVRNL-VTRFPLRSGLLNRVTREVHavekvsfd 346
Cdd:TIGR03258 239 LGAANILPAIAlGITEAPGLVDVSCGGAVIFAFGDGRHDGRDKLACIRPEHLaLTPRPAGEGRFHATIASVE-------- 310
|
330
....*....|
gi 1134749654 347 lWPGETLSLV 356
Cdd:TIGR03258 311 -WHGAALHLL 319
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
289-565 |
1.59e-29 |
|
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: 123.34 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 289 LISLEHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGR 368
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 369 ALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYAsldprqtIGDSIIEPLRVhgllpGKEAV--ARVAWL 446
Cdd:COG4987 380 LLLRFLDPQSGSITLGGVDLRDLDE---DDLRRRIAVVPQRPHL-------FDTTLRENLRL-----ARPDAtdEELWAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 447 LERVGL------LPE--HAWRYPH--EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIa 516
Cdd:COG4987 445 LERVGLgdwlaaLPDglDTWLGEGgrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV- 523
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1134749654 517 yLFISHDMAVVERIsHRVAVMYLGQIVEIGPRRAVFEnpQHPYTRKLLA 565
Cdd:COG4987 524 -LLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-262 |
2.59e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.41 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRL---LEQA-GGLVQCDkmllrrrSRDVI 88
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKS-T---LLRMiagLEDPtSGEILIG-------GRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 ELseqsAAQMRhvrgaDMAMIFQEPMtsLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQ 168
Cdd:COG3839 69 DL----PPKDR-----NIAMVFQSYA--LYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLED---LLDRKPKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD----MGvvaeIADRVLVMYQ 244
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMND 209
|
250
....*....|....*...
gi 1134749654 245 GEAVETGTVEQIFHAPQH 262
Cdd:COG3839 210 GRIQQVGTPEELYDRPAN 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
311-556 |
3.05e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.01 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridT 390
Cdd:PRK13632 5 SVMIKVENVSFSYP---------NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPGKLQALRRDIQFIFQDPyasldPRQTIGdSIIEPLRVHGL----LPGKEAVARVAWLLERVGLLpEHAWRYPHEFSG 466
Cdd:PRK13632 73 ISKENLKEIRKKIGIIFQNP-----DNQFIG-ATVEDDIAFGLenkkVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAvvERI-SHRVAVMYLGQIVEI 545
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD--EAIlADKVIVFSEGKLIAQ 223
|
250
....*....|.
gi 1134749654 546 GPRRAVFENPQ 556
Cdd:PRK13632 224 GKPKEILNNKE 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-256 |
3.88e-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: 115.16 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVielseqsaaqmRHVRGadmaMIF 110
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-----------RRRIG----IVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPmtSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQTILSRYphqLSGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03265 80 QDL--SVDDELTGWENLYIHARL-YGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-245 |
5.13e-29 |
|
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: 114.70 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQ-----RGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKMLLRRrSRDVIELSEQSaaqmRHVrgadm 106
Cdd:cd03297 9 RLPDFTLKidfdlNEEVTGIFGASGAGKS-TLLRCIAGLEKPdGGTIVLNGTVLFD-SRKKINLPPQQ----RKI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 107 AMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREeamVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:cd03297 78 GLVFQQ--YALFPHLNVRENLAFGLKRKRNREDR---ISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:cd03297 150 PELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-551 |
6.64e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.45 E-value: 6.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqaLRRDIQFIFQDpyasld 415
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEG------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 pRQTIGD-SIIEPLRVHGLLPGKEAV-ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:cd03224 84 -RRIFPElTVEENLLLGAYARRRAKRkARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 494 LDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:cd03224 163 LAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
314-546 |
1.30e-28 |
|
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: 113.62 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLrsgllnrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSp 393
Cdd:cd03266 2 ITADALTKRFRD-------VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gKLQALRRDIQFIFQDpyASLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRIC 473
Cdd:cd03266 72 -EPAEARRRLGFVSDS--TGLYDRLTARENLEYFAGLYGL-KGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMAT-RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
350-555 |
1.43e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.13 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQalRRDIQFIFQDpYAsLDPRQTIGDSIIEPLR 429
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQ--QRDICMVFQS-YA-LFPHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 430 VHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
Cdd:PRK11432 105 MLGV-PKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIREL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1134749654 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK11432 183 QQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
339-547 |
1.51e-28 |
|
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: 113.74 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY------- 411
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 412 ASLDPRQTIGDSIIEplrvhgllpgkEAVARVAwLLERVGLLPEHAwRYPHE-----FSGGQRQRICIARALALNPKVII 486
Cdd:cd03244 96 SNLDPFGEYSDEELW-----------QALERVG-LKEFVESLPGGL-DTVVEeggenLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 487 ADEAVSALDVSIRGQIINLlldLQRDF-GIAYLFISHdmavveRI-----SHRVAVMYLGQIVEIGP 547
Cdd:cd03244 163 LDEATASVDPETDALIQKT---IREAFkDCTVLTIAH------RLdtiidSDRILVLDKGRVVEFDS 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-255 |
1.73e-28 |
|
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: 120.25 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 4 SDELDAGNVLAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrr 83
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING------ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 84 srdvIELSEQSAAQMRhvrgADMAMIFQEPmtslnpvFTVGEQIAESIRLHQNASREEAMVEAkrmLDQVRIPEA----- 158
Cdd:COG4988 399 ----VDLSDLDPASWR----RQIAWVPQNP-------YLFAGTIRENLRLGRPDASDEELEAA---LEAAGLDEFvaalp 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 159 ---QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEi 235
Cdd:COG4988 461 dglDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT--VILITHRLALLAQ- 537
|
250 260
....*....|....*....|
gi 1134749654 236 ADRVLVMYQGEAVETGTVEQ 255
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEE 557
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-257 |
2.17e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.03 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTAL-ALMRLLEQAGGLVQCDKMLLRRRSRDViel 90
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLPPTSGTVRLFGKPPRRARRRI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 seqsaaqmrhvrgadmAMIFQepMTSLNPVF--TVGEQIA----ESIRLHQNASREEAMVeAKRMLDQVripEAQTILSR 164
Cdd:COG1121 78 ----------------GYVPQ--RAEVDWDFpiTVRDVVLmgryGRRGLFRRPSRADREA-VDEALERV---GLEDLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMyQ 244
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-N 213
|
250
....*....|...
gi 1134749654 245 GEAVETGTVEQIF 257
Cdd:COG1121 214 RGLVAHGPPEEVL 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-545 |
2.31e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 119.12 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVQCDKMLLRRRSRDVIELSEQSAAQMrhvrgaDMAM 108
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLS---GIHEPTKGTITINNINYNKLDHKLAAQL------GIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQE-----PMTSLNPVFtVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMAL 183
Cdd:PRK09700 85 IYQElsvidELTVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIfhapqhp 263
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 264 ytrallAAVPQLGAMKGLDYPRRFPLISLEHpakqappieqkTVVDGEPVLRVRNLvtrfplrsgllnrVTREVHAVEKV 343
Cdd:PRK09700 233 ------SNDDIVRLMVGRELQNRFNAMKENV-----------SNLAHETVFEVRNV-------------TSRDRKKVRDI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 344 SFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgkLQALRRDIQFIFQDP-----YASLDPRQ 418
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAYITESRrdngfFPNFSIAQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIgdSIIEPLRVHGLlpgkeavaRVAWllervGLLPEHAWRYP-------------------HEFSGGQRQRICIARALA 479
Cdd:PRK09700 361 NM--AISRSLKDGGY--------KGAM-----GLFHEVDEQRTaenqrellalkchsvnqniTELSGGNQQKVLISKWLC 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-257 |
2.33e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.88 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDvielseqsaAQMRHVRgADMAMIF 110
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKD---------KYIRPVR-KRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSLnpvF--TVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13646 92 QFPESQL---FedTVEREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIF 257
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-264 |
2.42e-28 |
|
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: 116.67 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVIELSE 92
Cdd:TIGR03265 5 LSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKT----TLLRII---AGLERQTAGTIYQGGRDITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAaqmrhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGG 172
Cdd:TIGR03265 74 QKR---------DYGIVFQS--YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:TIGR03265 139 QQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGT 218
|
250
....*....|..
gi 1134749654 253 VEQIFHAPQHPY 264
Cdd:TIGR03265 219 PQEIYRHPATPF 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-242 |
3.11e-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: 112.91 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFM---QDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeQAGGLVQCDKMLLRRRSRdVI 88
Cdd:COG4778 4 LLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCI-YGNYLPDSGSILVRHDGG-WV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 ELSEQSAAQMRHVRGADMAMIFQepmtSLNPVFTVG--EQIAESIrLHQNASREEAMVEAKRMLDQVRIPEAqtILSRYP 166
Cdd:COG4778 78 DLAQASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPL-LERGVDREEARARARELLARLNLPER--LWDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-256 |
3.47e-28 |
|
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: 113.16 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELS 91
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLE-------GTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHvrgaDMAMIFQE-----PMTSLNPVFT--VGEQ--IAESIRLHQNASREEAMveakRMLDQVRIpeAQTIL 162
Cdd:TIGR02315 71 GKKLRKLRR----RIGMIFQHynlieRLTVLENVLHgrLGYKptWRSLLGRFSEEDKERAL----SALERVGL--ADKAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 163 SRyPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:TIGR02315 141 QR-ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGL 219
|
250
....*....|....
gi 1134749654 243 YQGEAVETGTVEQI 256
Cdd:TIGR02315 220 KAGEIVFDGAPSEL 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-285 |
4.67e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 24 QDQQKIAaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrDVIElsEQSAAQMRHVRG 103
Cdd:PRK13633 19 ESTEKLA-LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL-------DTSD--EENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 admaMIFQEPMTSLnpVFT-VGEQIA----------ESIRlhqnaSREEAMVEAKRMLDQVRIPeaqtilsryPHQLSGG 172
Cdd:PRK13633 89 ----MVFQNPDNQI--VATiVEEDVAfgpenlgippEEIR-----ERVDESLKKVGMYEYRRHA---------PHLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGT 252
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
250 260 270
....*....|....*....|....*....|....*
gi 1134749654 253 VEQIFhapqhpytrallaavPQLGAMK--GLDYPR 285
Cdd:PRK13633 228 PKEIF---------------KEVEMMKkiGLDVPQ 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
340-525 |
5.32e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.80 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRAL---LRLVESQGGEIIFNGQRIDTlspgkLQALRRDIQFIFQDPYasLDP 416
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLLNGRRLTA-----LPAEQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIGDSIIEPLRVHglLPGKEAVARVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:COG4136 90 HLSVGENLAFALPPT--IGRAQRRARVEQALEEAG-LAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*....
gi 1134749654 497 SIRGQIINLLLDLQRDFGIAYLFISHDMA 525
Cdd:COG4136 167 ALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-261 |
5.42e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.74 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 14 AVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTAlalmRLLEqagGLVQCDKMLLRRRSRDVIELSEQ 93
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLIN---GLLLPDDNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 SAAQMRHVRGadmaMIFQEPMTSLNPVfTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGM 173
Cdd:PRK13640 78 TVWDIREKVG----IVFQNPDNQFVGA-TVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYI---DSEPANLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGTV 253
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSP 227
|
....*...
gi 1134749654 254 EQIFHAPQ 261
Cdd:PRK13640 228 VEIFSKVE 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
343-546 |
5.47e-28 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 112.63 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YASldprqTI 420
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPvlFDG-----TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIieplrVHGLLPGK----EAVARVAWLLERVGLLPEhawRY-----PH--EFSGGQRQRICIARALALNPKVIIADE 489
Cdd:cd03249 94 AENI-----RYGKPDATdeevEEAAKKANIHDFIMSLPD---GYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-562 |
5.91e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 113.22 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ---------RIDTLSpgklqaLRRDIQFIFQDPYASldPRQTIGDS 423
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIK------LRKEVGMVFQQPNPF--PHLSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 424 IIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRY---PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
Cdd:PRK14246 111 IAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 501 QIINLLLDLQRDfgIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRK 562
Cdd:PRK14246 191 AIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
343-555 |
6.56e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 115.18 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTtgraLLRLV---ESQ-GGEIIFNGQRIdtlspGKLQALRRDIQFIFQDpYAsLDPRQ 418
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTT----LLRIIaglEHQtSGHIRFHGTDV-----SRLHARDRKVGFVFQH-YA-LFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIIEPLRVhglLPGKE----AV--ARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:PRK10851 90 TVFDNIAFGLTV---LPRRErpnaAAikAKVTQLLEMVQL--AHlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-261 |
7.16e-28 |
|
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: 112.82 E-value: 7.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCD--KMLLRRRsrdviE 89
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKT-T---LFNLI---TGFYRPTsgRILFDGR-----D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 LSEQSAAQMRHvRGadMAMIFQepMTSLNPVFTVGE--QIAESIRLHQN------------ASREEAMVEAKRMLDQVRI 155
Cdd:COG0411 68 ITGLPPHRIAR-LG--IARTFQ--NPRLFPELTVLEnvLVAAHARLGRGllaallrlprarREEREARERAEELLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 156 peaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEI 235
Cdd:COG0411 143 ---ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGL 219
|
250 260
....*....|....*....|....*.
gi 1134749654 236 ADRVLVMYQGEAVETGTVEQIFHAPQ 261
Cdd:COG0411 220 ADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
338-537 |
7.67e-28 |
|
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: 111.47 E-value: 7.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgKLQALRRDIQFIFQDPYASLDPR 417
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK--------PLEKERKRIGYVPQRRSIDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVH-GLL--PGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:cd03235 85 ISVRDVVLMGLYGHkGLFrrLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1134749654 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVM 537
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-270 |
8.56e-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: 8.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 2 PHSDELDAGNVLAVENLniAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
Cdd:COG4987 323 AEPAPAPGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG---- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 82 rrsrdvIELSEQSAAQMRHVrgadMAMIFQEPmtslnPVF--TvgeqIAESIRL-HQNASrEEAMVEAkrmLDQVRI--- 155
Cdd:COG4987 397 ------VDLRDLDEDDLRRR----IAVVPQRP-----HLFdtT----LRENLRLaRPDAT-DEELWAA---LERVGLgdw 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 156 ----PEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMg 230
Cdd:COG4987 454 laalPDGlDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT--VLLITHRL- 530
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1134749654 231 VVAEIADRVLVMYQGEAVETGTVEQIfhAPQHPYTRALLA 270
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEEL--LAQNGRYRQLYQ 568
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-546 |
1.07e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.83 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgklqALRRDIQFIFQDpyASL 414
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AARNRIGYLPEE--RGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSIIEPLRVHGlLPGKEAVARVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:cd03269 82 YPKMKVIDQLVYLAQLKG-LKKEEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03269 160 DPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
334-554 |
1.10e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKLQALRRDIQFIFQDPyas 413
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 ldpRQTIGDSIIEPLRVHGL----LPGKEAVARVAWLLERVGLlpehaWRY----PHEFSGGQRQRICIARALALNPKVI 485
Cdd:PRK13633 95 ---DNQIVATIVEEDVAFGPenlgIPPEEIRERVDESLKKVGM-----YEYrrhaPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM-AVVEriSHRVAVMYLGQIVEIGPRRAVFEN 554
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-272 |
1.20e-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: 113.74 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 47 IVGESGSGKSVtalaLMRLLeqaGGLVQCDKMLLRRRSRDVIELseqsAAQMRHVrgadmAMIFQEpmTSLNPVFTVGEQ 126
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLL---AGFEQPDSGSIMLDGEDVTNV----PPHLRHI-----NMVFQS--YALFPHMTVEEN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 127 IAESIRLhQNASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQ 206
Cdd:TIGR01187 63 VAFGLKM-RKVPRAEI---KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 207 ILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLAAV 272
Cdd:TIGR01187 139 MQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-242 |
1.50e-27 |
|
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: 110.32 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVqcdkmllrRRSRDVIELSEQS 94
Cdd:cd03235 2 VEDLTVSY--GGHPV--LEDVSFEVKPGEFLAIVGPNGAGKS----TLLKAIL---GLL--------KPTSGSIRVFGKP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 AAQMRHV-------RGADMAMifqePMTSLNpvfTVGEQIAESIRLHQNASREEaMVEAKRMLDQVRIPEaqtILSRYPH 167
Cdd:cd03235 63 LEKERKRigyvpqrRSIDRDF----PISVRD---VVLMGLYGHKGLFRRLSKAD-KAKVDEALERVGLSE---LADRQIG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
310-542 |
1.69e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.44 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 310 GEPVLRVRNLVTRfplrsgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
Cdd:cd03215 1 GEPVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 TLSPGklQALRRDIQFIFQDPyasldprqtigdsiieplRVHGLLPGkEAVARVAWLlervgllpehawryPHEFSGGQR 469
Cdd:cd03215 66 RRSPR--DAIRAGIAYVPEDR------------------KREGLVLD-LSVAENIAL--------------SSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
30-299 |
1.87e-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: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLV--------QCDKMLLRRRSRDVIelseQSAAqmrh 100
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRMInRLIEPTSGRIlidgedirDLDPVELRRRIGYVI----QQIG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 101 vrgadmamifqepmtsLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQTiLSRYPHQLSGGMRQRVMIA 180
Cdd:COG1125 87 ----------------LFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEEY-RDRYPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1134749654 261 QHPYTRALL---AAVPQLGAMKGLDYPRR-FPLISLEHPAKQA 299
Cdd:COG1125 229 ANDFVADFVgadRGLRRLSLLRVEDLMLPePPTVSPDASLREA 271
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-272 |
1.89e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRSRDVielseqsaaqmRHVRgADMAMIFQE 112
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEEiTSGDLIVDGLKVNDPKVDE-----------RLIR-QEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 pmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
Cdd:PRK09493 86 --FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAER---AHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 193 DEPTTALDVTIQAQILQLIKVLQKE-MSMgvIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLAA 271
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEgMTM--VIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQH 238
|
.
gi 1134749654 272 V 272
Cdd:PRK09493 239 V 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
312-523 |
2.21e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtl 391
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKLQALrrdiqfIFQDpyASLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQR 471
Cdd:COG4525 73 GPGADRGV------VFQK--DALLPWLNVLDNVAFGLRLRGV-PKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-542 |
2.62e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 115.87 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLEqagGLVQCDKMLLRRRSRDVielseqSAAQMRHVRGADMAMIF 110
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKST----MMKVLT---GIYTRDAGSILYLGKEV------TFNGPKSSQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmtsLN--PVFTvgeqIAESIRLHQNASREEAMVEAKRMLDqvripEAQTILSRY-----PHQLSG----GMRQRVMI 179
Cdd:PRK10762 86 QE----LNliPQLT----IAENIFLGREFVNRFGRIDWKKMYA-----EADKLLARLnlrfsSDKLVGelsiGEQQMVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIfha 259
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 260 pqhpyTRALLaavpqLGAMKGldypRRfplisLEhpaKQAPPIEQKTvvdGEPVLRVRNLvtrfplrSGLlnrvtrevhA 339
Cdd:PRK10762 229 -----TEDSL-----IEMMVG----RK-----LE---DQYPRLDKAP---GEVRLKVDNL-------SGP---------G 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyasldpRQ- 418
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQ--DGLANGIVYISED-------RKr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 ---TIGDSIIEPL---------RVHGLLPGKEAVARVAWLLE-----------RVGLLpehawryphefSGGQRQRICIA 475
Cdd:PRK10762 339 dglVLGMSVKENMsltalryfsRAGGSLKHADEQQAVSDFIRlfniktpsmeqAIGLL-----------SGGNQQKVAIA 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 476 RALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-279 |
2.73e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.21 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 9 AGNVLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA--GGLVQCDKMLLRRRSRD 86
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPseGSIVVNGQTINLVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 87 ViELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTIlsRYP 166
Cdd:PRK10619 77 G-QLKVADKNQLRLLR-TRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG--KYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGE 246
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGK 229
|
250 260 270
....*....|....*....|....*....|...
gi 1134749654 247 AVETGTVEQIFHAPQHPYTRALLAavpqlGAMK 279
Cdd:PRK10619 230 IEEEGAPEQLFGNPQSPRLQQFLK-----GSLK 257
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-256 |
3.25e-27 |
|
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: 116.86 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQM 98
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG----------IDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHvrgaDMAMIFQEPMtslnpVF--TvgeqIAESIRLHQNASREEAMVEAKRM--LDQV--RIPEA-QTILSRYPHQLSG 171
Cdd:COG2274 548 RR----QIGVVLQDVF-----LFsgT----IRENITLGDPDATDEEIIEAARLagLHDFieALPMGyDTVVGEGGSNLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAeIADRVLVMYQGEAVETG 251
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT--VIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
....*
gi 1134749654 252 TVEQI 256
Cdd:COG2274 692 THEEL 696
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-289 |
4.59e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.87 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVIELSeqsaAQMRHVrgadmAMIFQEp 113
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKT----TLLRII---AGLEHQTSGHIRFHGTDVSRLH----ARDRKV-----GFVFQH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 114 mTSLNPVFTVGEQIAESIRL---HQNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK10851 83 -YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAH---LADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLA 270
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
250 260
....*....|....*....|...
gi 1134749654 271 AVPQL-GAMKGLDY---PRRFPL 289
Cdd:PRK10851 239 EVNRLqGTIRGGQFhvgAHRWPL 261
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-269 |
5.91e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.46 E-value: 5.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmQDQQKiaavrNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGlvqcdKMLLRRRSrdvieLS 91
Cdd:COG3840 2 LRLDDLTYRY-GDFPL-----RFDLTIAAGERVAILGPSGAGKS-TLLNLIAgFLPPDSG-----RILWNGQD-----LT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQmRHVrgadmAMIFQEpmTSLNPVFTVGEQIAESIR--LHQNASREEAMVEAkrmLDQVRIpeaQTILSRYPHQL 169
Cdd:COG3840 65 ALPPAE-RPV-----SMLFQE--NNLFPHLTVAQNIGLGLRpgLKLTAEQRAQVEQA---LERVGL---AGLLDRLPGQL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
250 260
....*....|....*....|
gi 1134749654 250 TGTVEQIFHAPQHPYTRALL 269
Cdd:COG3840 211 DGPTAALLDGEPPPALAAYL 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
313-544 |
6.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtLS 392
Cdd:PRK13642 4 ILEVENLVFKYEKES--------DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PGKLQALRRDIQFIFQDPYASLdPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRI 472
Cdd:PRK13642 73 AENVWNLRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGI-PREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVE 544
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
343-555 |
6.62e-27 |
|
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: 112.50 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-------QRIDtlspgkLQALRRDIQFIFQDpyASLD 415
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIF------LPPHRRRIGYVFQE--ARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:COG4148 90 PHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLD----RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
339-547 |
6.66e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.26 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasLdprq 418
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTF--L---- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 tIGDSIIEPLRVhgllpGK--------EAVARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPK 483
Cdd:COG1132 426 -FSGTIRENIRY-----GRpdatdeevEEAAKAAQAHEFIEALPD---GYDTVvgergvnLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 484 VIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGP 547
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGT 557
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-246 |
7.11e-27 |
|
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: 106.56 E-value: 7.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrdvielseqs 94
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG----------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 aaqmrhvrgadmamifqepmtslnpvftvgeqiaeSIRLHQNASREEAMVEAKRMLDQVripeaqtilsrypHQLSGGMR 174
Cdd:cd00267 55 -----------------------------------EILIDGKDIAKLPLEELRRRIGYV-------------PQLSGGQR 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd00267 87 QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-544 |
7.49e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 7.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvTalaLMRLL----EQAGGLVQCDKmllrrrsrdvielseqsaaqmrhvrGADMAM 108
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKS-T---LLKILagelEPDSGEVSIPK-------------------------GLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPmtSLNPVFTVGEQIAESIR------------LHQNASREEAMVE-------------------AKRMLDQVRIPE 157
Cdd:COG0488 66 LPQEP--PLDDDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERlaelqeefealggweaearAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 158 AQtiLSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQ--AQILqlikvlqKEMSMGVIFITHD------ 228
Cdd:COG0488 144 ED--LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEwlEEFL-------KNYPGTVLVVSHDryfldr 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 229 -MGVVAEIADRVLVMYQG----------------EAVETGTVEQI---------FHAPQHPYTRALlAAVPQLGAMKGLD 282
Cdd:COG0488 215 vATRILELDRGKLTLYPGnysayleqraerleqeAAAYAKQQKKIakeeefirrFRAKARKAKQAQ-SRIKALEKLEREE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 283 YPRRFPLISLEHPAKQAPpieqktvvdGEPVLRVRNLVTRFPlrsgllnrvTREVhaVEKVSFDLWPGETLSLVGESGSG 362
Cdd:COG0488 294 PPRRDKTVEIRFPPPERL---------GKKVLELEGLSKSYG---------DKTL--LDDLSLRIDRGDRIGLIGPNGAG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 363 KSTTGRALLRLVESQGGEIIFNgqriDTLSPGklqalrrdiqfIF-QDpYASLDPRQTIGDSIIEplrvhGLLPGKEAVA 441
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKLG----ETVKIG-----------YFdQH-QEELDPDKTVLDELRD-----GAPGGTEQEV 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 442 RVawLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFIS 521
Cdd:COG0488 413 RG--YLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVS 486
|
570 580
....*....|....*....|...
gi 1134749654 522 HDMAVVERISHRVAVMYLGQIVE 544
Cdd:COG0488 487 HDRYFLDRVATRILEFEDGGVRE 509
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
314-549 |
7.52e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 115.20 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLsp 393
Cdd:TIGR02203 331 VEFRNVTFRYP---------GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gKLQALRRDIQFIFQDPYASLDprqTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLP--------EHAWRypheFS 465
Cdd:TIGR02203 400 -TLASLRRQVALVSQDVVLFND---TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigENGVL----LS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEI 545
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVER 548
|
....
gi 1134749654 546 GPRR 549
Cdd:TIGR02203 549 GTHN 552
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-287 |
7.98e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 7.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrdviELS 91
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE----------LLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHvrgaDMAMIFQEPMTSLnpvftVGEQIAESIRL---HQNASREEAMVEAKRMLDQVRIPEAQTilsRYPHQ 168
Cdd:PRK13642 73 AENVWNLRR----KIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFKT---REPAR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1134749654 249 ETGTVEQIFHAPQH--------PYTRALLAAVpqlgAMKGLDYPRRF 287
Cdd:PRK13642 220 KEAAPSELFATSEDmveigldvPFSSNLMKDL----RKNGFDLPEKY 262
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-256 |
9.43e-27 |
|
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: 109.19 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrSRDVIELSE 92
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSV----------LIDGTDINK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHVRgADMAMIFQEPmtSLNPVFTVGEQIaesirLHQNASR------------EEAMVEAKRMLDQVRIPEaqt 160
Cdd:cd03256 68 LKGKALRQLR-RQIGMIFQQF--NLIERLSVLENV-----LSGRLGRrstwrslfglfpKEEKQRALAALERVGLLD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
Cdd:cd03256 137 KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIV 216
|
250
....*....|....*.
gi 1134749654 241 VMYQGEAVETGTVEQI 256
Cdd:cd03256 217 GLKDGRIVFDGPPAEL 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
342-559 |
1.08e-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: 111.74 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG-KLQALRRDIQFIFQDpyASLDPRQTI 420
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIieplrVHGL--LPGKEAVARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:TIGR02142 93 RGNL-----RYGMkrARPSERRISFERVIELLGI--GHLLgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-272 |
1.09e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.80 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 9 AGNVLAVENLNIAFMQDqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS---- 84
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGK----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifny 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 85 RDVIELSEQsaaqmrhvrgadMAMIFQEPmtslNPV-FTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEA-QTIL 162
Cdd:PRK14271 94 RDVLEFRRR------------VGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVM 242
Cdd:PRK14271 158 SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQAARISDRAALF 235
|
250 260 270
....*....|....*....|....*....|
gi 1134749654 243 YQGEAVETGTVEQIFHAPQHPYTRALLAAV 272
Cdd:PRK14271 236 FDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-567 |
1.14e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.80 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES-----QGGEIIFNGQRIdtLSPGKLQALRRDIQFIFQDPyasl 414
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRP---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DP-RQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGL---LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:PRK14271 111 NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAV 567
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-253 |
1.58e-26 |
|
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: 107.59 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqaGGLVqcdkmllrRRSRDVIELSEQS-AAQMRHVRGaDMAMI 109
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTT----LKML---TGEL--------RPTSGTAYINGYSiRTDRKAARQ-SLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMtsLNPVFTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03263 81 PQFDA--LFDELTVREHLRFYARLK-GLPKSEIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETGTV 253
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRS--IILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
313-556 |
1.98e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPLRSGLLNRVtrevhavekvSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtLS 392
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGI----------NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 PGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHglLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRI 472
Cdd:PRK13639 70 KKSLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNLG--LSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
....
gi 1134749654 553 ENPQ 556
Cdd:PRK13639 226 SDIE 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
27-249 |
2.01e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.45 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLL---EQA-GGLVQCDKMLLRRRSRDVIelseqsaAQMRhvR 102
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLygeERPtSGQVLVNGQDLSRLKRREI-------PYLR--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 103 gaDMAMIFQEpmtslnpvF------TVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQR 176
Cdd:COG2884 80 --RIGVVFQD--------FrllpdrTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKemsMG--VIFITHDMGVVAEIADRVLVMYQGEAVE 249
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR---RGttVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-265 |
2.57e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.08 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS---RDV 87
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDifkMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 IELSeqsaaqmRHVRgadmaMIFQEPmtslNPV--FTVGEQIAESIRLHQNA-SREEAMVEAKRMLDQVRI-PEAQTILS 163
Cdd:PRK14247 78 IELR-------RRVQ-----MVFQIP----NPIpnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMY 243
Cdd:PRK14247 142 APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT--IVLVTHFPQQAARISDYVAFLY 219
|
250 260
....*....|....*....|..
gi 1134749654 244 QGEAVETGTVEQIFHAPQHPYT 265
Cdd:PRK14247 220 KGQIVEWGPTREVFTNPRHELT 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-265 |
2.63e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrSRDVIELSeqsAAQMRHvrgaDMAMI 109
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF-GKDIFQID---AIKLRK----EVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPmtSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK14246 96 FQQP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYT 265
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-551 |
2.70e-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: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtls 392
Cdd:COG4152 1 MLELKGLTKRF-----------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 393 pgklQALRRDIQFIfqdP-----YasldPRQTIGDSIIEPLRVHGlLPGKEAVARVAWLLERVGlLPEHAWRYPHEFSGG 467
Cdd:COG4152 67 ----PEDRRRIGYL---PeerglY----PKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLG-LGDRANKKVEELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 468 QRQRICIARALALNPKVIIADEAVSALD-VSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDpVN-VELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*
gi 1134749654 547 PRRAV 551
Cdd:COG4152 212 SVDEI 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
336-544 |
3.01e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 106.53 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQDP--YAS 413
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK-----SYQKNIEALRRIGALIEAPgfYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 LDPRqtigdsiiEPLRVHGLLPGKEAvARVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:cd03268 87 LTAR--------ENLRLLARLLGIRK-KRIDEVLDVVG-LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 494 LD-VSIRgQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
Cdd:cd03268 157 LDpDGIK-ELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
343-547 |
8.14e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 106.16 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprqTIGD 422
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAIGVVPQDTVLFND---TIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SIieplRVHGLLPGKEAV---ARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:cd03253 94 NI----RYGRPDATDEEVieaAKAAQIHDKIMRFPD---GYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 493 ALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGP 547
Cdd:cd03253 167 ALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-257 |
8.25e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 106.16 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSEQSAAQM 98
Cdd:cd03254 7 NVNFSYDEKKPV-LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-------GIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 rhvrgadMAMIFQEPmtslnpvFTVGEQIAESIRL-HQNASREEAMVEAK--RMLDQV-RIPEA-QTILSRYPHQLSGGM 173
Cdd:cd03254 79 -------IGVVLQDT-------FLFSGTIMENIRLgRPNATDEEVIEAAKeaGAHDFImKLPNGyDTVLGENGGNLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGTV 253
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRT--SIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
....
gi 1134749654 254 EQIF 257
Cdd:cd03254 222 DELL 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
335-553 |
8.25e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 106.16 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasl 414
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQDTF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 dprqTIGDSIIEPLRVHGLLPGKEAVARVAwllERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPKV 484
Cdd:cd03254 88 ----LFSGTIMENIRLGRPNATDEEVIEAA---KEAGAhdfimkLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 485 IIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
28-256 |
8.91e-26 |
|
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: 107.86 E-value: 8.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRDVIelseQSAAQMRHVrgadMA 107
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTA-------RVAGYDVV----REPRKVRRS----IG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEPmtSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:TIGR01188 70 IVPQYA--SVDEDLTGRENLEMMGRL-YGLPKDEAEERAEELLELFELGEAA---DRPVGTYSGGMRRRLDIAASLIHQP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:TIGR01188 144 DVLFLDEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-246 |
1.13e-25 |
|
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: 103.62 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRHVrgadMAMIF 110
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----------VDLRDLDLESLRKN----IAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMtslnpVF--TVGEQIaesirlhqnasreeamveakrmldqvripeaqtilsryphqLSGGMRQRVMIAMALSCRPA 188
Cdd:cd03228 83 QDPF-----LFsgTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGE 246
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKT--VIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-257 |
1.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIELSEQsaaqmrhvrgadMAMIF 110
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKT------------VGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSLnpvF--TVGEQIAESiRLHQNASREEamVEaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13639 85 QNPDDQL---FapTVEEDVAFG-PLNLGLSKEE--VE-KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIF 257
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-260 |
1.53e-25 |
|
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: 108.26 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 36 SFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKMLLRRRSRDVIELSEQsaaqmRHVrgadmAMIFQEPm 114
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKT-TLLRAIAGLERPdSGRIRLGGEVLQDSARGIFLPPHR-----RRI-----GYVFQEA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 tSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDqvrIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
Cdd:COG4148 87 -RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLG---I---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-546 |
1.64e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 105.26 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDpyaSLDPRQ 418
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP---AWLRRQVGVVLQE---NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSII---EPLRVHGLlpgkEAVARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:cd03252 91 SIRDNIAladPGMSMERV----IEAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 492 SALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-566 |
1.68e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.27 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPlrsgllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG-----GEIIFNGQ 386
Cdd:PRK14258 6 PAIKVNNLSFYYD---------TQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 387 RIDTLSPgKLQALRRDIQFIFQDPyaSLDPrQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPE---HAWRYPHE 463
Cdd:PRK14258 75 NIYERRV-NLNRLRRQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEikhKIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY----- 538
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenr 230
|
250 260
....*....|....*....|....*...
gi 1134749654 539 LGQIVEIGPRRAVFENPQHPYTRKLLAA 566
Cdd:PRK14258 231 IGQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
311-556 |
1.87e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 105.06 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
Cdd:COG0410 1 MPMLEVENLHAGYG-----------GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPGKLqaLRRDIQFIFQDpyasldpRQTIGD-SIIEPLRVhGLLPGKEAvARVAWLLERV-GLLP---EHAWRYPHEFS 465
Cdd:COG0410 70 LPPHRI--ARLGIGYVPEG-------RRIFPSlTVEENLLL-GAYARRDR-AEVRADLERVyELFPrlkERRRQRAGTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
250
....*....|.
gi 1134749654 546 GPRRAVFENPQ 556
Cdd:COG0410 218 GTAAELLADPE 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
311-555 |
2.58e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.46 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFplrSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
Cdd:PRK11300 3 QPLLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LsPGKLQAlRRDIQFIFQDpyASLDPRQTIgdsiIEPLRV--H-----GLLPG-----------KEAVARVAWLLERVGL 452
Cdd:PRK11300 72 L-PGHQIA-RMGVVRTFQH--VRLFREMTV----IENLLVaqHqqlktGLFSGllktpafrraeSEALDRAATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 453 LpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISH 532
Cdd:PRK11300 144 L-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISD 222
|
250 260
....*....|....*....|...
gi 1134749654 533 RVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK11300 223 RIYVVNQGTPLANGTPEEIRNNP 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-260 |
3.34e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 107.73 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDkmllrrrSRDVIELSeqsaAQMRHVRgadmaMI 109
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGFETPdSGRIMLD-------GQDITHVP----AENRHVN-----TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEpmTSLNPVFTVGEQIAESIRLhQNASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:PRK09452 92 FQS--YALFPHMTVFENVAFGLRM-QKTPAAEI---TPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
338-552 |
5.56e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGkLQALRRDIQFIFQDPYASLDPR 417
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMKLRESVGMVFQDPDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHglLPGKEAVARVAWLLERVGLlpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:PRK13636 99 SVYQDVSFGAVNLK--LPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
33-240 |
5.97e-25 |
|
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: 102.69 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrDVIELSEQSAAQMRHvrgADMAMIFQ 111
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKfDSGQVYLNGQ-------ETPPLNSKKASKFRR---EKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 epmtslNPVFTVGEQIAESIRL---HQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:TIGR03608 84 ------NFALIENETVEENLDLglkYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMgVVAEIADRVL 240
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-242 |
7.90e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCdkmllrrrSRDVIELSE 92
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTT-------LLNLIAGFLAP--------SSGEITLDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQmrhvRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGG 172
Cdd:COG4525 69 VPVTG----PGADRGVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFA---RRRIWQLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmgvVAE---IADRVLVM 242
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVM 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-262 |
9.27e-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: 102.93 E-value: 9.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRDVIElseqsaaqmrhvRGADMAMIFQ 111
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST-------LLNLISGLAQPTSGGVILEGKQITE------------PGPDRMVVFQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EpmTSLNPVFTVGEQIA---ESIRLHQNASREEAMVEakRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:TIGR01184 62 N--YSLLPWLTVRENIAlavDRVLPDLSKSERRAIVE--EHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 189 VLIADEPTTALDVTIQAQIL-QLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI-FHAPQH 262
Cdd:TIGR01184 135 VLLLDEPFGALDALTRGNLQeELMQIWE-EHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-543 |
1.13e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 107.95 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLL-------EQAGGLVQCDKmllRRRSRDvIELSEQsaaqmrhvRG 103
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKST----LMKVLsgvyphgSYEGEILFDGE---VCRFKD-IRDSEA--------LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 adMAMIFQE----PMTSlnpvftvgeqIAESIRL-HQNASR-----EEAMVEAKRMLDQVRIPEA-QTILSryphQLSGG 172
Cdd:NF040905 80 --IVIIHQElaliPYLS----------IAENIFLgNERAKRgvidwNETNRRARELLAKVGLDESpDTLVT----DIGVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGT 252
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 253 VEQifhapqhpytrallAAVPQ---LGAMKGLDYPRRFPlislehpaKQAPPIeqktvvdGEPVLRVRNLVTRFPLRSGl 329
Cdd:NF040905 223 CRA--------------DEVTEdriIRGMVGRDLEDRYP--------ERTPKI-------GEVVFEVKNWTVYHPLHPE- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 lnrvtREVhaVEKVSFDLWPGETLSLVGESGSGK-----STTGRALLRLVesqGGEIIFNGQRIDTLSPGKlqALRRDIQ 404
Cdd:NF040905 273 -----RKV--VDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGRNI---SGTVFKDGKEVDVSTVSD--AIDAGLA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 405 fifqdpYASLDpRQTIGDSIIEPLRVHGLLPGKEAVARVAWL-----------------------LERVGLLpehawryp 461
Cdd:NF040905 341 ------YVTED-RKGYGLNLIDDIKRNITLANLGKVSRRGVIdeneeikvaeeyrkkmniktpsvFQKVGNL-------- 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 hefSGGQRQRICIARALALNPKVIIADEAVSALDV----SIRGqIINLLLDLqrdfGIAYLFISHDMAVVERISHRVAVM 537
Cdd:NF040905 406 ---SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYT-IINELAAE----GKGVIVISSELPELLGMCDRIYVM 477
|
....*.
gi 1134749654 538 YLGQIV 543
Cdd:NF040905 478 NEGRIT 483
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-284 |
3.32e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.99 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVqcdkmllrRRSRDVIEL------SEQSAAQMRHVRgADMA 107
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKST-------LMQHFNALL--------KPSSGTITIagyhitPETGNKNLKKLR-KKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEPMTSLnpvF--TVGEQIaESIRLHQNASREEAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PRK13641 89 LVFQFPEAQL---FenTVLKDV-EFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIF-------- 257
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsdkewlkk 241
|
250 260
....*....|....*....|....*..
gi 1134749654 258 HAPQHPYTrALLAAVPQLGAMKGLDYP 284
Cdd:PRK13641 242 HYLDEPAT-SRFASKLEKGGFKFSEMP 267
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-546 |
3.58e-24 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 101.54 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprq 418
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQIGLVSQDVFLFND--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSI------IEPLRVhgllpgkEAVARVAWLLERVGLLPEHawrYPHE-------FSGGQRQRICIARALALNPKVI 485
Cdd:cd03251 91 TVAENIaygrpgATREEV-------EEAARAANAHEFIMELPEG---YDTVigergvkLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-252 |
4.88e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 8 DAGNVL-AVENLNIAFMQDQQKiAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMllrrrsr 85
Cdd:PRK13657 327 DLGRVKgAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLqRVFDPQSGRILIDGT------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 86 DVIELSEQSaaqMRHvrgaDMAMIFQEPMTsLNpvftvgEQIAESIRL-HQNASREEAMVEAKRmldqvriPEAQTILSR 164
Cdd:PRK13657 398 DIRTVTRAS---LRR----NIAVVFQDAGL-FN------RSIEDNIRVgRPDATDEEMRAAAER-------AQAHDFIER 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVA 233
Cdd:PRK13657 457 KPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVR 534
|
250
....*....|....*....
gi 1134749654 234 EiADRVLVMYQGEAVETGT 252
Cdd:PRK13657 535 N-ADRILVFDNGRVVESGS 552
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-313 |
5.86e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.15 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLEQAGGLVQCDKMLlrrrsrDVIELS 91
Cdd:PRK11607 19 LLEIRNLTKSF--DGQ--HAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGFEQPTAGQIML------DGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMrhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171
Cdd:PRK11607 85 HVPPYQR------PINMMFQS--YALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM---QEFAKRKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQI-LQLIKVLQKemsMGV--IFITHDMGVVAEIADRVLVMYQGEAV 248
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER---VGVtcVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 249 ETGTVEQIFhapQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAP--PIEQKTVVDGEPV 313
Cdd:PRK11607 230 QIGEPEEIY---EHPTTRYSAEFIGSVNVFEGVLKERQEDGLVIDSPGLVHPlkVDADASVVDNVPV 293
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-256 |
6.37e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.49 E-value: 6.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVI-----ElseqsaaqmrhvRGad 105
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgylpeE------------RG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 106 mamifqepmtsLNPVFTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIPEAQT--IlsrypHQLSGGMRQRVMIAMAL 183
Cdd:COG4152 82 -----------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANkkV-----EELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 184 SCRPAVLIADEPTTALDVtIQAQILQliKVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:COG4152 145 LHDPELLILDEPFSGLDP-VNVELLK--DVIRELAAKGttVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
343-523 |
6.87e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.56 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYASLDprqTIGD 422
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIYRQQVSYCAQTPTLFGD---TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SIIEPLRVHGLLPGKEAVARVawlLERVGLlPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
Cdd:PRK10247 100 NLIFPWQIRNQQPDPAIFLDD---LERFAL-PDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180
....*....|....*....|..
gi 1134749654 502 IINLLLDLQRDFGIAYLFISHD 523
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHD 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-228 |
6.98e-24 |
|
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: 99.86 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqAGglvqcdkmlLRRRSRDVIELS 91
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKT-T---LLRIL--AG---------LLPPSAGEVLWN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHVRGADMAMIFQEPMtsLNPVFTVGEQIAESIRLHQNASREEAMVEAkrmLDQVRIPEAqtiLSRYPHQLSG 171
Cdd:COG4133 63 GEPIRDAREDYRRRLAYLGHADG--LKPELTVRENLRFWAALYGLRADREAIDEA---LEAVGLAGL---ADLPVRQLSA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHD 228
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-252 |
7.62e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.02 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKS-VTALaLMRLLEQAGGLVQCDKMLLRRRSRDVIelseqsaaqMRHVrgadmAMI 109
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKStLVNL-LLRFYDPTSGRILIDGVDIRDLTLESL---------RRQI-----GVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMtslnpVF--TvgeqIAESIRL-HQNASREEaMVEAKRM--LDQV--RIPEA-QTILSRYPHQLSGGMRQRVMIAM 181
Cdd:COG1132 420 PQDTF-----LFsgT----IRENIRYgRPDATDEE-VEEAAKAaqAHEFieALPDGyDTVVGERGVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGT 252
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGRT--TIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-251 |
7.77e-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: 100.13 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrDVieLSE 92
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF-------DV--VKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRhvrgadmaMIFQEPMTSLNPVFTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGG 172
Cdd:cd03266 73 PAEARRR--------LGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEE---LLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-557 |
1.01e-23 |
|
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: 100.23 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklqalrrDIQFIFQDpyASLDPRQT 419
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP--------DRMVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIEPL-RVHGLLPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
Cdd:TIGR01184 71 VRENIALAVdRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM------YLGQIVEIG---PRR--AVFENPQH 557
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPfprPRDrlEVVEDPSY 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
337-555 |
1.51e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.61 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV---ES-QGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYA 412
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVaglERiTSGEIWIGGRVVNELEPAD-----RDIAMVFQN-YA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 sLDPRQTIGDSIIEPLRVHGLlpGKEA----VARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIAD 488
Cdd:PRK11650 87 -LYPHMSVRENMAYGLKIRGM--PKAEieerVAEAARILELEPLLD----RKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMavVE--RISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ--VEamTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
336-556 |
1.58e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDPYASL 414
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSIIEPLRVhGLLPGKEAVARVAWLlERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK13641 99 FENTVLKDVEFGPKNF-GFSEDEAKEKALKWL-KKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
310-543 |
1.79e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 310 GEPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
Cdd:COG3845 2 MPPALELRGITKRFG-----------GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 TLSPGklQALRRDIQFIFQDPyaSLDPRQTIGDSII---EPLRvHGLLPGKEAVARVAWLLERVGL-LPEHAwrYPHEFS 465
Cdd:COG3845 71 IRSPR--DAIALGIGMVHQHF--MLVPNLTVAENIVlglEPTK-GGRLDRKAARARIRELSERYGLdVDPDA--KVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDvsirGQIINLLLDLQRDF---GIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLT----PQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
.
gi 1134749654 543 V 543
Cdd:COG3845 220 V 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
336-572 |
1.80e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.85 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQA------LRRDIQFIFQD 409
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI----PANLKKikevkrLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 410 PYASLDPRQTIGDSIIEPlrVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:PRK13645 99 PEYQLFQETIEKDIAFGP--VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENpqhpytRKLLAAVPV 569
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLTKIEI 250
|
...
gi 1134749654 570 AEP 572
Cdd:PRK13645 251 DPP 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
302-555 |
1.97e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 302 IEQKTVVDGEPVLRVRNLVTRFPlrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
Cdd:PRK13631 10 LKVPNPLSDDIILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 382 ----IFNGQRIDTLSPG---------KLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHglLPGKEAVARVAWLLE 448
Cdd:PRK13631 84 qvgdIYIGDKKNNHELItnpyskkikNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALG--VKKSEAKKLAKFYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 449 RVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVE 528
Cdd:PRK13631 162 KMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVL 240
|
250 260
....*....|....*....|....*..
gi 1134749654 529 RISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK13631 241 EVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-260 |
2.86e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLvqcdkmlLRRRSRDVIELSEQ-SAAQMRHVRGAdMA 107
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKST-------LFRHFNGI-------LKPTSGSVLIRGEPiTKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEPMtslNPVF--TVGEQIAESirlHQNASREEAMVeAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PRK13652 82 LVFQNPD---DQIFspTVEQDIAFG---PINLGLDEETV-AHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
336-556 |
3.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGR---ALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPya 412
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKlinGLLLPDDNPNSKITVDGI---TLTAKTVWDIREKVGIVFQNP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 slDPR---QTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
Cdd:PRK13640 94 --DNQfvgATVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-255 |
3.43e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 98.84 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSEQSaaqm 98
Cdd:cd03253 5 NVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-------GQDIREVTLDS---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 rhVRGAdMAMIFQEpmtslNPVF--TVGEQIAESiRLhqNASREEaMVEAKR--MLDQ--VRIPEA-QTILSRYPHQLSG 171
Cdd:cd03253 73 --LRRA-IGVVPQD-----TVLFndTIGYNIRYG-RP--DATDEE-VIEAAKaaQIHDkiMRFPDGyDTIVGERGLKLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQGEAVET 250
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAaLRDVSKGRTT---IVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
....*
gi 1134749654 251 GTVEQ 255
Cdd:cd03253 217 GTHEE 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-265 |
3.79e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-----QAGGLVQCDKMLLRRRSR 85
Cdd:PRK14267 3 FAIETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 86 DVIELSEQsaaqmrhvrgadMAMIFQEPmtslNPV--FTVGEQIAESIRLHQNA-SREEAMVEAKRMLDQVRI-PEAQTI 161
Cdd:PRK14267 79 DPIEVRRE------------VGMVFQYP----NPFphLTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALwDEVKDR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLV 241
Cdd:PRK14267 143 LNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAF 220
|
250 260
....*....|....*....|....
gi 1134749654 242 MYQGEAVETGTVEQIFHAPQHPYT 265
Cdd:PRK14267 221 LYLGKLIEVGPTRKVFENPEHELT 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
339-546 |
3.86e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.89 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDPRq 418
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNIAVVFQD--AGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 tigdSIIEPLRVhgllpGK---------EAVARVA---WLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
Cdd:PRK13657 424 ----SIEDNIRV-----GRpdatdeemrAAAERAQahdFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 487 ADEAVSALDVSIRGQIINLLLDLQRD---FGIAylfisHDMAVVeRISHRVAVMYLGQIVEIG 546
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGrttFIIA-----HRLSTV-RNADRILVFDNGRVVESG 551
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
350-546 |
4.21e-23 |
|
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: 97.56 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTtgraLLRLVE----SQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQDP--YASLDPRQTIGDS 423
Cdd:cd03298 24 GEITAIVGPSGSGKST----LLNLIAgfetPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENnlFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 424 IIEPLRVHgllpgKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
Cdd:cd03298 95 LSPGLKLT-----AEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1134749654 504 NLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-543 |
5.02e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 102.68 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRrrsrdvIELSEQSAAQMRHVRGADMAMIF 110
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKS----TLLKIL---SGNYQPDAGSIL------IDGQEMRFASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVgeqiAESIRLHQNASR------EEAMVEAKRMLDQVRI---PEAQtiLSRyphqLSGGMRQRVMIAM 181
Cdd:PRK11288 86 QE--LHLVPEMTV----AENLYLGQLPHKggivnrRLLNYEAREQLEHLGVdidPDTP--LKY----LSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 182 ALScRPAVLIA-DEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETgtveqifHAP 260
Cdd:PRK11288 154 ALA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRYVAT-------FDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 261 QHPYTRALLaavpqLGAMKGLD----Y---PRrfPLislehpakqappieqktvvdGEPVLRVRNLVTRfPLRsgllnrv 333
Cdd:PRK11288 225 MAQVDRDQL-----VQAMVGREigdiYgyrPR--PL--------------------GEVRLRLDGLKGP-GLR------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 334 trevhavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDPYA- 412
Cdd:PRK11288 270 -------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR--DAIRAGIMLCPEDRKAe 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 SLDPRQTIGDSI-IEPLRVH---GLL--PGKEA-VARvawllERVGLL------PEHAWRYpheFSGGQRQRICIARALA 479
Cdd:PRK11288 341 GIIPVHSVADNInISARRHHlraGCLinNRWEAeNAD-----RFIRSLniktpsREQLIMN---LSGGNQQKAILGRWLS 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-257 |
7.72e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 7.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTAlALMRLLEQAGglvqcDKMLLRRRSRdvieLSEQSAAQM 98
Cdd:PRK13648 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIA-KLMIGIEKVK-----SGEIFYNNQA----ITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHvrgaDMAMIFQEPMTSLnpvftVGEQIAESIRLhqnaSREEAMVEAKRMldQVRIPEAQTILSRY------PHQLSGG 172
Cdd:PRK13648 82 RK----HIGIVFQNPDNQF-----VGSIVKYDVAF----GLENHAVPYDEM--HRRVSEALKQVDMLeradyePNALSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGT 252
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
....*
gi 1134749654 253 VEQIF 257
Cdd:PRK13648 226 PTEIF 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-245 |
7.75e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.58 E-value: 7.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQcdkmllrRRSRDVI--- 88
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKST-------LLHLLGGLDT-------PTSGDVIfng 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 -ELSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQNASREEAMVEAKRMLDQVRIpeAQTILSRyPH 167
Cdd:PRK11629 71 qPMSKLSSAAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL--EHRANHR-PS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
Cdd:PRK11629 145 ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDG 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-248 |
9.38e-23 |
|
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: 96.56 E-value: 9.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFmQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRdvielseqs 94
Cdd:cd03226 2 IENISFSY-KKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 aaqmrhVRGADMAMifQEPMTSLnpvF--TVGEQIAESIRlhqNASREEAMVEAkrMLDQVRIPEAQtilSRYPHQLSGG 172
Cdd:cd03226 70 ------RKSIGYVM--QDVDYQL---FtdSVREELLLGLK---ELDAGNEQAET--VLKDLDLYALK---ERHPLSLSGG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAV 248
Cdd:cd03226 131 QKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-246 |
1.06e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 95.58 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAfmqdqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS-RDVIEL 90
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 -----SEQsaaqmRHVRGadmamifqepmtsLNPVFTVGEQIAesirlhqnasreeamveakrmldqvripeaqtilsrY 165
Cdd:cd03215 76 giayvPED-----RKREG-------------LVLDLSVAENIA------------------------------------L 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:cd03215 102 SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
.
gi 1134749654 246 E 246
Cdd:cd03215 181 R 181
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
29-246 |
1.16e-22 |
|
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: 96.55 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAgglvqcdkmllRRRSRDVIELSEQSAAQMRHVRGA---- 104
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLYGA-----------LTPSRGQVRIAGEDVNRLRGRQLPllrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 105 DMAMIFQEpmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALS 184
Cdd:TIGR02673 80 RIGVVFQD--FRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEHK---ADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
169-545 |
1.29e-22 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 101.34 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 249 ETG-----TVEQIfhapqhpytrallaavpqLGAMKGLDYPRRFPlislehpakqappieQKTVVDGEPVLRVRNLVTrf 323
Cdd:PRK10982 214 ATQplaglTMDKI------------------IAMMVGRSLTQRFP---------------DKENKPGEVILEVRNLTS-- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 324 plrsglLNRVTrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgkLQALRRDI 403
Cdd:PRK10982 259 ------LRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA--NEAINHGF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 404 QFIFQDP-----YASLDprqtIG-DSIIEPLRVH----GLLPGKEAVARVAWLLERVGL-LPEHAWRYpHEFSGGQRQRI 472
Cdd:PRK10982 326 ALVTEERrstgiYAYLD----IGfNSLISNIRNYknkvGLLDNSRMKSDTQWVIDSMRVkTPGHRTQI-GSLSGGNQQKV 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL-QRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEI 545
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-543 |
1.31e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 96.50 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDP---YA 412
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP---ADLRRNIGYVPQDVtlfYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 SLDPRQTIGDSIIEPLRVhgllpgkEAVARVAWLLERVGLLP--------EHAwrypHEFSGGQRQRICIARALALNPKV 484
Cdd:cd03245 93 TLRDNITLGAPLADDERI-------LRAAELAGVTDFVNKHPngldlqigERG----RGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 485 IIADEAVSALDVSIRGQIINLLLDLQRDfgIAYLFISHDMAVVERIShRVAVMYLGQIV 543
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVD-RIIVMDSGRIV 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-255 |
1.34e-22 |
|
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: 96.92 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQM 98
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG----------HDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RhvrgADMAMIFQEpmtslnpVFTVGEQIAESIRL-HQNASREEAMvEAKRM--LDQV--RIPEA-QTILSRYPHQLSGG 172
Cdd:cd03251 75 R----RQIGLVSQD-------VFLFNDTVAENIAYgRPGATREEVE-EAARAanAHEFimELPEGyDTVIGERGVKLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGEAVETGT 252
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRT--TFVIAHRLSTI-ENADRIVVLEDGKIVERGT 219
|
...
gi 1134749654 253 VEQ 255
Cdd:cd03251 220 HEE 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
334-542 |
1.63e-22 |
|
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: 96.39 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 334 TREVHAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYA 412
Cdd:cd03248 23 TRPDTLVLQdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 413 SldpRQTIGDSIIEPLRVHGLLPGKEAvARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIAD 488
Cdd:cd03248 100 F---ARSLQDNIAYGLQSCSFECVKEA-AQKAHAHSFISELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 489 EAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQI 542
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-249 |
2.20e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.00 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 9 AGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGglvQCDKMLLrrrSRDVI 88
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS---SGEVSLV---GQPLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 ELSEQSAAQMRhvrGADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQ 168
Cdd:PRK10584 76 QMDEEARAKLR---AKHVGFVFQSFM--LIPTLNALENV-ELPALLRGESSRQSRNGAKALLEQLGLGKR---LDHLPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
.
gi 1134749654 249 E 249
Cdd:PRK10584 226 E 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-524 |
2.82e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlSPGKLQALrrdiqfIFQDpyASLDPRQ 418
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGV------VFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
Cdd:PRK11248 86 NVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*.
gi 1134749654 499 RGQIINLLLDLQRDFGIAYLFISHDM 524
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
341-523 |
3.76e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 94.85 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTtgraLLR----LVESQGGEIIFNGQRIDTLSPgklqALRRDIQFIFqdPYASLDP 416
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRDARE----DYRRRLAYLG--HADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIGDSIIEPLRVHGLLPGKEAVARvawLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:COG4133 89 ELTVRENLRFWAALYGLRADREAIDE---ALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*..
gi 1134749654 497 SIRGQIINLLLDLQRDFGIAyLFISHD 523
Cdd:COG4133 165 AGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-250 |
4.70e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 93.26 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLEqagGLVQCDkmllrrrsrdvielseqsAAQMRhVRGadmam 108
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKS-T---LMKILS---GLYKPD------------------SGEIL-VDG----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 ifqEPMTSLNPvftvgeqiAESIRLHQnasreeAMVeakrmldqvripeaqtilsrypHQLSGGMRQRVMIAMALSCRPA 188
Cdd:cd03216 62 ---KEVSFASP--------RDARRAGI------AMV----------------------YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-260 |
6.62e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.48 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDkmllrrrSRDVIElseqSAAQMRhvrgaDMAMIFQE 112
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKT-TVLRLVAGLEKpTEGQIFID-------GEDVTH----RSIQQR-----DICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 pmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
Cdd:PRK11432 87 --YALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 193 DEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
293-546 |
7.02e-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: 99.77 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 293 EHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR 372
Cdd:TIGR02204 317 AEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARP--------DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 373 LVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPyasldprQTIGDSIIEPLR---VHGLLPGKEAVARVAWLLER 449
Cdd:TIGR02204 389 FYDPQSGRILLDGVDLRQLDP---AELRARMALVPQDP-------VLFAASVMENIRygrPDATDEEVEAAARAAHAHEF 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 450 VGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLLDLQRDfGIAYLFISHDMA 525
Cdd:TIGR02204 459 ISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALD-AESEQLVQQALETLMK-GRTTLIIAHRLA 536
|
250 260
....*....|....*....|.
gi 1134749654 526 VVERiSHRVAVMYLGQIVEIG 546
Cdd:TIGR02204 537 TVLK-ADRIVVMDQGRIVAQG 556
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
32-300 |
7.33e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLL----EQAGGLVQCDKMllrrrsrdviELSEQSAAQMRHVRgadmA 107
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKS-T---LLKLLtgelTPSSGEVRLNGR----------PLAAWSPWELARRR----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEpmTSLNPVFTVgeqiAESIRL-----HQNASREEAMVEakRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMA 182
Cdd:COG4559 79 VLPQH--SSLAFPFTV----EEVVALgraphGSSAAQDRQIVR--EALALV---GLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 183 L-------SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQ 255
Cdd:COG4559 148 LaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRG-GGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1134749654 256 IFhapqhpyTRALLAAVPQLgamkgldyprrfPLISLEHPAKQAP 300
Cdd:COG4559 227 VL-------TDELLERVYGA------------DLRVLAHPEGGCP 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
350-556 |
7.45e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRidTLSPGK----LQALRRDIQFIFQDPYASLDPRQTIGDSII 425
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GER--VITAGKknkkLKPLRKKVGIVFQFPEHQLFEETVEKDICF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 426 EPLRVHglLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
Cdd:PRK13634 110 GPMNFG--VSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEM 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 506 LLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK13634 188 FYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-251 |
8.94e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 93.88 E-value: 8.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIE-LS 91
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGyLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQsaaqmrhvRGadmamifqepmtsLNPVFTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
Cdd:cd03269 77 EE--------RG-------------LYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYA---NKRVEELSK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-568 |
1.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDPYASL 414
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DpRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK13646 99 F-EDTVEREIIFGPKNFKM-NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEnpQHPYTRKLLAAVP 568
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADWHIGLP 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-300 |
1.33e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ----AGGLVQCDkmllrrrSRDVIELSEQSAAQMRhvrgadmA 107
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGelspDSGEVRLN-------GRPLADWSPAELARRR-------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEpmTSLNPVFTVgEQIAESIRLHQNASREEAMVEAKRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMAL---- 183
Cdd:PRK13548 80 VLPQH--SSLSFPFTV-EEVVAMGRAPHGLSRAEDDALVAAALAQV---DLAHLAGRDYPQLSGGEQQRVQLARVLaqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 184 --SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFhapq 261
Cdd:PRK13548 154 epDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL---- 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 1134749654 262 hpyTRALLAAVPQLgamkgldyprrfPLISLEHPAKQAP 300
Cdd:PRK13548 230 ---TPETLRRVYGA------------DVLVQPHPETGAP 253
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-256 |
1.50e-21 |
|
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: 93.65 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRDVIELSE 92
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI-------RFDGRDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMrhvrGadMAMIFQEPMtsLNPVFTVgeqiAESIRLHQNASREEamvEAKRMLDQV--RIPEAQTILSRYPHQLS 170
Cdd:cd03224 70 HERARA----G--IGYVPEGRR--IFPELTV----EENLLLGAYARRRA---KRKARLERVyeLFPRLKERRKQLAGTLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
....*.
gi 1134749654 251 GTVEQI 256
Cdd:cd03224 214 GTAAEL 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-256 |
1.54e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.09 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLEqagglvqcdKMLLRRRSRDVIELSEQSAAQMRHVRgADMAMIF 110
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKST----LTKLIQ---------RFYVPENGRVLVDGHDLALADPAWLR-RQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmtslNPVFTvgEQIAESIRLHQNASREEAMVEAKRMLDQ----VRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:cd03252 83 QE-----NVLFN--RSIRDNIALADPGMSMERVIEAAKLAGAhdfiSELPEGyDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGTVEQI 256
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRT--VIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-265 |
1.76e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRL------LEQAGGLVQCDKMLLRRRSr 85
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGHNIYSPRT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 86 DVIELSEQsaaqmrhvrgadMAMIFQEPmtslNPV-FTVGEQIAESIRLhqNASREEAMVEA--KRMLDQVRI-PEAQTI 161
Cdd:PRK14239 80 DTVDLRKE------------IGMVFQQP----NPFpMSIYENVVYGLRL--KGIKDKQVLDEavEKSLKGASIwDEVKDR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEIADRVLV 241
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGF 219
|
250 260
....*....|....*....|....
gi 1134749654 242 MYQGEAVETGTVEQIFHAPQHPYT 265
Cdd:PRK14239 220 FLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-257 |
1.85e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIEL 90
Cdd:PRK13636 4 YILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEqsaaqmrhvrgaDMAMIFQEPMTSLNPVfTVGEQIAESIrLHQNASREEAMVEAKRMLDQVRIPEaqtiLSRYP-HQL 169
Cdd:PRK13636 81 RE------------SVGMVFQDPDNQLFSA-SVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGIEH----LKDKPtHCL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
Cdd:PRK13636 143 SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
....*...
gi 1134749654 250 TGTVEQIF 257
Cdd:PRK13636 223 QGNPKEVF 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
334-546 |
2.05e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.55 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYAS 413
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLRNQVALVSQNVHLF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 LDprqTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADE 489
Cdd:PRK11176 430 ND---TIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 490 AVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
338-546 |
2.24e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 92.64 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGeTLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQDPyaSLDPR 417
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIGYLPQEF--GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIgdsiIEPLRVHGLL---PGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:cd03264 87 FTV----REFLDYIAWLkgiPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 495 DVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
339-546 |
2.25e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 98.66 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYasldprq 418
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH---TLRQFINYLPQEPY------- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIIEPLrvhgLLPGKEAV-----------ARVAWLLERVGL-----LPEHAwrypHEFSGGQRQRICIARALALNP 482
Cdd:TIGR01193 559 IFSGSILENL----LLGAKENVsqdeiwaaceiAEIKDDIENMPLgyqteLSEEG----SSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 483 KVIIADEAVSALDVSIRGQIINLLLDLQRDFGIaylFISHDMAVVERiSHRVAVMYLGQIVEIG 546
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDKTII---FVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-246 |
2.71e-21 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 92.47 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIELSEQSaaqmrhvrgadMAM 108
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-----------IGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEpmTSLNPVFTVGEQIAESIRLHQnASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPA 188
Cdd:cd03292 83 VFQD--FRLLPDRNVYENVAFALEVTG-VPPREIRKRVPAALELVGLSHKH---RALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-251 |
3.18e-21 |
|
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: 92.17 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQ--RGETLAIVGESGSGKSvTALALMR--LLEQAGGLVqcdkmllrrrsrdvieLSEQSAAQMRHVRgADMAMI 109
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKS-TLLNLIAgfETPQSGRVL----------------INGVDVTAAPPAD-RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEpmTSLNPVFTVGEQI--AESIRLHQNASREEAMveaKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:cd03298 76 FQE--NNLFAHLTVEQNVglGLSPGLKLTAEDRQAI---EVALARVGL---AGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
339-555 |
3.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKLQALRRDIQFIFQDPYAsldprQ 418
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNPET-----Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIIEPLRV---HGLLPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:PRK13644 90 FVGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK13644 169 PDSGIAVLERIKKLHEK-GKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-564 |
3.86e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 93.68 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQ----GGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDP 416
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQiapdHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQhPYTRKLL 564
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFL 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
31-257 |
4.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMR--LLEQAGGLVQCDKmllrrrsrdVIELSEQSAAQMRHVRgADMAM 108
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKS-TMIQLTNglIISETGQTIVGDY---------AIPANLKKIKEVKRLR-KEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPMTSLnpvftVGEQIAESIR---LHQNASREEAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PRK13645 95 VFQFPEYQL-----FQETIEKDIAfgpVNLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIF 257
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
341-547 |
9.72e-21 |
|
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: 96.56 E-value: 9.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprQTI 420
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD---VQAVRRQLGVVLQNG-------RLM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIIEPLRVHGLLPGKEA--VARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:TIGR03797 540 SGSIFENIAGGAPLTLDEAweAARMAGLAEDIRAMPMGMHTVISEgggtLSGGQRQRLLIARALVRKPRILLFDEATSAL 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 495 DVSIRGQIINLLLDLQrdfgIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGP 547
Cdd:TIGR03797 620 DNRTQAIVSESLERLK----VTRIVIAHRLSTI-RNADRIYVLDAGRVVQQGT 667
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
349-534 |
1.39e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 90.99 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQTIgdsiIEP 427
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQS--FMLIPTLNA----LEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 428 LRVHGLLPG---KEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
Cdd:PRK10584 109 VELPALLRGessRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|
gi 1134749654 505 LLLDLQRDFGIAYLFISHDMAVVERISHRV 534
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
33-252 |
1.71e-20 |
|
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: 91.06 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSeqsaaqMRHVRgADMAMIFQE 112
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-------GVDIRDLN------LRWLR-SQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 PM---TSlnpvftvgeqIAESIRLHQNASREEAMVEAKRMldqvriPEAQTILSRYPH-----------QLSGGMRQRVM 178
Cdd:cd03249 86 PVlfdGT----------IAENIRYGKPDATDEEVEEAAKK------ANIHDFIMSLPDgydtlvgergsQLSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 179 IAMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQKEM-SMGVIFITHDMGVVAEiADRVLVMYQGEAVETGT 252
Cdd:cd03249 150 IARALLRNPKILLLDEATSALD-AESEKLVQ--EALDRAMkGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-264 |
1.77e-20 |
|
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: 93.25 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIELSEQSAaqmrhvrgadMAMIFQEpm 114
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRR----------IGYVFQE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 TSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDqvripeAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
Cdd:TIGR02142 84 ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLG------IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPY 264
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-256 |
1.86e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIElseqsaaqmRHVrgadmAMIFQE 112
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH---------RQV-----ALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 PMtslnpVF--TVGEQIAESIRlhqNASREEAMVEAKRMLDQVRIPEAQ----TILSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:TIGR00958 564 PV-----LFsgSVRENIAYGLT---DTPDEEIMAAAKAANAHDFIMEFPngydTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 187 PAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGTVEQI 256
Cdd:TIGR00958 636 PRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
309-546 |
1.97e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 89.78 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 309 DGEpvLRVRNLVTRFplrSGLLNRVTREVhavekvSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
Cdd:cd03369 4 HGE--IEVENLSVRY---APDLPPVLKNV------SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 389 DTLspgKLQALRRDIQFIFQDPY-------ASLDPRQTIGD-SIIEPLRVhgllpgKEAvarvawllervGLlpehawry 460
Cdd:cd03369 73 STI---PLEDLRSSLTIIPQDPTlfsgtirSNLDPFDEYSDeEIYGALRV------SEG-----------GL-------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 461 phEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLG 540
Cdd:cd03369 125 --NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTI--LTIAHRLRTIIDYD-KILVMDAG 199
|
....*.
gi 1134749654 541 QIVEIG 546
Cdd:cd03369 200 EVKEYD 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
277-555 |
2.22e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 277 AMKGLDYPRRFPliSLEHPAKQAPPieqktVVDGepVLRVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLV 356
Cdd:TIGR00958 451 SEKVFEYLDRKP--NIPLTGTLAPL-----NLEG--LIEFQDVSFSYPNRP--------DVPVLKGLTFTLHPGEVVALV 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 357 GESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPyasLDPRQTIGDSIIEPLRVHgllPG 436
Cdd:TIGR00958 514 GPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH---HYLHRQVALVGQEP---VLFSGSVRENIAYGLTDT---PD 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 437 KE--AVARVAWLLERVGLLP--------EHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLL 506
Cdd:TIGR00958 585 EEimAAAKAANAHDFIMEFPngydtevgEKG----SQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLL 656
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1134749654 507 LDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:TIGR00958 657 QESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
36-246 |
2.32e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 89.92 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 36 SFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrdvielseqSAAQMRHVrgadmAMIFQEpmT 115
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----------LAPYQRPV-----SMLFQE--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 116 SLNPVFTVGEQIAESIR--LHQNASREEAMVEAKRmldQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
Cdd:TIGR01277 80 NLFAHLTVRQNIGLGLHpgLKLNAEQQEKVVDAAQ---QVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:TIGR01277 154 EPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
312-536 |
2.52e-20 |
|
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: 94.66 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPLRSgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTL 391
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR----------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKLQALRRDIQFIFQDPYasldprqTIGDSIIEPLRvHGLLPGKEA----VARVAWLLERVGLLPEH----AWRYPHE 463
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPF-------LFAGTIAENIR-LARPDASDAeireALERAGLDEFVAALPQGldtpIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAV 536
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
344-547 |
2.58e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.03 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 344 SFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQDP--YASLDPR 417
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKST----LLNLIagflTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENnlFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGdsiieplrvHGLLPG-------KEAVARVAwllERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:PRK10771 90 QNIG---------LGLNPGlklnaaqREKLHAIA---RQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-266 |
3.52e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 14 AVENLNIAFMQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmllrrRSRDVIELSEQ 93
Cdd:PRK14258 7 AIKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEV----------RVEGRVEFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 SAAQMR----HVRgADMAMIFQEPmtSLNPVfTVGEQIAESIRL---HQNASRE---EAMVEAKRMLDQVRIPEAQTILs 163
Cdd:PRK14258 75 NIYERRvnlnRLR-RQVSMVHPKP--NLFPM-SVYDNVAYGVKIvgwRPKLEIDdivESALKDADLWDEIKHKIHKSAL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 ryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY 243
Cdd:PRK14258 150 ----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
250 260
....*....|....*....|....*...
gi 1134749654 244 QGEA-----VETGTVEQIFHAPQHPYTR 266
Cdd:PRK14258 226 GNENrigqlVEFGLTKKIFNSPHDSRTR 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-278 |
3.71e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.46 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSE 92
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG-------DKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAqmRHVrgadmAMIFQEPMTSLNpvFTVGEQIAESIRLHQN-----ASREEAMVEakRMLDQVRIPE-AQTILSryp 166
Cdd:PRK11231 72 RQLA--RRL-----ALLPQHHLTPEG--ITVRELVAYGRSPWLSlwgrlSAEDNARVN--QAMEQTRINHlADRRLT--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 167 hQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:PRK11231 138 -DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
250 260 270
....*....|....*....|....*....|..
gi 1134749654 247 AVETGTVEQIFhapqhpyTRALLAAVPQLGAM 278
Cdd:PRK11231 216 VMAQGTPEEVM-------TPGLLRTVFDVEAE 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-242 |
3.86e-20 |
|
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: 94.28 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 2 PHSDELDAG----NVLAVENLNIAFmqdQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK 77
Cdd:TIGR02857 307 PLAGKAPVTaapaSSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 78 mllrrrsrdvIELSEQSAAQMRhvrgADMAMIFQEPmtslnpvFTVGEQIAESIRLHQNASREEAMVEAKRM-----LDQ 152
Cdd:TIGR02857 384 ----------VPLADADADSWR----DQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREALERagldeFVA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 153 VRIPEAQTILSRYPHQLSGGMRQRVMIAMALsCRPA-VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGV 231
Cdd:TIGR02857 443 ALPQGLDTPIGEGGAGLSGGQAQRLALARAF-LRDApLLLLDEPTAHLDAETEAEVLEALRALAQGRT--VLLVTHRLAL 519
|
250
....*....|.
gi 1134749654 232 VAEiADRVLVM 242
Cdd:TIGR02857 520 AAL-ADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
314-542 |
4.32e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 88.04 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSGLLnrvtrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:cd03246 1 LEVENVSFRYPGAEPPV---------LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GklqALRRDIQFIFQDPyasldprQTIGDSIIEPLrvhgllpgkeavarvawllervgllpehawrypheFSGGQRQRIC 473
Cdd:cd03246 72 N---ELGDHVGYLPQDD-------ELFSGSIAENI-----------------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERIShRVAVMYLGQI 542
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
336-547 |
4.78e-20 |
|
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: 94.63 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQA----LRRDIqFIFQ--- 408
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANsvamVDQDI-FLFEgtv 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 409 -DPYASLDPrqTIGDSIIEplrvhgllpgkeAVARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALAL 480
Cdd:TIGR03796 570 rDNLTLWDP--TIPDADLV------------RACKDAAIHDVITSRPG---GYDAElaegganLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 481 NPKVIIADEAVSALDVSIRGQII-NLlldlqRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGP 547
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDdNL-----RRRGCTCIIVAHRLSTI-RDCDEIIVLERGKVVQRGT 694
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-246 |
5.25e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 89.31 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 22 FMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqaGGLVQCDKMLLRRRSRDVIELSEQSAAQMRHV 101
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT----LKIL---SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 102 RGADMAMIFQEPmtslnpvftvgeqIAESIRLHQNASREEAmVEAKRMLDQ-VRIPEAQTILSRYPHQLSGGMRQRVMIA 180
Cdd:cd03267 100 FGQKTQLWWDLP-------------VIDSFYLLAAIYDLPP-ARFKKRLDElSELLDLEELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-575 |
6.50e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYasL 414
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRYH--L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSIIEPlRVHGLLPGKEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK10535 98 LSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 495 DVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRavfenPQHPYTRKLLAAVPVAEPSR 574
Cdd:PRK10535 176 DSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ-----EKVNVAGGTEPVVNTASGWR 248
|
.
gi 1134749654 575 Q 575
Cdd:PRK10535 249 Q 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-256 |
7.46e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAfmqDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRDVIELS 91
Cdd:COG3845 257 VLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQS----ELAEAL--AG---------LRPPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQM--RHVRGADMAMIFQEPM-TSLNPVFTVGEQIAesIRLHQNA--------SREEAMVEAKRMLDQ--VRIPEA 158
Cdd:COG3845 319 GEDITGLspRERRRLGVAYIPEDRLgRGLVPDMSVAENLI--LGRYRRPpfsrggflDRKAIRAFAEELIEEfdVRTPGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 159 QTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkVLQKEMSMGVIFITHDMGVVAEIADR 238
Cdd:COG3845 397 DTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-LELRDAGAAVLLISEDLDEILALSDR 471
|
250 260
....*....|....*....|...
gi 1134749654 239 VLVMYQGE-----AVETGTVEQI 256
Cdd:COG3845 472 IAVMYEGRivgevPAAEATREEI 494
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-257 |
8.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 8.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDvielseqsaAQMRHVRgADMAMI 109
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKN---------KDIKQIR-KKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMTSLnpvF--TVGEQIAESirlHQN--ASREEAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:PRK13649 91 FQFPESQL---FeeTVLKDVAFG---PQNfgVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIF 257
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-259 |
8.50e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 2 PHSDELDAGNVLAVENLNIAfmqdqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
Cdd:COG1129 246 PKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 82 RRS-RDVIE-----LSEQsaaqmRHVRGadmamifqepmtsLNPVFTVGEQIA----ESIRLHQNASREEAMVEAKRMLD 151
Cdd:COG1129 318 IRSpRDAIRagiayVPED-----RKGEG-------------LVLDLSIRENITlaslDRLSRGGLLDRRRERALAEEYIK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 152 QVRI--PEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDM 229
Cdd:COG1129 380 RLRIktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSEL 454
|
250 260 270
....*....|....*....|....*....|....*
gi 1134749654 230 GVVAEIADRVLVMYQGEAV-----ETGTVEQIFHA 259
Cdd:COG1129 455 PELLGLSDRILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
312-578 |
8.54e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRfplRSGllnrvtREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:PRK13548 1 AMLEARNLSVR---LGG------RTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPGKLqALRRdiqfifqdpyASLdPRQTigdSIIEPLRVH-----GLLPGKEAVARVAWL----LERVGLLpEHAWRYPH 462
Cdd:PRK13548 70 SPAEL-ARRR----------AVL-PQHS---SLSFPFTVEevvamGRAPHGLSRAEDDALvaaaLAQVDLA-HLAGRDYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 463 EFSGGQRQRICIARALA------LNPKVIIADEAVSALDvsIRGQIInlLLDLQRDF----GIAYLFISHDMAVVERISH 532
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD--LAHQHH--VLRLARQLaherGLAVIVVLHDLNLAARYAD 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 533 RVAVMYLGQIVEIGPRRAVFenpqhpyTRKLLAAV---PV---AEPSRQRPQ 578
Cdd:PRK13548 210 RIVLLHQGRLVADGTPAEVL-------TPETLRRVygaDVlvqPHPETGAPL 254
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-251 |
1.48e-19 |
|
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: 87.25 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGeTLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVIElseqsaaQMRHVRGAdMAMIF 110
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRIL---ATLTPPSSGTIRIDGQDVLK-------QPQKLRRR-IGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSlnPVFTVGEQIAESIRLHQ-NASREEAMVEakRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03264 79 QEFGVY--PNFTVREFLDYIAWLKGiPSKEVKARVD--EVLELVNLGDR---AKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDRI--VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-550 |
1.52e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVE------SQGGEIIFN 384
Cdd:PRK13549 3 EYLLEMKNITKTFG-----------GVKALDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSgvyphgTYEGEIIFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 385 GQridtlspgKLQAL------RRDIQFIFQDpyASLDPRQTIGDSII---EPLRvHGLLPGKEAVARVAWLLERVGLLPE 455
Cdd:PRK13549 68 GE--------ELQASnirdteRAGIAIIHQE--LALVKELSVLENIFlgnEITP-GGIMDYDAMYLRAQKLLAQLKLDIN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 456 HAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVA 535
Cdd:PRK13549 137 PATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTIC 214
|
250
....*....|....*
gi 1134749654 536 VMYLGQivEIGPRRA 550
Cdd:PRK13549 215 VIRDGR--HIGTRPA 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
295-523 |
1.58e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 92.42 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 295 PAKQAPpiEQKTVVDGEPVLRVRNLVTRFPLRSGLLNRVtrevhavekvSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
Cdd:TIGR02868 318 AEGSAP--AAGAVGLGKPTLELRDLSAGYPGAPPVLDGV----------SLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 375 ESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYasldprqTIGDSIIEPLRVhgllpGKEAV--ARVAWLLERVGL 452
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQD---EVRRRVSVCAQDAH-------LFDTTVRENLRL-----ARPDAtdEELWAALERVGL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 453 LpEHAWRYPH-----------EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFIS 521
Cdd:TIGR02868 451 A-DWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLIT 527
|
..
gi 1134749654 522 HD 523
Cdd:TIGR02868 528 HH 529
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
339-561 |
1.75e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR---LVES--QGGEIIFNGQ-----RIDTLspgklqALRRDIQFIFQ 408
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKnlyapDVDPV------EVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 409 DPYASldPRqTIGDSIIEPLRVHGLLPG-KEAVAR-----VAW-----LLERVGLlpehawryphEFSGGQRQRICIARA 477
Cdd:PRK14243 99 KPNPF--PK-SIYDNIAYGARINGYKGDmDELVERslrqaALWdevkdKLKQSGL----------SLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVM---------YLGQIVEIGPR 548
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRT 243
|
250
....*....|...
gi 1134749654 549 RAVFENPQHPYTR 561
Cdd:PRK14243 244 EKIFNSPQQQATR 256
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
343-495 |
2.46e-19 |
|
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: 91.81 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyasldprqTI-- 420
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRAAIGIVPQD---------TVlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIIEPLRVhgllpGK--------EAVARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVI 485
Cdd:COG5265 445 NDTIAYNIAY-----GRpdaseeevEAAARAAQIHDFIESLPD---GYDTRvgerglkLSGGEKQRVAIARTLLKNPPIL 516
|
170
....*....|
gi 1134749654 486 IADEAVSALD 495
Cdd:COG5265 517 IFDEATSALD 526
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-258 |
2.51e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.64 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRrrSRDVIELSEQSAAQMRHVRgADMAMIF 110
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKST-------LLQHLNGLLQPTEGKVT--VGDIVVSSTSKQKEIKPVR-KKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMTSLnpvftVGEQIAESIRLH-QN--ASREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:PRK13643 91 QFPESQL-----FEETVLKDVAFGpQNfgIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFH 258
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-256 |
2.57e-19 |
|
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: 91.70 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 5 DELDAGNVLA------VENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdKM 78
Cdd:TIGR02203 315 PEKDTGTRAIerargdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG-----QI 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 79 LLrrrsrDVIELSEQSAAQMRhvrgADMAMIFQEPMtslnpVF--TVGEQIAESIRLHQNASREEAMVEAKRMLDQV-RI 155
Cdd:TIGR02203 390 LL-----DGHDLADYTLASLR----RQVALVSQDVV-----LFndTIANNIAYGRTEQADRAEIERALAAAYAQDFVdKL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 156 PEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaE 234
Cdd:TIGR02203 456 PLGlDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT--TLVIAHRLSTI-E 532
|
250 260
....*....|....*....|..
gi 1134749654 235 IADRVLVMYQGEAVETGTVEQI 256
Cdd:TIGR02203 533 KADRIVVMDDGRIVERGTHNEL 554
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
36-245 |
3.17e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 36 SFSLQRGETLAIVGESGSGKSvTALALMrlleqaGGLVQCDKMLLRRRSRDvieLSEQSAAQmRHVrgadmAMIFQEpmT 115
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLI------AGFLTPASGSLTLNGQD---HTTTPPSR-RPV-----SMLFQE--N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 116 SLNPVFTVGEQIAESIR--LHQNASREEAMveaKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
Cdd:PRK10771 81 NLFSHLTVAQNIGLGLNpgLKLNAAQREKL---HAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
343-546 |
4.55e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 91.34 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYasldprqTIGD 422
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA---WLRRQMGVVLQENV-------LFSR 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SIIEPLRVHGllPGKE-----AVARVAWLLERVGLLPEHawrYPHE-------FSGGQRQRICIARALALNPKVIIADEA 490
Cdd:TIGR01846 546 SIRDNIALCN--PGAPfehviHAAKLAGAHDFISELPQG---YNTEvgekganLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAHRLSTV-RACDRIIVLEKGQIAESG 673
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-245 |
4.78e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.45 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 2 PHSDELDAGNVLAVENLNIAfmqdqqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQA----GGLVQCD- 76
Cdd:PRK10762 247 PRLDKAPGEVRLKVDNLSGP---------GVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGAlprtSGYVTLDg 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 77 KMLLRRRSRD-----VIELSEQsaaqmRHVRGADMAMIFQEPM--TSLNPVFTVGEQIaesirlhqNASREEAMVEAKRM 149
Cdd:PRK10762 314 HEVVTRSPQDglangIVYISED-----RKRDGLVLGMSVKENMslTALRYFSRAGGSL--------KHADEQQAVSDFIR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 150 LDQVRIPEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDM 229
Cdd:PRK10762 381 LFNIKTPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEM 455
|
250
....*....|....*.
gi 1134749654 230 GVVAEIADRVLVMYQG 245
Cdd:PRK10762 456 PEVLGMSDRILVMHEG 471
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
31-260 |
6.54e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdKMLLRRrsrdvIELSEQSAAQ-MRHVRGadmaMI 109
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKG-----KVLVSG-----IDTGDFSKLQgIRKLVG----IV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMTSLnpvftVGEQIAESIrlhqnASREEAM----VEAKRMLDQVRipeAQTILSRY----PHQLSGGMRQRVMIAM 181
Cdd:PRK13644 83 FQNPETQF-----VGRTVEEDL-----AFGPENLclppIEIRKRVDRAL---AEIGLEKYrhrsPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-259 |
7.03e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCDKMLLRRRSRdvielseqsaaqmrhvrgadMAMIF 110
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLI---AGILEPTSGRVEVNGR--------------------VSALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 qEPMTSLNPVFTVgeqiAESIRLhqNA-----SREEAmveaKRMLDQVripEAQTILSRYPHQ----LSGGMRQRVMIAM 181
Cdd:COG1134 94 -ELGAGFHPELTG----RENIYL--NGrllglSRKEI----DEKFDEI---VEFAELGDFIDQpvktYSSGMRARLAFAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHA 259
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
314-555 |
7.42e-19 |
|
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: 86.06 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSP 393
Cdd:cd03218 1 LRAENLSKRYG---------KRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 GKLQAlRRDIQFIFQDpyASLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlpEH-AWRYPHEFSGGQRQRI 472
Cdd:cd03218 69 MHKRA-RLGIGYLPQE--ASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI--THlRKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
...
gi 1134749654 553 ENP 555
Cdd:cd03218 222 ANE 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-257 |
9.99e-19 |
|
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: 89.81 E-value: 9.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIelse 92
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsaaqMRHV----------RGadmamifqepmtslnpvfTVGEQIAesiRLhqNASREEAMVEAKRMLDQ----VRIPEA 158
Cdd:COG4618 405 -----GRHIgylpqdvelfDG------------------TIAENIA---RF--GDADPEKVVAAAKLAGVhemiLRLPDG 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 159 -QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAeIAD 237
Cdd:COG4618 457 yDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLA-AVD 534
|
250 260
....*....|....*....|
gi 1134749654 238 RVLVMYQGEAVETGTVEQIF 257
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVL 554
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
338-548 |
1.39e-18 |
|
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: 85.27 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgkLQALRRDIQFIFQdpyasldpr 417
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP--HERARAGIAYVPQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 qtiGDSIIEPLRVH-GLLPGKEAVARV-----AWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:TIGR03410 83 ---GREIFPRLTVEeNLLTGLAALPRRsrkipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAG 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-247 |
1.51e-18 |
|
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: 83.42 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDviELSEQSAAQM 98
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN--ELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHVrgadmaMIFqepmtslnpvftvGEQIAESIrlhqnasreeamveakrmldqvripeaqtilsryphqLSGGMRQRVM 178
Cdd:cd03246 83 QDD------ELF-------------SGSIAENI-------------------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGEA 247
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
316-547 |
1.62e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.06 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 316 VRNLVTRFPLRS----------GLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
Cdd:COG4586 4 VENLSKTYRVYEkepglkgalkGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 386 qridtLSPGKLQ-ALRRDIQFIF-QdpyasldpR-QTIGD-SIIEPLRVHGL---LPGKEAVARVAWLLERVGLlpEHAW 458
Cdd:COG4586 84 -----YVPFKRRkEFARRIGVVFgQ--------RsQLWWDlPAIDSFRLLKAiyrIPDAEYKKRLDELVELLDL--GELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 459 RYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
Cdd:COG4586 149 DTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
250
....*....|
gi 1134749654 538 YLGQIVEIGP 547
Cdd:COG4586 229 DHGRIIYDGS 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-254 |
1.90e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALmrlleqagglvqcDKMLLRRRSRDVIEL 90
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-------------NGIYLPQRGRVKVMG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAQMRHVRGAdMAMIFQEPMtslNPVF--TVGEQIAESIRlHQNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ 168
Cdd:PRK13647 67 REVNAENEKWVRSK-VGLVFQDPD---DQVFssTVWDDVAFGPV-NMGLDKDEVERRVEEALKAVRM---WDFRDKPPYH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAV 248
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVL 217
|
....*.
gi 1134749654 249 ETGTVE 254
Cdd:PRK13647 218 AEGDKS 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-257 |
2.17e-18 |
|
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: 85.14 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQC---DKMLL-RRRSR-D 86
Cdd:COG1119 3 LLELRNVTVRR--GGKTI--LDDISWTVKPGEHWAILGPNGAGKS----TLLSLI--TGDLPPTygnDVRLFgERRGGeD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 87 VIELseqsAAQMRHVrGADMAMIFQEPMTSLNPV---FTvgeqiaESIRLHQNASREEAMvEAKRMLDQVRIpeaQTILS 163
Cdd:COG1119 73 VWEL----RKRIGLV-SPALQLRFPRDETVLDVVlsgFF------DSIGLYREPTDEQRE-RARELLELLGL---AHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmgvVAEIAD---RVL 240
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPgitHVL 214
|
250
....*....|....*..
gi 1134749654 241 VMYQGEAVETGTVEQIF 257
Cdd:COG1119 215 LLKDGRVVAAGPKEEVL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
311-543 |
3.22e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
Cdd:PRK09700 3 TPYISMAGIGKSFG-----------PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPgKLQAlRRDIQFIFQDPyasldprqtigdSIIEPLRVH-----GLLPGK-----------EAVARVAWLLERVGLLp 454
Cdd:PRK09700 72 LDH-KLAA-QLGIGIIYQEL------------SVIDELTVLenlyiGRHLTKkvcgvniidwrEMRVRAAMMLLRVGLK- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 455 ehawRYPHEFSG----GQRQRICIARALALNPKVIIADEAVSAL---DVSIRGQIINLLldlqRDFGIAYLFISHDMAVV 527
Cdd:PRK09700 137 ----VDLDEKVAnlsiSHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQL----RKEGTAIVYISHKLAEI 208
|
250
....*....|....*.
gi 1134749654 528 ERISHRVAVMYLGQIV 543
Cdd:PRK09700 209 RRICDRYTVMKDGSSV 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-245 |
3.47e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.77 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 16 ENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDKMLLRRRSRDVIELSEQ 93
Cdd:PRK10908 5 EHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERpsAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 saaqmrhvrgadMAMIFQEPMTSLNPvfTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGM 173
Cdd:PRK10908 81 ------------IGMIFQDHHLLMDR--TVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLDKA---KNFPIQLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-242 |
3.96e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.30 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAfmqdQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGL---VQCD-KMLLRRRSRDVI 88
Cdd:COG4136 2 LSLENLTIT----LGGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAI-----AGTLspaFSASgEVLLNGRRLTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 elseqsAAQMRHVrgadmAMIFQEPMtsLNPVFTVGEQIAESIRLHQNASREEAMVEAkrMLDQVripEAQTILSRYPHQ 168
Cdd:COG4136 72 ------PAEQRRI-----GILFQDDL--LFPHLSVGENLAFALPPTIGRAQRRARVEQ--ALEEA---GLAGFADRDPAT 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVM 242
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDL 206
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-252 |
4.12e-18 |
|
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: 83.31 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRHvrgaDMAMIF 110
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG----------VDISKIGLHDLRS----RISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEPMtslnpVFTvGeqiaeSIR-----LHQnaSREEAMVEAkrmLDQVRIPEA--------QTILSRYPHQLSGGMRQRV 177
Cdd:cd03244 85 QDPV-----LFS-G-----TIRsnldpFGE--YSDEELWQA---LERVGLKEFveslpgglDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 178 MIAMALSCRPAVLIADEPTTALDVtIQAQILQliKVLQKEMS-MGVIFITHDMGVVAEiADRVLVMYQGEAVETGT 252
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDP-ETDALIQ--KTIREAFKdCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-251 |
4.49e-18 |
|
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: 83.41 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLrrrsrDVIELSEQSAAQM 98
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-----LL-----DGTDIRQLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHvrgaDMAMIFQEPMtslnpVF--TVGEQIAESIRLHQNAsreeamveakRMLDQVRIPEAQTILSRYPH--------- 167
Cdd:cd03245 77 RR----NIGYVPQDVT-----LFygTLRDNITLGAPLADDE----------RILRAAELAGVTDFVNKHPNgldlqiger 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 --QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVaEIADRVLVMYQG 245
Cdd:cd03245 138 grGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSG 214
|
....*.
gi 1134749654 246 EAVETG 251
Cdd:cd03245 215 RIVADG 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-256 |
5.36e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.52 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDKMLLRRRSRdvielseqsaaqmRHVRgaDMA 107
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgILVPTSGEVRVLGYVPFKRRK-------------EFAR--RIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIF-QEpmTSLN---PVftvgeqiAESIRLHQN---------ASREEAMVEakrMLD-------QVRipeaqtilsryph 167
Cdd:COG4586 99 VVFgQR--SQLWwdlPA-------IDSFRLLKAiyripdaeyKKRLDELVE---LLDlgelldtPVR------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
....*....
gi 1134749654 248 VETGTVEQI 256
Cdd:COG4586 234 IYDGSLEEL 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
330-546 |
5.99e-18 |
|
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: 82.99 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 LNRVTREVHAvEKVSFDLW--PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklqaLRRDIQFIF 407
Cdd:TIGR01277 3 LDKVRYEYEH-LPMEFDLNvaDGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP-----YQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 408 QDP--YASLDPRQTIGDSIIEPLRVHGLlpGKEAVARVAwllERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:TIGR01277 77 QENnlFAHLTVRQNIGLGLHPGLKLNAE--QQEKVVDAA---QQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
334-555 |
6.92e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.08 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYAS 413
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 LDPRQTIGDSIIEPLRVhGLlpGKEAVA-RVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:PRK13652 91 IFSPTVEQDIAFGPINL-GL--DEETVAhRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-251 |
6.94e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.97 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqaGGLVQCDkmllrrrSRDVIelseqsaaqmrhVRGADM 106
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLL---AGIYPPD-------SGTVT------------VRGRVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 107 AMIfqEPMTSLNPVFTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIPEAQTI-LSRYphqlSGGMRQRVMIAMALSC 185
Cdd:cd03220 87 SLL--GLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELGDFIDLpVKTY----SSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-522 |
1.11e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 86.22 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNL---SFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmlLRRRSRDVIELSEQSA 95
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLqlpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---FSHITRLSFEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 96 AQMRHVRGADMAMIFQEpmtslnpvfTVGEQIAESIrlhQNASREEAMVEakRMLDQVRIpeaQTILSRYPHQLSGGMRQ 175
Cdd:PRK10938 80 SDEWQRNNTDMLSPGED---------DTGRTTAEII---QDEVKDPARCE--QLAQQFGI---TALLDRRFKYLSTGETR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQ 255
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 256 IFhapqhpyTRALLAavpQLGamkgldYPRRFPLISLehPAKQAPPIeQKTVVDGEPVLRVRNLVTRFPLRSgLLNRVTR 335
Cdd:PRK10938 222 IL-------QQALVA---QLA------HSEQLEGVQL--PEPDEPSA-RHALPANEPRIVLNNGVVSYNDRP-ILHNLSW 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHavekvsfdlwPGETLSLVGESGSGKSTtgraLLRLV---ESQGGE---IIFNGQRidtLSPGKLQALRRDIQF---- 405
Cdd:PRK10938 282 QVN----------PGEHWQIVGPNGAGKST----LLSLItgdHPQGYSndlTLFGRRR---GSGETIWDIKKHIGYvsss 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 406 IFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKEAVARVAWlLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:PRK10938 345 LHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQW-LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 1134749654 486 IADEAVSALDVSIRgQIINLLLD-LQRDFGIAYLFISH 522
Cdd:PRK10938 424 ILDEPLQGLDPLNR-QLVRRFVDvLISEGETQLLFVSH 460
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-256 |
1.47e-17 |
|
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: 86.25 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDV---- 87
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkh 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 -------IELSEQsaaqmrhvrgadmamifqepmtslnpvfTVGEQIAesiRLHQNASrEEAMVEAKRMLDQ----VRIP 156
Cdd:TIGR01842 394 igylpqdVELFPG----------------------------TVAENIA---RFGENAD-PEKIIEAAKLAGVheliLRLP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 157 EA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVaEI 235
Cdd:TIGR01842 442 DGyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GC 519
|
250 260
....*....|....*....|.
gi 1134749654 236 ADRVLVMYQGEAVETGTVEQI 256
Cdd:TIGR01842 520 VDKILVLQDGRIARFGERDEV 540
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-248 |
1.48e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVIELSE 92
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNIL---GCLDKPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHvrgADMAMIFQEpmTSLNPVFTvGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGG 172
Cdd:PRK10535 78 DALAQLRR---EHFGFIFQR--YHLLSHLT-AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDR---VEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-546 |
1.55e-17 |
|
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: 80.82 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklQALRRDIQFIFQDPYasld 415
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE----KALSSLISVLNQRPY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 prqtigdsiieplrvhgLLPGKeavarvawLLERVGLlpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:cd03247 86 -----------------LFDTT--------LRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 496 VSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
Cdd:cd03247 131 PITERQLLSLIFEVLKDKTL--IWITHHLTGIEHMD-KILFLENGKIIMQG 178
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-543 |
1.75e-17 |
|
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: 82.00 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 328 GLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtLSPGKLQ-ALRRDIQFI 406
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRkKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 407 FQDPyasldpRQTIGD-SIIEPLRVH----GLLPG--KEAVARVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALA 479
Cdd:cd03267 100 FGQK------TQLWWDlPVIDSFYLLaaiyDLPPArfKKRLDELSELLDLEELLDTPV----RQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-229 |
1.76e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQcdkmllrrRSRDVIELSEQSAAQmrhvRGADMAMIF 110
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTT-------LLNLIAGFVP--------YQHGSITLDGKPVEG----PGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLhQNASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PRK11248 77 QN--EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM 229
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
314-546 |
1.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSGLlnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI--IFNGQRIDTL 391
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT------ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPG-------------------KLQALRRDIQFIFQdpYASLDP-RQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVG 451
Cdd:PRK13651 77 TKEkekvleklviqktrfkkikKIKEIRRRVGVVFQ--FAEYQLfEQTIEKDIIFGPVSMGV-SKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 452 LLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERIS 531
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWT 232
|
250
....*....|....*
gi 1134749654 532 HRVAVMYLGQIVEIG 546
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-260 |
1.88e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.12 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRL---LEQ-AGGLVQCDkmllRRRSRDViELSEQsaaqmrhvrg 103
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMvagLERiTSGEIWIG----GRVVNEL-EPADR---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 aDMAMIFQEpmTSLNPVFTVGEQIAESIRLhQNASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMAL 183
Cdd:PRK11650 77 -DIAMVFQN--YALYPHMSVRENMAYGLKI-RGMPKAEI---EERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-252 |
2.56e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.46 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLrrrsrDVIELSEQS 94
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD-----IDEGEILL-----DGHDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 AAQMRHvrgadmamifQEPMTSLNpVFTVGEQIAESIRLHQNA--SREEaMVEAKRM-------------LDQVrIPEAQ 159
Cdd:PRK11176 412 LASLRN----------QVALVSQN-VHLFNDTIANNIAYARTEqySREQ-IEEAARMayamdfinkmdngLDTV-IGENG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 160 TILSryphqlsGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRV 239
Cdd:PRK11176 479 VLLS-------GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRT--SLVIAHRLSTI-EKADEI 548
|
250
....*....|...
gi 1134749654 240 LVMYQGEAVETGT 252
Cdd:PRK11176 549 LVVEDGEIVERGT 561
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-257 |
2.82e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIELS 91
Cdd:PRK13638 1 MLATSDLWFRY-QDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQsaaqmrhvrgadMAMIFQEPMTSLnpVFT-VGEQIAESIRlhqNASREEAMVeAKRMLDQVRIPEAQtilsRYPHQ-- 168
Cdd:PRK13638 77 QQ------------VATVFQDPEQQI--FYTdIDSDIAFSLR---NLGVPEAEI-TRRVDEALTLVDAQ----HFRHQpi 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 --LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:PRK13638 135 qcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQ 213
|
250
....*....|.
gi 1134749654 247 AVETGTVEQIF 257
Cdd:PRK13638 214 ILTHGAPGEVF 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
336-556 |
2.87e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.93 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLD 415
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQS-YA-LY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGDSIIEPLRVHGLLPG--KEAVARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEeiNQRVNQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
350-549 |
2.97e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtLSPGKLQALRRDIQFIFQDpyASLDPRQTIGDSIieplr 429
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAREDTRLMFQD--ARLLPWKKVIDNV----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 430 vhGL-LPGK-EAVARVAwlLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
Cdd:PRK11247 103 --GLgLKGQwRDAALQA--LAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1134749654 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI-----VEIG-PRR 549
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDLPrPRR 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-260 |
3.07e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRDVIELSE 92
Cdd:PRK11300 6 LSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-------LLRGQHIEGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMRHVRGADMAMIFQEpmtslnpvFTVGEQIAESIRLHQNA--------------SREEAMVEAKRMLDQVRIPEa 158
Cdd:PRK11300 75 HQIARMGVVRTFQHVRLFRE--------MTVIENLLVAQHQQLKTglfsgllktpafrrAESEALDRAATWLERVGLLE- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 159 qtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
Cdd:PRK11300 146 --HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDR 223
|
250 260
....*....|....*....|..
gi 1134749654 239 VLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK11300 224 IYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-252 |
5.65e-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: 79.76 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVielse 92
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID-------GIDI----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qSAAQMRHVRGAdMAMIFQEPMTslnpvftvgeqIAESIRLhqNASREEamveakrMLDQVRIPEAQTIlSRYPHQLSGG 172
Cdd:cd03369 73 -STIPLEDLRSS-LTIIPQDPTL-----------FSGTIRS--NLDPFD-------EYSDEEIYGALRV-SEGGLNLSQG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMSMGVIF-ITHDMGVVAEIaDRVLVMYQGEAVETG 251
Cdd:cd03369 130 QRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ---KTIREEFTNSTILtIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
.
gi 1134749654 252 T 252
Cdd:cd03369 206 H 206
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
35-272 |
6.05e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVqcdkmLLRRRSrdvieLSEQSAAQMRHVRgadmAMIFQEPM 114
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMAGLLPGQGEI-----LLNGRP-----LSDWSAAELARHR----AYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 TSLN-PVFtvgeqiaESIRLHQNASREEAMVEA--KRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMAL-----SCR 186
Cdd:COG4138 80 PPFAmPVF-------QYLALHQPAGASSEAVEQllAQLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 187 P--AVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFhapqhpy 264
Cdd:COG4138 150 PegQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM------- 221
|
....*...
gi 1134749654 265 TRALLAAV 272
Cdd:COG4138 222 TPENLSEV 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
314-553 |
6.21e-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: 84.41 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
Cdd:COG4618 331 LSVENLTVVPP---------GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gklQALRRDIQFIFQDPyaSLDPrQTIGDSI-----IEPLRVHgllpgkeAVARVAWLLERVGLLPEhawRY-------P 461
Cdd:COG4618 402 ---EELGRHIGYLPQDV--ELFD-GTIAENIarfgdADPEKVV-------AAAKLAGVHEMILRLPD---GYdtrigegG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVeRISHRVAVMYLGQ 541
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDGR 543
|
250
....*....|..
gi 1134749654 542 IVEIGPRRAVFE 553
Cdd:COG4618 544 VQAFGPRDEVLA 555
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-522 |
8.49e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.35 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqridtlsPGklqalRRDIQFIFQDPYAsldPRQT 419
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PE-----GEDLLFLPQRPYL---PLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIEPlrvhgllpgkeavarvawllervgllpehaWRypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:cd03223 80 LREQLIYP------------------------------WD--DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 1134749654 500 GQIINLLldlqRDFGIAYLFISH 522
Cdd:cd03223 128 DRLYQLL----KELGITVISVGH 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
168-542 |
9.66e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.41 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEM-SMGVIFITHDMGVvAEIADRVLVMYQGE 246
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEE-AERFDWLVAMDAGR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 247 AVETGTveqifhapqhpyTRALLAavpQLGAmKGLDypRRFplISLEHPAKQA-------PPIEQKTvvDGEPVLRVRNL 319
Cdd:NF033858 215 VLATGT------------PAELLA---RTGA-DTLE--AAF--IALLPEEKRRghqpvviPPRPADD--DDEPAIEARGL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 320 VTRFplrsGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLqAL 399
Cdd:NF033858 273 TMRF----G-------DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDI-AT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 400 RRDIQFIFQ--DPYASLDPRQTigdsiiepLRVHGLL---PGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICI 474
Cdd:NF033858 338 RRRVGYMSQafSLYGELTVRQN--------LELHARLfhlPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSL 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 475 ARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAyLFIS-HDMAVVERIShRVAVMYLGQI 542
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIStHFMNEAERCD-RISLMHAGRV 475
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-246 |
1.08e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.44 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrdvielseqSAAQMRHVRgADMAMIFQ 111
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-------------SQYEHKYLH-SKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EPMTSLNpvfTVGEQIAESIrlhQNASREEAMVEAKRMLDQVRIPEAQ----TILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:cd03248 96 EPVLFAR---SLQDNIAYGL---QSCSFECVKEAAQKAHAHSFISELAsgydTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVaEIADRVLVMYQGE 246
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
339-552 |
1.19e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgklQALRRD-IQFIFQDPYASLDPR 417
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-------QALQKNlVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVH-GLL--PGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK15056 95 VLVEDVVMMGRYGHmGWLrrAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 495 DVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVF 552
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-553 |
1.26e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQdpYASLDPRQT 419
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQRVGVVPQ--FDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IgdsiIEPLRVHGL---LPGKEAVARVAWLLErVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:PRK13537 97 V----RENLLVFGRyfgLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
Cdd:PRK13537 172 QARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-553 |
1.27e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDPYASLDPR 417
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHglLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:PRK13643 101 TVLKDVAFGPQNFG--IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 498 IRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
Cdd:PRK13643 179 ARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-267 |
1.58e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrdvIELS 91
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKN---LYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHVRGadmaMIFQEPmtslNPvF--TVGEQIAESIRLHQNASREEAMVEakRMLDQVRI-PEAQTILSRYPHQ 168
Cdd:PRK14243 83 DVDPVEVRRRIG----MVFQKP----NP-FpkSIYDNIAYGARINGYKGDMDELVE--RSLRQAALwDEVKDKLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVM------ 242
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT--IIIVTHNMQQAARVSDMTAFFnvelte 229
|
250 260
....*....|....*....|....*...
gi 1134749654 243 ---YQGEAVETGTVEQIFHAPQHPYTRA 267
Cdd:PRK14243 230 gggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
27-251 |
1.68e-16 |
|
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: 78.41 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrdvielseQSAAQMRHVRGADM 106
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD----------------GKSYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 107 AMIFQEPmtSLNPVFTVGEQIAESIRLHQNASREeamveAKRMLDQVRipeaqtiLSRYPH----QLSGGMRQRVMIAMA 182
Cdd:cd03268 75 GALIEAP--GFYPNLTARENLRLLARLLGIRKKR-----IDEVLDVVG-------LKDSAKkkvkGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
336-553 |
1.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQDPYASL 414
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQIRKKVGLVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSIIEPlRVHGLLPgKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK13649 99 FEETVLKDVAFGP-QNFGVSQ-EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-271 |
1.88e-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: 82.95 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSEQSaaqmrhVRGAdMAMIFQE 112
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID-------GQDIRDVTQAS------LRAA-IGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 pmTSLnpvF--TVGEQIAESiRLhqNASREEaMVEAKRM--LDQ--VRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:COG5265 441 --TVL---FndTIAYNIAYG-RP--DASEEE-VEAAARAaqIHDfiESLPDGyDTRVGERGLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 186 RPAVLIADEPTTALDV----TIQAQIlqlikvlqKEMSMG--VIFITHDMGVVAEiADRVLVMYQGEAVETGTveqifHA 259
Cdd:COG5265 512 NPPILIFDEATSALDSrterAIQAAL--------REVARGrtTLVIAHRLSTIVD-ADEILVLEAGRIVERGT-----HA 577
|
250
....*....|..
gi 1134749654 260 pqhpytrALLAA 271
Cdd:COG5265 578 -------ELLAQ 582
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-259 |
2.14e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNiAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQA--GGLVQCDKMLLRRRSRDVIE 89
Cdd:PRK13549 259 ILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRweGEIFIDGKPVKIRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 lseqsaaqmrhvrgADMAMIFQE-PMTSLNPVFTVGEQIAESI--------RLHQNASREEAMVEAKRMldQVRIPEAQT 160
Cdd:PRK13549 338 --------------QGIAMVPEDrKRDGIVPVMGVGKNITLAAldrftggsRIDDAAELKTILESIQRL--KVKTASPEL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRyphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVL 240
Cdd:PRK13549 402 AIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVL 476
|
250 260
....*....|....*....|....
gi 1134749654 241 VMYQGE-----AVETGTVEQIFHA 259
Cdd:PRK13549 477 VMHEGKlkgdlINHNLTQEQVMEA 500
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
29-251 |
2.27e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQC---DKMLLRRRSRDVIELSEQ--SAAQMRHVRG 103
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLEKLviQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 AdmamifQEPMTSLNPVFTVGE-QIAESI--------RLHQNASREEAMVEAKRMLDQVRIPEaqTILSRYPHQLSGGMR 174
Cdd:PRK13651 100 I------KEIRRRVGVVFQFAEyQLFEQTiekdiifgPVSMGVSKEEAKKRAAKYIELVGLDE--SYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-259 |
2.75e-16 |
|
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: 81.79 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNiAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE--QAGGLVQCDKMLLRRRSRDVIE 89
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 lseqsaaqmrhvrgADMAMIFQE-PMTSLNPVFTVGEQIAESI------RLHQNASREEAMVEAKRMLDQVRIPEAQTIL 162
Cdd:TIGR02633 336 --------------AGIAMVPEDrKRHGIVPILGVGKNITLSVlksfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLPI 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 163 SRyphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:TIGR02633 402 GR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
250 260
....*....|....*....|..
gi 1134749654 243 YQGEA----VETG-TVEQIFHA 259
Cdd:TIGR02633 477 GEGKLkgdfVNHAlTQEQVLAA 498
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
303-505 |
2.81e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.07 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 303 EQKTVVDGEPVLrvrnlvtrfPLRSGLLNRVTREVH-------AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE 375
Cdd:PRK10789 296 EAPVVKDGSEPV---------PEGRGELDVNIRQFTypqtdhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 376 SQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprqTIGDSIIEPlRVHGLLPGKEAVARVAWLLERVGLLPE 455
Cdd:PRK10789 367 VSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLFSD---TVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQ 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 456 HawrYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII-NL 505
Cdd:PRK10789 440 G---YDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILhNL 494
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
343-552 |
4.25e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGkLQALRRDIQFIFQDP-----YASLDpr 417
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRG-LLALRQQVATVFQDPeqqifYTDID-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 qtigDSIIEPLRVHGLlPGKEAVARVAWLLERVgllpeHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:PRK13638 97 ----SDIAFSLRNLGV-PEAEITRRVDEALTLV-----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
34-251 |
5.72e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 77.31 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLlrrRSRDVIELSEQSAAQMR----HVRGADMami 109
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTT-------LLDAISGRVEGGGTT---SGQILFNGQPRKPDQFQkcvaYVRQDDI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 fqepmtsLNPVFTVGEQIAESIRL----HQNASREEAMVEAKRMLDQvripeAQTIL-SRYPHQLSGGMRQRVMIAMALS 184
Cdd:cd03234 92 -------LLPGLTVRETLTYTAILrlprKSSDAIRKKRVEDVLLRDL-----ALTRIgGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDMGV-VAEIADRVLVMYQGEAVETG 251
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
311-556 |
5.98e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.76 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdT 390
Cdd:COG1137 1 MMTLEAENLVKSYG---------KRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-T 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPGKLQAlRRDIQFIFQDPyaSLDPRQTIGDSIIEPLRVHGLlPGKEAVARVAWLLERVGLlpEH-AWRYPHEFSGGQR 469
Cdd:COG1137 69 HLPMHKRA-RLGIGYLPQEA--SIFRKLTVEDNILAVLELRKL-SKKEREERLEELLEEFGI--THlRKSKAYSLSGGER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 470 QRICIARALALNPKVIIADEAVSALD---VS-IRGQIINLlldlqRDFGIAYLFISHDmaVVE--RISHRVAVMYLGQIV 543
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVLITDHN--VREtlGICDRAYIISEGKVL 215
|
250
....*....|...
gi 1134749654 544 EIGPRRAVFENPQ 556
Cdd:COG1137 216 AEGTPEEILNNPL 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-248 |
6.09e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.20 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQ--QKIAaVRNLSFSLQRGETLAIVGESGSGKSvTalaLMRLLeqaGGLVQCDKMLLRRRSRDVIEL 90
Cdd:COG1101 2 LELKNLSKTFNPGTvnEKRA-LDGLNLTIEEGDFVTVIGSNGAGKS-T---LLNAI---AGSLPPDSGSILIDGKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEqsaaqmrHVRGADMAMIFQEPMTSLNPVFTVGEQIA--------ESIRLHQNASREEAMVEA---------KRMLDQV 153
Cdd:COG1101 74 PE-------YKRAKYIGRVFQDPMMGTAPSMTIEENLAlayrrgkrRGLRRGLTKKRRELFRELlatlglgleNRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 154 RipeaqtilsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVA 233
Cdd:COG1101 147 G-------------LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAL 213
|
250
....*....|....*
gi 1134749654 234 EIADRVLVMYQGEAV 248
Cdd:COG1101 214 DYGNRLIMMHEGRII 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-261 |
6.14e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDKmllrrRSRDViELSEqsaaqmrhvRGadMAMIF 110
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKS-TLLRMIAGLEDitSGDLFIGEK-----RMNDV-PPAE---------RG--VGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVFTVGEQIAESIRLhqnASREEAmvEAKRMLDQV-RIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:PRK11000 82 QS--YALYPHLSVAENMSFGLKL---AGAKKE--EINQRVNQVaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQ 261
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
314-546 |
6.36e-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: 77.19 E-value: 6.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPLRSGLLNRVT-----------REVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVesqGGeii 382
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLL---AG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 383 fngqrIDTLSPGKLQALRRDIQFIfqDPYASLDPRQTIGDSIIEPLRVHGLLPgKEAVARVAWLLERVGLlpEHAWRYP- 461
Cdd:cd03220 71 -----IYPPDSGTVTVRGRVSSLL--GLGGGFNPELTGRENIYLNGRLLGLSR-KEIDEKIDEIIEFSEL--GDFIDLPv 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAyLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTV-ILVSHDPSSIKRLCDRALVLEKGK 219
|
....*
gi 1134749654 542 IVEIG 546
Cdd:cd03220 220 IRFDG 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-246 |
6.64e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 1 MPHSDELDAGNVLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGlvqcdKMLL 80
Cdd:PRK11247 1 MMNTARLNQGTPLLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLAGLETPSA-----GELL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 81 rrrsrdvielseQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQNASREEAmveakrmLDQVRIPEAQT 160
Cdd:PRK11247 71 ------------AGTAPLAEAR-EDTRLMFQD--ARLLPWKKVIDNVGLGLKGQWRDAALQA-------LAAVGLADRAN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ilsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
Cdd:PRK11247 129 ---EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
....*.
gi 1134749654 241 VMYQGE 246
Cdd:PRK11247 206 LIEEGK 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
314-543 |
8.62e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFPlrSGLLNrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRID 389
Cdd:COG1101 2 LELKNLSKTFN--PGTVN----EKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIagslPPDSGSILIDGKDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 390 TLSPGKlqalR-RDIQFIFQDPYASLDPRQTIGdsiiEPL-------RVHGLLPG---------KEAVARVAWLLE---- 448
Cdd:COG1101 72 KLPEYK----RaKYIGRVFQDPMMGTAPSMTIE----ENLalayrrgKRRGLRRGltkkrrelfRELLATLGLGLEnrld 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 449 -RVGLLpehawryphefSGGQRQriciarALAL------NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFIS 521
Cdd:COG1101 144 tKVGLL-----------SGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVT 206
|
250 260
....*....|....*....|....
gi 1134749654 522 HDM--AVveRISHRVAVMYLGQIV 543
Cdd:COG1101 207 HNMeqAL--DYGNRLIMMHEGRII 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
32-257 |
9.74e-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: 76.81 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTalalmrlLEQAGGLVQCDKmllrrrsrDVIELSEQSAAQMRHVRGADMAMIF- 110
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTT-------FYMIVGLVKPDS--------GKILLDGQDITKLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 -QEPmtSLNPVFTVGEQIAESIRLHqNASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:cd03218 81 pQEA--SIFRKLTVEENILAVLEIR-GLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 190 LIADEPTTALDVTIQAQILQLIKVLqKEMSMGvIFIT-HDMGVVAEIADRVLVMYQGEAVETGTVEQIF 257
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-322 |
1.03e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSE 92
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVA-------GDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQMrhvrgadMAMIFQEpmTSLNPVFTVgEQIAESIRlHQNASREEAMVEAKRMLdqVRIPEAQTILSRYPHQ---- 168
Cdd:PRK09536 73 RAASRR-------VASVPQD--TSLSFEFDV-RQVVEMGR-TPHRSRFDTWTETDRAA--VERAMERTGVAQFADRpvts 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFItHDMGVVAEIADRVLVMYQGEAV 248
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVR 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 249 ETGTVEQIFHAPQhpyTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAPPIEQkTVVDGEPVLR-VRNLVTR 322
Cdd:PRK09536 219 AAGPPADVLTADT---LRAAFDARTAVGTDPATGAPTVTPLPDPDRTEAAADTRVH-VVGGGQPAARaVSRLVAA 289
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-556 |
1.46e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKLQAlRRDIQFIFQDpyASLDPRQT 419
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLHARA-RRGIGYLPQE--ASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIEPLRVHGLLPGKEAVARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvSI 498
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLRdSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD-PI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK10895 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
313-547 |
1.49e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPLRSGLLNRV-----------TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 382 IFNGqRIDTL-SPGklqalrrdiqfifqdpyASLDPRQTIGDSIIEPLRVHGLLPG--KEAVARVAWL--LERVGLLPEH 456
Cdd:COG1134 84 EVNG-RVSALlELG-----------------AGFHPELTGRENIYLNGRLLGLSRKeiDEKFDEIVEFaeLGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 457 awRYphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAV 536
Cdd:COG1134 146 --TY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|.
gi 1134749654 537 MYLGQIVEIGP 547
Cdd:COG1134 219 LEKGRLVMDGD 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
340-567 |
2.04e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPyasLDP--- 416
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQHH---LTPegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 --RQTIGDSIIEPLRVHGLLPGKEAvARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK11231 92 tvRELVAYGRSPWLSLWGRLSAEDN-ARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 495 DVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGprravfeNPQHPYTRKLLAAV 567
Cdd:PRK11231 170 DINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLRTV 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
337-553 |
2.29e-15 |
|
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: 79.10 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE--SQGGEIIFNGQRIDTLSPGKLQalRRDIQFIFQDpyASL 414
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTE--RAGIVIIHQE--LTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSII---EPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
Cdd:TIGR02633 90 VPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE 230
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
37-256 |
2.64e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 75.27 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 37 FSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIELSEqsaaqmRHVRGADMamifqePMTS 116
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQ------RHEFAWDF------PISV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 117 LNPVFTVGEQIAESIRlhqnASREEAMVEAKRMLDQVRIPEaqtiLSRYP-HQLSGGMRQRVMIAMALSCRPAVLIADEP 195
Cdd:TIGR03771 69 AHTVMSGRTGHIGWLR----RPCVADFAAVRDALRRVGLTE----LADRPvGELSGGQRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 196 TTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVlVMYQGEAVETGTVEQI 256
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
340-548 |
2.77e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.87 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL--VESQGGEIIFNGQRIDTLSPgKLQAlRRDIQFIFQdpyasldpr 417
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP-EERA-RLGIFLAFQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 qtigdsiiEPLRVHGLlpgkeavaRVAWLLervgllpehawRYPHE-FSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:cd03217 85 --------YPPEIPGV--------KNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 497 -SIR--GQIINLLldlqRDFGIAYLFISHDMAVVERI-SHRVAVMYLGQIVEIGPR 548
Cdd:cd03217 138 dALRlvAEVINKL----REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-255 |
4.12e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLleQAGGLVQCDKMLLRRRSRDVIELSEQSAaqmrHVRGADMamifqep 113
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFR--SPKGVKGSGSVLLNGMPIDAKEMRAISA----YVQQDDL------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 114 mtsLNPVFTVGEQIAES--IRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ---LSGGMRQRVMIAMALSCRPA 188
Cdd:TIGR00955 110 ---FIPTLTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLIKVL-QKEMSmgVIFITHD-MGVVAEIADRVLVMYQGEAVETGTVEQ 255
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKT--IICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
311-544 |
6.20e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridt 390
Cdd:PRK11288 2 SPYLSFDGIGKTFP-----------GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 lsPGKLQ----ALRRDIQFIFQDpyASLDPRQTIGDSIIE---PLRvHGLLPGKEAVARVAWLLERVGLL--PEHAWRYp 461
Cdd:PRK11288 67 --EMRFAsttaALAAGVAIIYQE--LHLVPEMTVAENLYLgqlPHK-GGIVNRRLLNYEAREQLEHLGVDidPDTPLKY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 heFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
Cdd:PRK11288 141 --LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
...
gi 1134749654 542 IVE 544
Cdd:PRK11288 218 YVA 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-256 |
6.77e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLLRRRSrdvieLSEQSAAQMRHVRGadmAMIFQEPM 114
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARM-----AGLLPGSGSIQFAGQP-----LEAWSAAELARHRA---YLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 TSLNPVFtvgeqiaESIRLHQNASREEAMVEA--KRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMA-LSCRPAV-- 189
Cdd:PRK03695 81 PFAMPVF-------QYLTLHQPDKTRTEAVASalNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 190 ----LIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:PRK03695 151 agqlLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
28-259 |
7.44e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrdvielSEQSAAQMrhvrgadmA 107
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA------SKEVARRI--------G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQEPMTSLNpvFTVGEQIAESIRLHQ------NASREEAMVEAKRMLDQVRIPeAQTIlsrypHQLSGGMRQRVMIAM 181
Cdd:PRK10253 85 LLAQNATTPGD--ITVQELVARGRYPHQplftrwRKEDEEAVTKAMQATGITHLA-DQSV-----DTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHA 259
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-256 |
7.53e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLRR-RSRDVielseqsaAQMrhvrgadMAMI 109
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPDSGEVLVDGLDVATtPSREL--------AKR-------LAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPmtSLNPVFTVGEQIA------ESIRLhqnASREEAMVEakRMLDQVripEAQTILSRYPHQLSGGMRQRVMIAMAL 183
Cdd:COG4604 81 RQEN--HINSRLTVRELVAfgrfpySKGRL---TAEDREIID--EAIAYL---DLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
311-541 |
7.98e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
Cdd:PRK10762 2 QALLQLKGIDKAFP-----------GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 LSPGKLQAlrRDIQFIFQDpyASLDPRQTIGDSII---EPLRVHGLLPGKEAVARVAWLLERVGlLPEHAWRYPHEFSGG 467
Cdd:PRK10762 71 NGPKSSQE--AGIGIIHQE--LNLIPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLN-LRFSSDKLVGELSIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQ-RDFGIAYlfISHDMAVVERISHRVAVMYLGQ 541
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVY--ISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
343-546 |
8.14e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 73.84 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG---GEIIFNGQRidtLSPGKLQalrRDIQFIFQDPY--ASLDPR 417
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQ---KCVAYVRQDDIllPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIgdSIIEPLRVHGLLPGKEAVARVA-WLLERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:cd03234 100 ETL--TYTAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1134749654 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
339-534 |
1.05e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridtlspgkLQALRRDIQFIFQdpyasldpRQ 418
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------------RRAGGARVAYVPQ--------RS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIiePLRVHGLL-------------PGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
Cdd:NF040873 65 EVPDSL--PLTVRDLVamgrwarrglwrrLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRV 534
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-261 |
1.85e-14 |
|
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: 73.09 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCD-KMLLRRRSRDVIEL 90
Cdd:COG0410 3 MLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SeqsaaqMRHV---RGadmamIFQEpMTslnpvftvgeqIAESIRLHQNASREEAmvEAKRMLDQV--RIPEAQTILSRY 165
Cdd:COG0410 79 G------IGYVpegRR-----IFPS-LT-----------VEENLLLGAYARRDRA--EVRADLERVyeLFPRLKERRRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 1134749654 246 EAVETGTVEQIFHAPQ 261
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-255 |
2.65e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 6 ELDAGNVLAVENLNIAFmQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmllrrrsr 85
Cdd:COG4178 356 ETSEDGALALEDLTLRT-PDGRPL--LEDLSLSLKPGERLLITGPSGSGKS----TLLRAI--AG--------------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 86 dvieLSEQSAAQMRHVRGADMAMIFQEPMTslnPVFTVGEQI-----AESIRlhqnasrEEAMVEAkrmLDQVRIPEAQT 160
Cdd:COG4178 412 ----LWPYGSGRIARPAGARVLFLPQRPYL---PLGTLREALlypatAEAFS-------DAELREA---LEAVGLGHLAE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILS---RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLikvLQKEM-SMGVIFITHDmGVVAEIA 236
Cdd:COG4178 475 RLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELpGTTVISVGHR-STLAAFH 550
|
250
....*....|....*....
gi 1134749654 237 DRVLVMYQGEAVETGTVEQ 255
Cdd:COG4178 551 DRVLELTGDGSWQLLPAEA 569
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-246 |
2.82e-14 |
|
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: 71.81 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQQKIAA--VRNLSFSLQRGETLAIVGESGSGKS--VTALALMRLLEQAGGLVqcdkmLLRRRSRDV 87
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKStlLNALAGRRTGLGVSGEV-----LINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 88 IELSEQSAAQMRHvrgaDMAMifqepmtslnPVFTVgeqiaesirlhqnasREEAMVEAKrmldqvripeaqtiLSryph 167
Cdd:cd03213 78 RSFRKIIGYVPQD----DILH----------PTLTV---------------RETLMFAAK--------------LR---- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHD-MGVVAEIADRVLVMYQ 244
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD---SSSALQVMSLLRRLADTGrtIICSIHQpSSEIFELFDKLLLLSQ 187
|
..
gi 1134749654 245 GE 246
Cdd:cd03213 188 GR 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
162-264 |
2.92e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.53 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
Cdd:PRK11144 122 LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVV 201
|
90 100
....*....|....*....|....
gi 1134749654 242 MYQGEAVETGTVEQIFHAPQ-HPY 264
Cdd:PRK11144 202 LEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-536 |
3.13e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRV 239
Cdd:PRK13409 205 ILDRDISELSGGELQRVAIAAALL-RDAdFYFFDEPTSYLDIRQRLNVARLIRELAEGKY--VLVVEHDLAVLDYLADNV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 240 LVMYqGEAVETGTVeqifhapQHPYtrallaavpqlGAMKGLDY------P------RRFPLISLEHPakqappieQKTV 307
Cdd:PRK13409 282 HIAY-GEPGAYGVV-------SKPK-----------GVRVGINEylkgylPeenmriRPEPIEFEERP--------PRDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 308 VDGEPVLRVRNLVTRfplrsglLNRVTREVHAVEkvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN--- 384
Cdd:PRK13409 335 SERETLVEYPDLTKK-------LGDFSLEVEGGE-----IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElki 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 385 ---GQRIDTLSPGKLQALRRDIQFIFQDPYASLDprqtigdsIIEPLRVHGLLPgkeavarvawllervgllpehawRYP 461
Cdd:PRK13409 403 sykPQYIKPDYDGTVEDLLRSITDDLGSSYYKSE--------IIKPLQLERLLD-----------------------KNV 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-251 |
3.33e-14 |
|
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: 71.19 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVIELSEQsaaqM 98
Cdd:cd03247 5 NVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-------GVPVSDLEKA----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 RHVrgadMAMIFQEPMtslnpVFtvgeqiaesirlhqnasreeamveakrmldqvripeAQTILSRYPHQLSGGMRQRVM 178
Cdd:cd03247 74 SSL----ISVLNQRPY-----LF------------------------------------DTTLRNNLGRRFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGEAVETG 251
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKT--LIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-244 |
5.29e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLEqagGLVQCDKMLLRRRSRDVIEL 90
Cdd:PRK09544 3 SLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKST----LVRVVL---GLVAPDEGVIKRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSaaqmrhvrgadmamifqepmTSLNPvfTVGEQIAESIRLHQNASREEAMVEAKRMldqvripEAQTILSRYPHQLS 170
Cdd:PRK09544 72 VPQK--------------------LYLDT--TLPLTVNRFLRLRPGTKKEDILPALKRV-------QAGHLIDAPMQKLS 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-260 |
5.59e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL-----RRRSRDVIELSEQ-SAAQMRHVRgaDMAM 108
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswssKAFARKVAYLPQQlPAAEGMTVR--ELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPMTSLNPVFTVG--EQIAESIrlhqnasreeAMVEAKrmldqvriPEAQtilsRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:PRK10575 108 IGRYPWHGALGRFGAAdrEKVEEAI----------SLVGLK--------PLAH----RLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-269 |
8.49e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQDQQKIAAvrNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVIELSEQS 94
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFD--NISLTVPRGKITAIMGPSGIGKT----TLLRLI---GGQIAPDHGEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 95 AAQMRHvrgaDMAMIFQEP--MTSLNpVFtvgEQIAESIRLHQNASreEAMVEAKRM--LDQVRIPEAQTILsryPHQLS 170
Cdd:PRK11831 79 LYTVRK----RMSMLFQSGalFTDMN-VF---DNVAYPLREHTQLP--APLLHSTVMmkLEAVGLRGAAKLM---PSELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
Cdd:PRK11831 146 GGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
250
....*....|....*....
gi 1134749654 251 GTVEQIfHAPQHPYTRALL 269
Cdd:PRK11831 226 GSAQAL-QANPDPRVRQFL 243
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-242 |
8.85e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 19 NIAFMQDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRDVIELSEQSAAQm 98
Cdd:PRK10247 12 NVGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKST-------LLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 99 rhvrgaDMAMIFQEPMtslnpVF--TVGEQIAESIRLHQNASREEAMVeakRMLDQVRIPEaqTILSRYPHQLSGGMRQR 176
Cdd:PRK10247 82 ------QVSYCAQTPT-----LFgdTVYDNLIFPWQIRNQQPDPAIFL---DDLERFALPD--TILTKNIAELSGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVM 242
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-242 |
9.38e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.96 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrdvielseqsaaqmRHVRGADMAMIF 110
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------------------RRAGGARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QEpmTSLNPVF--TVGEQIAESIRLHQNASRE---EAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
Cdd:NF040873 62 QR--SEVPDSLplTVRDLVAMGRWARRGLWRRltrDDRAAVDDALERVGL---ADLAGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEiADRVLVM 242
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-547 |
1.21e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQdpYASLDPRQT 419
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIEPLRVHGlLPGKEAVARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:PRK13536 131 VRENLLVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1134749654 500 GQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLG-QIVEIGP 547
Cdd:PRK13536 209 HLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRP 256
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-571 |
1.22e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 357 GESGSGKSTTGRALLRLVESQGGEIIFNGQR-IDTLSPGKLQALRRDIQFIFQDpyASLDPRqtigdsiiepLRVHGLLP 435
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQD--ARLFPH----------YKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 436 GKEAVARVAWLLERVGLLP-EHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDF 513
Cdd:PRK11144 99 YGMAKSMVAQFDKIVALLGiEPLLdRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 514 GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ-HPY----TRKLLAAVPVAE 571
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPWlpkeEQSSILKVTVLE 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
291-522 |
1.29e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 291 SLEHPAKQAPPIEQKTVVDGEpVLRVRNLVTRFPLRSGLlnrvtrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
Cdd:COG4178 341 ALEAADALPEAASRIETSEDG-ALALEDLTLRTPDGRPL----------LEDLSLSLKPGERLLITGPSGSGKSTLLRAI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 371 LRLVESQGGEIIFngqridtlsPGKLQALrrdiqFIFQDPYAsldPRQTIGDSIIEPLRVHGLlpGKEAVARVawlLERV 450
Cdd:COG4178 410 AGLWPYGSGRIAR---------PAGARVL-----FLPQRPYL---PLGTLREALLYPATAEAF--SDAELREA---LEAV 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 451 GL--LPEH-----AWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLldLQRDFGIAYLFISH 522
Cdd:COG4178 468 GLghLAERldeeaDW--DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
314-554 |
1.53e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 71.09 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 314 LRVRNLVTRFplrSGLLNRVTREVHAVEKvsfdlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
Cdd:cd03288 20 IKIHDLCVRY---ENNLKPVLKHVKAYIK------PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 394 gkLQALRRDIQFIFQDPYA-------SLDPRQTIGDSII-EPLRVHGLlpgKEAVARVAWLLERVglLPEHAwrypHEFS 465
Cdd:cd03288 90 --LHTLRSRLSIILQDPILfsgsirfNLDPECKCTDDRLwEALEIAQL---KNMVKSLPGGLDAV--VTEGG----ENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVEI 545
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVSTILDADLVLV 226
|
....*....
gi 1134749654 546 GPRRAVFEN 554
Cdd:cd03288 227 LSRGILVEC 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-556 |
1.81e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprqTIG 421
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDP--------VLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 422 DSIIEplrvHGLLPGKEAVARVAW-LLERVGLLPehawRYPHE--------------FSGGQRQRICIARA-LALNPKVI 485
Cdd:PTZ00243 1397 DGTVR----QNVDPFLEASSAEVWaALELVGLRE----RVASEsegidsrvleggsnYSVGQRQLMCMARAlLKKGSGFI 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLqrdFGiAYLFIShdmavverISHR---VA------VMYLGQIVEIGPRRAVFENPQ 556
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSA---FS-AYTVIT--------IAHRlhtVAqydkiiVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-256 |
2.23e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRDVIELSEQSAAQmrhvRGadMAMIFQ 111
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI-------RLNGKDISPRSPLDAVK----KG--MAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EPM-TSLNPVFTVGEQIAESIRLHQ----------NASREEAMVEAKRMLDQVRIPEA-QTIlsrypHQLSGGMRQRVMI 179
Cdd:PRK09700 346 SRRdNGFFPNFSIAQNMAISRSLKDggykgamglfHEVDEQRTAENQRELLALKCHSVnQNI-----TELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGE------AVETGTV 253
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRltqiltNRDDMSE 499
|
...
gi 1134749654 254 EQI 256
Cdd:PRK09700 500 EEI 502
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
312-555 |
2.81e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
Cdd:PRK09536 2 PMIDVSDLSVEFG-----------DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 SPgklQALRRDIQFIFQDPYASLDPRqtiGDSIIE----P--LRVHGLLPGKEAVARVAwlLERVGLlPEHAWRYPHEFS 465
Cdd:PRK09536 71 SA---RAASRRVASVPQDTSLSFEFD---VRQVVEmgrtPhrSRFDTWTETDRAAVERA--MERTGV-AQFADRPVTSLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
|
250
....*....|
gi 1134749654 546 GPRRAVFENP 555
Cdd:PRK09536 221 GPPADVLTAD 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-255 |
3.38e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.07 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNiAFMQdqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQC-DKMLLRRRSRDVIEL 90
Cdd:PRK10982 250 ILEVRNLT-SLRQ-----PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKINNHNANEAINH 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAQMRHVRGadmamIFQEPMTSLNPVFTVGEQIAESIRLHQNA---SREEAMVEAKRmldqVRIPEAQTILSryph 167
Cdd:PRK10982 324 GFALVTEERRSTG-----IYAYLDIGFNSLISNIRNYKNKVGLLDNSrmkSDTQWVIDSMR----VKTPGHRTQIG---- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
250
....*....|.
gi 1134749654 248 ---VETGTVEQ 255
Cdd:PRK10982 470 agiVDTKTTTQ 480
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
340-551 |
3.43e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 72.38 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQA----LRRDIQFI--------- 406
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKhigyLPQDVELFpgtvaenia 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 407 -FQDpyaSLDPRQTIgdsiieplrvhgllpgkeAVARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALN 481
Cdd:TIGR01842 414 rFGE---NADPEKII------------------EAAKLAGVHELILRLPDGYDTVIGPggatLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 482 PKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAV 551
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVD-KILVLQDGRIARFGERDEV 540
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
330-528 |
3.48e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 330 LNRVTRevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqalrrDIQFifqd 409
Cdd:COG2401 38 LRVVER--YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVP---------------DNQF---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 410 pyaslDPRQTIGDSIieplrvhgllPGKEAVARVAWLLERVGLLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIAD 488
Cdd:COG2401 97 -----GREASLIDAI----------GRKGDFKDAVELLNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1134749654 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVE 528
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-256 |
3.54e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.67 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRDVIELS 91
Cdd:COG1137 3 TLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-------EDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 eqsaaqMrHVRgADMAMIF--QEPmtSlnpVF---TVGEQIAeSIRLHQNASREEAMVEAKRMLDQVRIpeaQTILSRYP 166
Cdd:COG1137 72 ------M-HKR-ARLGIGYlpQEA--S---IFrklTVEDNIL-AVLELRKLSKKEREERLEELLEEFGI---THLRKSKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD---VT-IQAQILQLikvlqKEMSMGVIfIT-HDmgvVAE---IADR 238
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVL-ITdHN---VREtlgICDR 205
|
250
....*....|....*...
gi 1134749654 239 VLVMYQGEAVETGTVEQI 256
Cdd:COG1137 206 AYIISEGKVLAEGTPEEI 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-242 |
4.28e-13 |
|
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: 66.70 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLvqcdkmllrrrsrdvielse 92
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKS----TLLKLI--AGEL-------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsaaqmrhvrgadmamifqepmtslnpvftvgEQIAESIRLHQNasreeamveakrmldqVRIPeaqtilsrYPHQLSGG 172
Cdd:cd03221 51 --------------------------------EPDEGIVTWGST----------------VKIG--------YFEQLSGG 74
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:cd03221 75 EKMRLALAKLLLENPNLLLLDEPTNHLDLE---SIEALEEAL-KEYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-617 |
4.39e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQA--GGLVQCDKMLLRRR-----SRDVIE---------LSEQSA 95
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKS----TLMKILngEVLldDGRIIYEQDLIVARlqqdpPRNVEGtvydfvaegIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 96 AQMRHVRGADMAMifQEPMTS-LNPVFTVGEQIAesirlHQNASREEAMVeaKRMLDQVRIPeAQTILSryphQLSGGMR 174
Cdd:PRK11147 97 YLKRYHDISHLVE--TDPSEKnLNELAKLQEQLD-----HHNLWQLENRI--NEVLAQLGLD-PDAALS----SLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 175 QRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIADR-------VLVMYQGEa 247
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIE---TIEWLEGFL-KTFQGSIIFISHDRSFIRNMATRivdldrgKLVSYPGN- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 248 vetgtveqifhapqhpYTRALLAAVPQL--GAMKGLDYPRRFplislehpAKQAPPIEQ-----KTVVDGepvlRVRNLV 320
Cdd:PRK11147 238 ----------------YDQYLLEKEEALrvEELQNAEFDRKL--------AQEEVWIRQgikarRTRNEG----RVRALK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 321 TRFPLRSGLLNRV----------TRE---VHAVEKVSFDLwPGETL--------------SLVGESGSGKSTTGRALLRL 373
Cdd:PRK11147 290 ALRRERSERREVMgtakmqveeaSRSgkiVFEMENVNYQI-DGKQLvkdfsaqvqrgdkiALIGPNGCGKTTLLKLMLGQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 374 VESQGGEIifngqRIDTlspgKLqalrrDIQFIfqDPY-ASLDPRQTIGDSIIEplrvhgllpGKEAVArvawllerVGL 452
Cdd:PRK11147 369 LQADSGRI-----HCGT----KL-----EVAYF--DQHrAELDPEKTVMDNLAE---------GKQEVM--------VNG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 453 LPEHAWRYPHEF--------------SGGQRQRICIARaLALNP-KVIIADEAVSALDVsirgQIINLLLDLQRDFGIAY 517
Cdd:PRK11147 416 RPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTV 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 518 LFISHDMAVVErisHRVAVMYL----GQIVE--------IGPRRAVFENPQHPYTRKLLAAVPVAEPSRQRP-------Q 578
Cdd:PRK11147 491 LLVSHDRQFVD---NTVTECWIfegnGKIGRyvggyhdaRQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSkklsyklQ 567
|
650 660 670
....*....|....*....|....*....|....*....
gi 1134749654 579 RVLlsDDLPSNIHLRGEEVAAVSLQCVGPGHYvAQPQSE 617
Cdd:PRK11147 568 REL--EQLPQLLEDLEAEIEALQAQVADADFF-SQPHEQ 603
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
338-546 |
5.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYASLDPR 417
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDPDDQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHglLPGKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:PRK13647 96 TVWDDVAFGPVNMG--LDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1134749654 498 IRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
313-544 |
6.38e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLVTRFPlrsGllnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVE------SQGGEIIFNGQ 386
Cdd:NF040905 1 ILEMRGITKTFP---G--------VKALDDVNLSVREGEIHALCGENGAGKST----LMKVLSgvyphgSYEGEILFDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 387 --RIDTLSpgklQALRRDIQFIFQDpyASLDPRQTIGDSII---EPLRvHGLLPGKEAVARVAWLLERVGlLPEHawryP 461
Cdd:NF040905 66 vcRFKDIR----DSEALGIVIIHQE--LALIPYLSIAENIFlgnERAK-RGVIDWNETNRRARELLAKVG-LDES----P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSG----GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVM 537
Cdd:NF040905 134 DTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVL 212
|
....*..
gi 1134749654 538 YLGQIVE 544
Cdd:NF040905 213 RDGRTIE 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-546 |
6.58e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 298 QAPPI---EQKTVVDGEPVLRVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
Cdd:PRK11160 320 QKPEVtfpTTSTAAADQVSLTLNNVSFTYP---------DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 375 ESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYasldprqTIGDSIIEPLRVHGLLPGKEAVARVawlLERVGL-- 452
Cdd:PRK11160 391 DPQQGEILLNGQPIADYSE---AALRQAISVVSQRVH-------LFSATLRDNLLLAAPNASDEALIEV---LQQVGLek 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 453 LPEH-----AW-----RyphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISH 522
Cdd:PRK11160 458 LLEDdkglnAWlgeggR---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITH 532
|
250 260
....*....|....*....|....
gi 1134749654 523 DMAVVERIShRVAVMYLGQIVEIG 546
Cdd:PRK11160 533 RLTGLEQFD-RICVMDNGQIIEQG 555
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-227 |
1.01e-12 |
|
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: 66.41 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKiaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCdkmllrrRSRDVIelse 92
Cdd:cd03223 1 IELENLSLATPDGRVL---LKDLSFEIKPGDRLLITGPSGTGKS----SLFRAL---AGLWPW-------GSGRIG---- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 qsaaqmRHvRGADMAMIFQEPMTslnPVFTVGEQIAesirlhqnasreeamveakrmldqvripeaqtilsrYP--HQLS 170
Cdd:cd03223 60 ------MP-EGEDLLFLPQRPYL---PLGTLREQLI------------------------------------YPwdDVLS 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvlqKEMSMGVIFITH 227
Cdd:cd03223 94 GGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-260 |
1.19e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 21 AFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLrrrsrdvielseqSAAQMR 99
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSLIqRHFDVSEGDIRFHDIPL-------------TKLQLD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 100 HVRGAdMAMIFQEPmtslnpvFTVGEQIAESIRLHQNASREEAMVEAKRML----DQVRIPEA-QTILSRYPHQLSGGMR 174
Cdd:PRK10789 386 SWRSR-LAVVSQTP-------FLFSDTVANNIALGRPDATQQEIEHVARLAsvhdDILRLPQGyDTEVGERGVMLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGTVE 254
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT--VIISAHRLSALTE-ASEILVMQHGHIAQRGNHD 534
|
....*.
gi 1134749654 255 QIFHAP 260
Cdd:PRK10789 535 QLAQQS 540
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
311-552 |
1.26e-12 |
|
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: 68.19 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 311 EPVLRVRNlVTrfplrsgllnrVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV-----ESQGGEIIFN 384
Cdd:COG1119 1 DPLLELRN-VT-----------VRRgGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLItgdlpPTYGNDVRLF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 385 GQRIDTLSpgkLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLR-VHGLL--PGKEAVARVAWLLERVGLLpEHAWRYP 461
Cdd:COG1119 65 GERRGGED---VWELRKRIGLVSPALQLRFPRDETVLDVVLSGFFdSIGLYrePTDEQRERARELLELLGLA-HLADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMA-VVERISHrVAVMYLG 540
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITH-VLLLKDG 219
|
250
....*....|..
gi 1134749654 541 QIVEIGPRRAVF 552
Cdd:COG1119 220 RVVAAGPKEEVL 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-228 |
1.31e-12 |
|
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: 70.47 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRDVIELSEQSAAQMRHVRGADmami 109
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTT---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 fqepmtslnpvftvgeqIAESIRL-HQNASREE--AMVEAKRMLDQVR-IPE-AQTILSRYPHQLSGGMRQRVMIAMALS 184
Cdd:TIGR02868 425 -----------------VRENLRLaRPDATDEElwAALERVGLADWLRaLPDgLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1134749654 185 CRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHD 228
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
315-558 |
1.32e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 315 RVRNLVTRFPLRSGLLNRVTREvhavekvsfdLWPGETLSLVGESGSGKSTTGRAL--LRLVESQG-GEIIFNGQRIDtl 391
Cdd:TIGR00955 26 RLRGCFCRERPRKHLLKNVSGV----------AKPGELLAVMGSSGAGKTTLMNALafRSPKGVKGsGSVLLNGMPID-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 392 spgkLQALRRDIQFIFQDP--YASLDPRQTIgdSIIEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHE-----F 464
Cdd:TIGR00955 94 ----AKEMRAISAYVQQDDlfIPTLTVREHL--MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgrvkgL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAY 247
|
250
....*....|....*..
gi 1134749654 545 IG-PRRAV--FENPQHP 558
Cdd:TIGR00955 248 LGsPDQAVpfFSDLGHP 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
343-561 |
1.32e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLD 415
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQSPVLfsgtvrfNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGDS-IIEPL-RVHgllpGKEAVARVAWLLErvgllpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:PLN03232 1332 PFSEHNDAdLWEALeRAH----IKDVIDRNPFGLD------AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 494 LDVSIRGQIINlllDLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEigprravFENPQHPYTR 561
Cdd:PLN03232 1402 VDVRTDSLIQR---TIREEFkSCTMLVIAHRLNTIIDCD-KILVLSSGQVLE-------YDSPQELLSR 1459
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-249 |
1.45e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLvqcdkmllrrrsrdviels 91
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLL--AGEL------------------- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 EQSAAQMRHVRGADMAMIFQEpMTSLNPVFTVGEQIAesiRLHQNASREEAMVEAKRML---DQVRipeaqtilsRYPHQ 168
Cdd:COG0488 366 EPDSGTVKLGETVKIGYFDQH-QEELDPDKTVLDELR---DGAPGGTEQEVRGYLGRFLfsgDDAF---------KPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAqilqLIKVLQK-EmsmG-VIFITHDMGVVAEIADRVLVMYQG 245
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDfP---GtVLLVSHDRYFLDRVATRILEFEDG 505
|
....
gi 1134749654 246 EAVE 249
Cdd:COG0488 506 GVRE 509
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-255 |
2.13e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.85 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 3 HSDELDAGNvLAVENLNIAFMQDQQKiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAgglVQCDKMLLRR 82
Cdd:PRK11160 330 STAAADQVS-LTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRA---WDPQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 83 RSRDVIELSEQSAAQMrhvrgadMAMIFQEpmtslnpVFTVGEQIAESIRLHQNASREEAMVEakrMLDQVripEAQTIL 162
Cdd:PRK11160 400 NGQPIADYSEAALRQA-------ISVVSQR-------VHLFSATLRDNLLLAAPNASDEALIE---VLQQV---GLEKLL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 163 SRYP----------HQLSGGMRQRVMIAMALsCRPA-VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGV 231
Cdd:PRK11160 460 EDDKglnawlgeggRQLSGGEQRRLGIARAL-LHDApLLLLDEPTEGLDAETERQILELLAEHAQNKT--VLMITHRLTG 536
|
250 260
....*....|....*....|....
gi 1134749654 232 VAEIaDRVLVMYQGEAVETGTVEQ 255
Cdd:PRK11160 537 LEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
313-522 |
3.59e-12 |
|
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: 65.65 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 313 VLRVRNLvtRFPLRSGLLNRVTREVHaveKVSFDLWPGETLSLVGESGSGKSTTGRAL--LRLVESQGGEIIFNGQridt 390
Cdd:cd03213 3 TLSFRNL--TVTVKSSPSKSGKQLLK---NVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 391 lsPGKLQALRRDIQFIFQDpyasldprqtigDSIIEPLRVhgllpgKEAVARVAWLleRvGLlpehawryphefSGGQRQ 470
Cdd:cd03213 74 --PLDKRSFRKIIGYVPQD------------DILHPTLTV------RETLMFAAKL--R-GL------------SGGERK 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISH 522
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-259 |
4.13e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagGLVQCDKMLLRRRSRDVIELSE 92
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLM-------GYYPLTEGEIRLDGRPLSSLSH 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAQmrhvrgaDMAMIFQEPMTSLNPVF---TVGEQIAESirlhqnasREEAMVEAKRMLDQVR-IPEA-QTILSRYPH 167
Cdd:PRK10790 411 SVLRQ-------GVAMVQQDPVVLADTFLanvTLGRDISEE--------QVWQALETVQLAELARsLPDGlYTPLGEQGN 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLVMYQGEA 247
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQA 552
|
250
....*....|..
gi 1134749654 248 VETGTVEQIFHA 259
Cdd:PRK10790 553 VEQGTHQQLLAA 564
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-251 |
4.32e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTAlalmrlleqagglvqcdKMLLRRRSRDVIELSEQSAAQMRHVRGADMAMI 109
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIA-----------------RMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPMTSLNPVFTVGEQIAESIRLHQNASRE-EAMVEAkrMLDQVRIP-EAQTILSryphQLSGGMRQRVMIAMALSCRP 187
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREiEAVIPS--LLEFARLEsKADARVS----DLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-259 |
5.03e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSR-DVIELSEQSaaqmrhvrgadmami 109
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQkNLVAYVPQS--------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 fqEPMTSLNPVFTvgEQIAESIR------LHQNASREEAMVEAKrmLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMAL 183
Cdd:PRK15056 87 --EEVDWSFPVLV--EDVVMMGRyghmgwLRRAKKRDRQIVTAA--LARVDMVEFR---HRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVlVMYQGEAVETGTVEQIFHA 259
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTA 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
325-554 |
5.26e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 325 LRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV---ESQGGEIIFNG---QRIDTLSpGKLQA 398
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvQREGRLA-RDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 399 LRRDIQFIFQDpyASLDPRQTIGDSIIepLRVHGLLP---------GKEAVARVAWLLERVGLLpEHAWRYPHEFSGGQR 469
Cdd:PRK09984 84 SRANTGYIFQQ--FNLVNRLSVLENVL--IGALGSTPfwrtcfswfTREQKQRALQALTRVGMV-HFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
....*
gi 1134749654 550 AvFEN 554
Cdd:PRK09984 239 Q-FDN 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
350-546 |
5.88e-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: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTIGD 422
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVlfsgslrMNLDPFSQYSD 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SiieplrvhgllpgkeavaRVAWLLER------VGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADE 489
Cdd:TIGR00957 1389 E------------------EVWWALELahlktfVSALPD---KLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 490 AVSALDVSIrGQIINLLLDLQRDfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
Cdd:TIGR00957 1448 ATAAVDLET-DNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
341-551 |
5.89e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPyasldprQTI 420
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVARRIGLLAQNA-------TTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIIEPLRVHGLLPG--------KEAVARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:PRK10253 94 GDITVQELVARGRYPHqplftrwrKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG-PRRAV 551
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGaPKEIV 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-260 |
6.20e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 6 ELDAGNVLAVENLNIAFMQDQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdKMllrrrsr 85
Cdd:PRK11174 343 ASNDPVTIEAEDLEILSPDGKT---LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSL----KI------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 86 DVIELSEQSAAQMRHvrgaDMAMIFQEPMTslnpvftVGEQIAESIRL-HQNASREEAMveakRMLDQVRIPEaqtILSR 164
Cdd:PRK11174 409 NGIELRELDPESWRK----HLSWVGQNPQL-------PHGTLRDNVLLgNPDASDEQLQ----QALENAWVSE---FLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlikVLQKEM-SMGVIFITHDMGVV 232
Cdd:PRK11174 471 LPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ---ALNAASrRQTTLMVTHQLEDL 547
|
250 260
....*....|....*....|....*...
gi 1134749654 233 AEIaDRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PRK11174 548 AQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-254 |
7.13e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.86 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALM--RLLEQAGGlvqcdKMLLRrrSRDVIEL 90
Cdd:COG0396 1 LEIKNLHVSV--EGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSG-----SILLD--GEDILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 S-EQSAAqmrhvrgADMAMIFQepmtslNPV----FTVGE--QIAESIRLHQNASREEAMVEAKRMLDQVRIPEAqtILS 163
Cdd:COG0396 70 SpDERAR-------AGIFLAFQ------YPVeipgVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLDED--FLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 164 RYPHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAqILQLIKVLQKEmSMGVIFITHDMGVVAEI-ADRVL 240
Cdd:COG0396 135 RYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPDFVH 212
|
250
....*....|....
gi 1134749654 241 VMYQGEAVETGTVE 254
Cdd:COG0396 213 VLVDGRIVKSGGKE 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
343-496 |
1.06e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPYA-------SLD 415
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFG-LMDLRKVLGIIPQAPVLfsgtvrfNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGDS-IIEPL-RVHgllpGKEAVARVAwllerVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:PLN03130 1335 PFNEHNDAdLWESLeRAH----LKDVIRRNS-----LGLDAEVS-EAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
...
gi 1134749654 494 LDV 496
Cdd:PLN03130 1405 VDV 1407
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
343-527 |
1.28e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalrrdiqfifqdpyaSLDPRQtigd 422
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL----------------YLDTTL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 siiePLRVHGLLPGKEAVARVAWL--LERVGllPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:PRK09544 83 ----PLTVNRFLRLRPGTKKEDILpaLKRVQ--AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 1134749654 500 GQIINLLLDLQRDFGIAYLFISHDMAVV 527
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
161-536 |
1.29e-11 |
|
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: 67.50 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRV 239
Cdd:COG1245 205 ILDRDISELSGGELQRVAIAAALL-RDAdFYFFDEPSSYLDIYQRLNVARLIRELAEEGKY-VLVVEHDLAILDYLADYV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 240 LVMYqGEAVETGTVeqifhapQHPY-TRallAAVPQ-----LGA--MKGLDYPRRFPlislEHPAKQappieqktVVDGE 311
Cdd:COG1245 283 HILY-GEPGVYGVV-------SKPKsVR---VGINQyldgyLPEenVRIRDEPIEFE----VHAPRR--------EKEEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRFPlrsgllnRVTREVHAVEkvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN------G 385
Cdd:COG1245 340 TLVEYPDLTKSYG-------GFSLEVEGGE-----IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 386 QRIDTLSPGKLQA-LRRDIQFIFQDPYASLDprqtigdsIIEPLRVHGLLPgkeavarvawllervgllpehawRYPHEF 464
Cdd:COG1245 408 QYISPDYDGTVEEfLRSANTDDFGSSYYKTE--------IIKPLGLEKLLD-----------------------KNVKDL 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
335-495 |
1.41e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidTLSPGKLQALRRDIQFIFQDP---- 410
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRSKIGVVSQDPllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 411 -------------------------------YASLDPRQ----------------TIGDSIIEPLRVHGLLPGKEAV--A 441
Cdd:PTZ00265 474 nsiknnikyslyslkdlealsnyynedgndsQENKNKRNscrakcagdlndmsntTDSNELIEMRKNYQTIKDSEVVdvS 553
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 442 RVAWLLERVGLLPEhawRY-------PHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:PTZ00265 554 KKVLIHDFVSALPD---KYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-261 |
1.54e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK-----MLLRRRSRD 86
Cdd:PRK10895 3 TLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 87 VIELSEQSAAQMRHVrgadmamifqepmtslnpvfTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRyp 166
Cdd:PRK10895 79 GIGYLPQEASIFRRL--------------------SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 167 hQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
Cdd:PRK10895 137 -SLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
250
....*....|....*
gi 1134749654 247 AVETGTVEQIFHAPQ 261
Cdd:PRK10895 215 LIAHGTPTEILQDEH 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-546 |
2.00e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGgEIIFNGQRIDTLSPgklQALRRDIQFIFQDPyasLDPRQTIGD 422
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDP---ESWRKHLSWVGQNP---QLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SIieplrvhglLPGK---------EAVARvAWLLERVGLLP--------EHAWRypheFSGGQRQRICIARALALNPKVI 485
Cdd:PRK11174 442 NV---------LLGNpdasdeqlqQALEN-AWVSEFLPLLPqgldtpigDQAAG----LSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 486 IADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISH---DMAVVERIshrvAVMYLGQIVEIG 546
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHqleDLAQWDQI----WVMQDGQIVQQG 565
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-258 |
2.36e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.44 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 17 NLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGL--------VQCDKMLLRRRsRDVI 88
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegdihyngIPYKEFAEKYP-GEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 89 ELSEQSaaqmRHVrgadmamifqepmtslnPVFTVGEQIAESIRLHQNASreeamveakrmldqVRipeaqtilsryphQ 168
Cdd:cd03233 87 YVSEED----VHF-----------------PTLTVRETLDFALRCKGNEF--------------VR-------------G 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVA-EIADRVLVMYQGea 247
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEG-- 196
|
250
....*....|.
gi 1134749654 248 vetgtvEQIFH 258
Cdd:cd03233 197 ------RQIYY 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-251 |
2.47e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.21 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-QAGGLVQCDKMLLRRRSRdvielseqsaAQMRhvrgadMAMIF 110
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARH----------ARQR------VGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 111 QepMTSLNPVFTVGEQIAESIRL-----HQNASREEAMVEAKRMLDQVripEAQTilsrypHQLSGGMRQRVMIAMALSC 185
Cdd:PRK13537 87 Q--FDNLDPDFTVRENLLVFGRYfglsaAAARALVPPLLEFAKLENKA---DAKV------GELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 186 RPAVLIADEPTTALDVTIQAQILQLIKVLqkeMSMG--VIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSL---LARGktILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
349-547 |
2.50e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQD-PYASldprqtiGDSIIEP 427
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQlPAAE-------GMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 428 LRV-----HGLLP--GKEAVARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
Cdd:PRK10575 106 VAIgrypwHGALGrfGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1134749654 501 QIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
340-522 |
3.00e-11 |
|
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: 66.31 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALlrlvesqgGEI--IFNGqRIDTLSPGKlqalrrdIQFIFQDPYASLdpr 417
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELwpVYGG-RLTKPAKGK-------LFYVPQRPYMTL--- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSIIEPLRVHGL----LPGKEAVA-----RVAWLLER-VGLLPEHAWRypHEFSGGQRQRICIARALALNPKVIIA 487
Cdd:TIGR00954 529 GTLRDQIIYPDSSEDMkrrgLSDKDLEQildnvQLTHILEReGGWSAVQDWM--DVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 1134749654 488 DEAVSALDVSIRGQIINLLldlqRDFGIAYLFISH 522
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-242 |
3.25e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 24 QDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLeqagglvqcdkmllrrrsrdvielseqsAAQMRHVRG 103
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL----------------------------AGALKGTPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 ADMAMIFQEPmtslnpvFTVGEQIAESIrlhqnaSREEAMVEAKRMLDQVRIPEAQTILSRYPHqLSGGMRQRVMIAMAL 183
Cdd:COG2401 86 AGCVDVPDNQ-------FGREASLIDAI------GRKGDFKDAVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 184 SCRPAVLIADEPTTALDVTiQAQILQL-IKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-255 |
3.40e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFMQDQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKM------LLRRrsr 85
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKST-------LLRHLSGLITGDKSagshieLLGR--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 86 dVIELSEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIA----ESIRLHQNASREEAMVEAKRMLDQVripeAQTI 161
Cdd:PRK09984 70 -TVQREGRLARDIRKSR-ANTGYIFQQ--FNLVNRLSVLENVLigalGSTPFWRTCFSWFTREQKQRALQAL----TRVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIAD 237
Cdd:PRK09984 142 MVHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCE 221
|
250
....*....|....*...
gi 1134749654 238 RVLVMYQGEAVETGTVEQ 255
Cdd:PRK09984 222 RIVALRQGHVFYDGSSQQ 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-245 |
3.61e-11 |
|
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: 63.12 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrDVIELSEQSAAQMRHVRGAdMAM 108
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS---------NKNESEPSFEATRSRNRYS-VAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPMTsLNPvfTVGEQIAESIRLhqNASREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALSCR 186
Cdd:cd03290 84 AAQKPWL-LNA--TVEENITFGSPF--NKQRYKAVTDACSLQPDIDLlPFGdQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 187 PAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQG 245
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-LVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
339-540 |
6.09e-11 |
|
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: 65.81 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQ--FDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIIEPLRVHGlLPGKEaVARVA-WLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:TIGR01257 2028 TGREHLYLYARLRG-VPAEE-IEKVAnWSIQSLG-LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1134749654 498 IRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLG 540
Cdd:TIGR01257 2105 ARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-241 |
7.18e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 15 VENLNIAFMQdQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL---------------------------- 66
Cdd:PTZ00265 1168 IMDVNFRYIS-RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgde 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 67 EQAGGLVQCDKMLLRRRSR----------------DVIELSEQSAAQMRHVrgadMAMIFQEPMtslnpVFTVgeQIAES 130
Cdd:PTZ00265 1247 EQNVGMKNVNEFSLTKEGGsgedstvfknsgkillDGVDICDYNLKDLRNL----FSIVSQEPM-----LFNM--SIYEN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 131 IRL-HQNASREEAMVEAK-RMLDQV--RIP-EAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQA 205
Cdd:PTZ00265 1316 IKFgKEDATREDVKRACKfAAIDEFieSLPnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
250 260 270
....*....|....*....|....*....|....*.
gi 1134749654 206 QILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLV 241
Cdd:PTZ00265 1396 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
30-211 |
8.06e-11 |
|
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: 61.61 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKmllrrrsrDVIELSEQSAAQMRHVRGADMAMI 109
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRIL---AGLLRPDS--------GEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPmtSLNPVFTVGEQIAESIRLHQNASReeaMVEAkrMLDQVRIPEAQTILSrypHQLSGGMRQRVMIAMALSCRPAV 189
Cdd:TIGR01189 79 GHLP--GLKPELSALENLHFWAAIHGGAQR---TIED--ALAAVGLTGFEDLPA---AQLSAGQQRRLALARLWLSRRPL 148
|
170 180
....*....|....*....|..
gi 1134749654 190 LIADEPTTALDVTIQAQILQLI 211
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLL 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-260 |
9.52e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFMQDQQK-IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGG------------------ 71
Cdd:PTZ00265 379 DIKKIQFKNVRFHYDTRKdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdiiindshnlkdinlkww 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 72 -----LVQCDKMLLRRRSRDVIELS--------------------EQSAAQMRHVRGADMAMIFQEPMTSlnpvfTVGEQ 126
Cdd:PTZ00265 459 rskigVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndSQENKNKRNSCRAKCAGDLNDMSNT-----TDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 127 IAESIRLHQNASREEAMVEAKRML--DQVR-IPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVT 202
Cdd:PTZ00265 534 LIEMRKNYQTIKDSEVVDVSKKVLihDFVSaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 203 IQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGTVEQIFHAP 260
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-551 |
1.59e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTtgraLL----RLVESQGGEIIFNGQRIDTLSPG----KLQALRRDIQFIfqdpy 411
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKST----LLsmisRLLPPDSGEVLVDGLDVATTPSRelakRLAILRQENHIN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 412 asldPRqtigdsiiepLRVHGLL-----------PGKEAVARVAWLLERVGLLP-EHawRYPHEFSGGQRQRICIARALA 479
Cdd:COG4604 88 ----SR----------LTVRELVafgrfpyskgrLTAEDREIIDEAIAYLDLEDlAD--RYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
312-546 |
1.68e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 312 PVLRVRNLVTRfplrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQ------GGEIIFNG 385
Cdd:CHL00131 6 PILEIKNLHAS-----------VNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAGHpaykilEGDILFKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 386 QRIDTLSPGklQALRRDIQFIFQDPY------------ASLDPRQT-IGDSIIEPLRVHGLLPGKeavarvawlLERVGL 452
Cdd:CHL00131 71 ESILDLEPE--ERAHLGIFLAFQYPIeipgvsnadflrLAYNSKRKfQGLPELDPLEFLEIINEK---------LKLVGM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 453 LPEHAWRYPHE-FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI---INLLLDLQRdfgiAYLFISHDMAVVE 528
Cdd:CHL00131 140 DPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSEN----SIILITHYQRLLD 215
|
250
....*....|....*....
gi 1134749654 529 RIS-HRVAVMYLGQIVEIG 546
Cdd:CHL00131 216 YIKpDYVHVMQNGKIIKTG 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
288-553 |
2.90e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 288 PLISLEhpAKQAppIEQKTVVDGEpvlRVRNLVTR---------FPLRSGL--LNRVT---REVHAV-EKVSFDLWPGET 352
Cdd:PRK10790 297 PLIELT--TQQS--MLQQAVVAGE---RVFELMDGprqqygnddRPLQSGRidIDNVSfayRDDNLVlQNINLSVPSRGF 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPY---ASLDPRQTIGDSIIEplr 429
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDPVvlaDTFLANVTLGRDISE--- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 430 vhgllpgkEAVARVawlLERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDvSIR 499
Cdd:PRK10790 444 --------EQVWQA---LETVQLaelarsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANID-SGT 511
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 500 GQIINLLLDLQRDfgiaylfisHDMAVVerISHRVA---------VMYLGQIVEIGPRRAVFE 553
Cdd:PRK10790 512 EQAIQQALAAVRE---------HTTLVV--IAHRLStiveadtilVLHRGQAVEQGTHQQLLA 563
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-262 |
5.57e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLvqCDKMLLR-RRSRDVIELSEQSAAQMRHVRGADMAM 108
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKS----TLLKAL--AGDL--TGGGAPRgARVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 109 IFQEPMTSLNPvFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS---- 184
Cdd:PRK13547 87 VLPQAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 185 -----CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFhA 259
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-T 244
|
...
gi 1134749654 260 PQH 262
Cdd:PRK13547 245 PAH 247
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
248-286 |
6.78e-10 |
|
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: 55.10 E-value: 6.78e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1134749654 248 VETGTVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRR 286
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIP 39
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
138-256 |
8.06e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 138 SREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKE 217
Cdd:NF000106 117 SRKDARARADELLERFSLTEAA---GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110
....*....|....*....|....*....|....*....
gi 1134749654 218 MSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:NF000106 194 GAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-234 |
1.03e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRDVielseqsaAQMRHVRGADMAMIFQE 112
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKT----SLLRIL---AGLARPDAGEVLWQGEPI--------RRQRDEYHQDLLYLGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 PmtSLNPVFTVGEQIAESIRLHQNASrEEAMVEAkrmLDQVRipeaqtiLSRY---P-HQLSGGMRQRVMIAMALSCRPA 188
Cdd:PRK13538 83 P--GIKTELTALENLRFYQRLHGPGD-DEALWEA---LAQVG-------LAGFedvPvRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1134749654 189 VLIADEPTTALDVTIQAQILQLikvLQKEMSMG--VIFITH-DMGVVAE 234
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEAL---LAQHAEQGgmVILTTHqDLPVASD 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
337-547 |
1.29e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyASLDP 416
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK--EALENGISMVHQE--LNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIGDSIieplrvhgllpgkeavarvaWL--LERVGLLPEHAWRY---------------PHE----FSGGQRQRICIA 475
Cdd:PRK10982 87 QRSVMDNM--------------------WLgrYPTKGMFVDQDKMYrdtkaifdeldididPRAkvatLSVSQMQMIEIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 476 RALALNPKVIIADEAVSAL---DVSIRGQIINLLldlqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKL----KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQP 217
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
541-590 |
1.44e-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: 55.06 E-value: 1.44e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1134749654 541 QIVEIGPRRAVFENPQHPYTRKLLAAVpvaePSRQRPQRVLLSddLPSNI 590
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAI----PTIKKRDRKLIS--IPGEV 44
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
246-293 |
1.82e-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: 54.68 E-value: 1.82e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1134749654 246 EAVETGTVEQIFHAPQHPYTRALLAAVPQLGAmkgldypRRFPLISLE 293
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKK-------RDRKLISIP 41
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
41-246 |
2.18e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 41 RGETLAIVGESGSGKSVTALALMRLLEqagglvqcdkmllrRRSRDVIELSeqsaaqmrhvrgadmamifqepmtslnpv 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG--------------PPGGGVIYID----------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 121 ftvgeqiaesirlhqnasreeamveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
Cdd:smart00382 38 -------------------------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLD 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 201 VTIQAQILQLI-----KVLQKEMSMGVIFITHDMGVVAE-----IADRVLVMYQGE 246
Cdd:smart00382 93 AEQEALLLLLEelrllLLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLIL 148
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-252 |
2.56e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 14 AVENLNIAFMQDQqkiaavrnlsfslqrgeTLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRDVielsEQ 93
Cdd:TIGR01257 945 AVDRLNITFYENQ-----------------ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-------GKDI----ET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 94 SAAQMRHVRGadmaMIFQEpmtslNPVF---TVGEQIAESIRLhQNASREEAMVEAKRMLDQV-----RIPEAQtilsry 165
Cdd:TIGR01257 997 NLDAVRQSLG----MCPQH-----NILFhhlTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTglhhkRNEEAQ------ 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 166 phQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
Cdd:TIGR01257 1061 --DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
....*..
gi 1134749654 246 EAVETGT 252
Cdd:TIGR01257 1137 RLYCSGT 1143
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-254 |
3.12e-09 |
|
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: 57.15 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRL--LEQAGGLVQCDKmllrrrsRDVIELSEQSAAQMrhvrgaDMAMI 109
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG-------EDITDLPPEERARL------GIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 110 FQEPmtslnpvftvgeqiaesirlhqnasreeamveakrmldqVRIPEAQTI-LSRYPHQ-LSGGMRQRVMIAMALSCRP 187
Cdd:cd03217 83 FQYP---------------------------------------PEIPGVKNAdFLRYVNEgFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEI-ADRVLVMYQGEAVETGTVE 254
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
543-572 |
3.34e-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: 53.17 E-value: 3.34e-09
10 20 30
....*....|....*....|....*....|
gi 1134749654 543 VEIGPRRAVFENPQHPYTRKLLAAVPVAEP 572
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
349-497 |
3.43e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTTGRALLRLVESQG--GEIIFNGQRIDTlspgklQALRRdIQFIFQDP--YASLDPRQTIgdSI 424
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK------QILKR-TGFVTQDDilYPHLTVRETL--VF 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 425 IEPLRVHGLLPGKEAVARVAWLLERVGLLPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:PLN03211 164 CSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
11-227 |
3.61e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLniafmqdqqkiAAVR-------NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmLLRRR 83
Cdd:PRK13539 1 MMLEGEDL-----------ACVRggrvlfsGLSFTLAAGEALVLTGPNGSGKT----TLLRLI--AG--------LLPPA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 84 SRdvielseqsaaqmrHVRGADMAMIFQEPMTS---------LNPVFTVgeqiAESIRLHQN--ASREEAMVEAkrmLDQ 152
Cdd:PRK13539 56 AG--------------TIKLDGGDIDDPDVAEAchylghrnaMKPALTV----AENLEFWAAflGGEELDIAAA---LEA 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 153 VRIPEAQTILSRYphqLSGGMRQRVMIA-MALSCRPaVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITH 227
Cdd:PRK13539 115 VGLAPLAHLPFGY---LSAGQKRRVALArLLVSNRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATH 185
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-246 |
3.66e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.09 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQKIAAV-RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrsrdviels 91
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 92 eqsaaqmrhvrGADMAMIFQEPmtslnpvFTVGEQIAESIRLHQ--NASREEAMVEA-------KRM--LDQVRIPEAQT 160
Cdd:cd03250 65 -----------PGSIAYVSQEP-------WIQNGTIRENILFGKpfDEERYEKVIKAcalepdlEILpdGDLTEIGEKGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ilsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEMSMG--VIFITHDMGVVAEiADR 238
Cdd:cd03250 127 -------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFE--NCILGLLLNNktRILVTHQLQLLPH-ADQ 196
|
....*...
gi 1134749654 239 VLVMYQGE 246
Cdd:cd03250 197 IVVLDNGR 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-531 |
3.75e-09 |
|
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: 59.56 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-------------AGGLVQCDKMllrRRSRDVIELSEQSAAQMR 99
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDKdfngearpqpgikVGYLPQEPQL---DPTKTVRENVEEGVAEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 100 HV--RGADMAMIFQEPMTSLNPVFTVGEQIAESIRlHQNASREEAMVEakRMLDQVRIPEAQTILSRyphqLSGGMRQRV 177
Cdd:TIGR03719 98 DAldRFNEISAKYAEPDADFDKLAAEQAELQEIID-AADAWDLDSQLE--IAMDALRCPPWDADVTK----LSGGERRRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 178 MIAMALSCRPAVLIADEPTTALDVtiqAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE-----TGT 252
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQ-EYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPwegnySSW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 253 VEQ-------------------------IFHAP--QHPYTRALLAAVPQLGAMkglDYPRRFPLISLehpakQAPPIEQK 305
Cdd:TIGR03719 247 LEQkqkrleqeekeesarqktlkrelewVRQSPkgRQAKSKARLARYEELLSQ---EFQKRNETAEI-----YIPPGPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 306 tvvdGEPVLRVRNLVTRFPLRsgLLnrvtrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNg 385
Cdd:TIGR03719 319 ----GDKVIEAENLTKAFGDK--LL---------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 386 qriDTLSPGKLQALRrdiqfifqdpyASLDPRQTIGDSIIEPLRVhgLLPGKEAVARVAWL----------LERVGLLpe 455
Cdd:TIGR03719 383 ---ETVKLAYVDQSR-----------DALDPNKTVWEEISGGLDI--IKLGKREIPSRAYVgrfnfkgsdqQKKVGQL-- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 456 hawryphefSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLdlqrDFGIAYLFISHDMAVVERIS 531
Cdd:TIGR03719 445 ---------SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL----NFAGCAVVISHDRWFLDRIA 507
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
353-536 |
4.00e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 353 LSLVGESGSGKSTTgrallrlVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyasldprQTIGDSIIEPLRVHG 432
Cdd:PTZ00265 1258 FSLTKEGGSGEDST-------VFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEP-------MLFNMSIYENIKFGK 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 433 LLPGKEAVARV---AWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
Cdd:PTZ00265 1321 EDATREDVKRAckfAAIDEFIESLPNkydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
170 180 190
....*....|....*....|....*....|.
gi 1134749654 506 LLDLQRDFGIAYLFISHDMAVVERiSHRVAV 536
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
339-542 |
4.86e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQ--HNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 TIGDSIIeplrVHGLLPGK---EAVARVAWLLERVGLlpeHAWR--YPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:TIGR01257 1019 TVAEHIL----FYAQLKGRsweEAQLEMEAMLEDTGL---HHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1134749654 494 LDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
339-545 |
6.01e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.83 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDPYasldprq 418
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKLFSAVFTDFH------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 419 tigdsiiepLRVHGLLPGKEAV--ARVAWLLERVGL---LPEHAWRYPH-EFSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:PRK10522 408 ---------LFDQLLGPEGKPAnpALVEKWLERLKMahkLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEI 545
Cdd:PRK10522 479 DQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
316-503 |
6.38e-09 |
|
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: 57.56 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 316 VRNLVTRFplrsgllnrvTREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSpg 394
Cdd:cd03289 5 VKDLTAKY----------TEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 395 kLQALRRDIQ------FIFQDPY-ASLDPRQTIGDSiiEPLRVH---GL------LPGKeavarVAWLLERVGLLPEHaw 458
Cdd:cd03289 72 -LQKWRKAFGvipqkvFIFSGTFrKNLDPYGKWSDE--EIWKVAeevGLksvieqFPGQ-----LDFVLVDGGCVLSH-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1134749654 459 ryphefsgGQRQRICIARALALNPKVIIADEAVSALDvSIRGQII 503
Cdd:cd03289 142 --------GHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVI 177
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
42-251 |
6.38e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 42 GETLAIVGESGSGKSVtalalmrLLEQAGGLVQCD----KMLLRRRsrdviELSEQSAAQMRHVRGADMamifqepmtsL 117
Cdd:PLN03211 94 GEILAVLGPSGSGKST-------LLNALAGRIQGNnftgTILANNR-----KPTKQILKRTGFVTQDDI----------L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 118 NPVFTVGEQI--AESIRLHQNASREEAMVEAKRMLDQVRIP--EAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
Cdd:PLN03211 152 YPHLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
35-239 |
9.21e-09 |
|
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: 55.58 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmLLRRRSRDVIeLSEQSAAQMRHVRGADMAMIFQEPm 114
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKT----TLLRIL--AG--------LSPPLAGRVL-LNGGPLDFQRDSIARGLLYLGHAP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 tSLNPVFTVGEQIAESIRLHQNASREEAmveakrmLDQVRIPEAQTILSrypHQLSGGMRQRVMIAMALSCRPAVLIADE 194
Cdd:cd03231 83 -GIKTTLSVLENLRFWHADHSDEQVEEA-------LARVGLNGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1134749654 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-286 |
9.69e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRHVrgadMAMIFQEPM 114
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD----------CDVAKFGLTDLRRV----LSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 TSLNPVFTVGEQIAEsirlHQNASREEAMvEAKRMLDQVRIP----EAQtiLSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
Cdd:PLN03232 1321 LFSGTVRFNIDPFSE----HNDADLWEAL-ERAHIKDVIDRNpfglDAE--VSEGGENFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLA 270
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
250
....*....|....*..
gi 1134749654 271 AVPQLGA-MKGLDYPRR 286
Cdd:PLN03232 1471 TGPANAQyLSNLVFERR 1487
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-524 |
1.06e-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: 55.80 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDPY---ASLDPRQTIGdSII 425
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQKPWllnATVEENITFG-SPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 426 EPLRVhgllpgkEAVARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
Cdd:cd03290 106 NKQRY-------KAVTDACSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180
....*....|....*....|....
gi 1134749654 502 IINL-LLDLQRDFGIAYLFISHDM 524
Cdd:cd03290 179 LMQEgILKFLQDDKRTLVLVTHKL 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-556 |
1.17e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGgEIIFNGQRIDTLSPGKLqALRRDIQFIFQDPYASLDPRQTigd 422
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAEL-ARHRAYLSQQQTPPFAMPVFQY--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 siiepLRVHglLPGKEAVARVAWLL----ERVGLLPEHAwRYPHEFSGGQRQRICIARAL-----ALNP--KVIIADEAV 491
Cdd:PRK03695 90 -----LTLH--QPDKTRTEAVASALnevaEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 492 SALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
302-546 |
1.31e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 302 IEQKTVVDG-EPVLRVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSttgRALLRlVESQGGE 380
Cdd:NF000106 1 MTRKTISNGaRNAVEVRGLVKHFG-----------EVKAVDGVDLDVREGTVLGVLGP*GAA**---RGALP-AHV*GPD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 381 IIFNGQRIDTLSPGKlQALRRDI------QFIFQDPYASLDPRQTIGDSIIeplrvhglLPGKEAVARVAWLLERVGLlP 454
Cdd:NF000106 66 AGRRPWRF*TWCANR-RALRRTIg*hrpvR*GRRESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSL-T 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 455 EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRV 534
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHEL 214
|
250
....*....|..
gi 1134749654 535 AVMYLGQIVEIG 546
Cdd:NF000106 215 TVIDRGRVIADG 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
332-557 |
1.43e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 332 RVTREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVESQG-------GEIIFNGQRIDTLSPGKLQALRRD 402
Cdd:PRK13547 8 HVARRHRAIlRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 403 IqfifqdPYASLDPRQTIGDSIIEPLRV-HGLLPGKEAVA--RVAW-LLERVGLLPEHAwRYPHEFSGGQRQRICIARAL 478
Cdd:PRK13547 88 L------PQAAQPAFAFSAREIVLLGRYpHARRAGALTHRdgEIAWqALALAGATALVG-RDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 479 A---------LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
....*...
gi 1134749654 550 AVFEnPQH 557
Cdd:PRK13547 241 DVLT-PAH 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
343-516 |
1.54e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP-------GKLQALRrdiqfifqdpyASLd 415
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylGHRNAMK-----------PAL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 prqtigdSIIEPLRV-HGLLPGKEAVARVAwlLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
Cdd:PRK13539 89 -------TVAENLEFwAAFLGGEELDIAAA--LEAVGLAPlAH--LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|...
gi 1134749654 494 LDVSIRGQIINLLLDLQRDFGIA 516
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIV 180
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-261 |
1.60e-08 |
|
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: 55.88 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 38 SLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrDVIELSEQSAAQMRHVRgADMAMifqepmtsl 117
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG--------------DIEIELDTVSYKPQYIK-ADYEG--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 118 npvfTVGEQIAESIRLHQNASREEAMVEAKRMLDQvripeaqtILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEPT 196
Cdd:cd03237 77 ----TVRDLLSSITKDFYTHPYFKTEIAKPLQIEQ--------ILDREVPELSGGELQRVAIAACLS-KDAdIYLLDEPS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 197 TALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVmYQGEAVETGTVeqifHAPQ 261
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEPSVNGVA----NPPQ 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-532 |
2.96e-08 |
|
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: 52.84 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVesqggeiifNGQRIDTlsPGKLQalrrdiqfifqdpyasLDPRQTI 420
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKST----LLKLI---------AGELEPD--EGIVT----------------WGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GdsiieplrvhgllpgkeavarvawllervgllpehawrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
Cdd:cd03221 66 G--------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 1134749654 501 QIINLLldlqRDFGIAYLFISHDM----AVVERISH 532
Cdd:cd03221 108 ALEEAL----KEYPGTVILVSHDRyfldQVATKIIE 139
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
341-528 |
5.93e-08 |
|
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: 53.27 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRrdiqfifqdpYASLDPRQTI 420
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL----------YLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 421 GDSIIEPLRVHGLLPGKEAVARVawlLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEA---LARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....*....
gi 1134749654 500 GQIINLLLDLQRDFGIAYLFISHDMAVVE 528
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
328-503 |
6.04e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 328 GLLNRVTREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSpgkLQALRRDIQ-- 404
Cdd:TIGR01271 1222 GLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT---LQTWRKAFGvi 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 405 ----FIFQDPY-ASLDPRQTIGDsiieplrvhgllpgkEAVARVAwllERVGlLPEHAWRYPHE-----------FSGGQ 468
Cdd:TIGR01271 1298 pqkvFIFSGTFrKNLDPYEQWSD---------------EEIWKVA---EEVG-LKSVIEQFPDKldfvlvdggyvLSNGH 1358
|
170 180 190
....*....|....*....|....*....|....*
gi 1134749654 469 RQRICIARALALNPKVIIADEAVSALDvSIRGQII 503
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLD-PVTLQII 1392
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
350-536 |
6.09e-08 |
|
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: 53.95 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEII-------FNGQRIDTLSPGKLQALRRDIQFIF-QDPYASLDprqtig 421
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEieldtvsYKPQYIKADYEGTVRDLLSSITKDFyTHPYFKTE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 422 dsIIEPLRVHGLLpgkeavarvawllERvgLLPEhawrypheFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR-- 499
Cdd:cd03237 99 --IAKPLQIEQIL-------------DR--EVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlm 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1134749654 500 -GQIINLLLDLQRDfgiAYLFISHDMAVVERISHRVAV 536
Cdd:cd03237 154 aSKVIRRFAENNEK---TAFVVEHDIIMIDYLADRLIV 188
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
32-256 |
6.17e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.48 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRdvIELSEQSAAQMrhvrgadmamifq 111
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSGR--ISFSSQFSWIM------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 ePMTslnpvftvgeqIAESI--RLHQNASREEAMVEAKRML-DQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:cd03291 111 -PGT-----------IKENIifGVSYDEYRYKSVVKACQLEeDITKFPEKdNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQliKVLQKEMSMGV-IFITHDMGVVaEIADRVLVMYQGEAVETGTVEQI 256
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFE--SCVCKLMANKTrILVTSKMEHL-KKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-243 |
8.95e-08 |
|
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: 51.98 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 141 EAMVEAKRMLDQVRIPEAQTILSRYP--HQLSGGMRQRVMIAMAL---SCRPAVLIA-DEPTTALDVTIQAQILQLIKVL 214
Cdd:cd03227 48 AQSATRRRSGVKAGCIVAAVSAELIFtrLQLSGGEKELSALALILalaSLKPRPLYIlDEIDRGLDPRDGQALAEAILEH 127
|
90 100
....*....|....*....|....*....
gi 1134749654 215 QKEMSMgVIFITHDMGvVAEIADRVLVMY 243
Cdd:cd03227 128 LVKGAQ-VIVITHLPE-LAELADKLIHIK 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-246 |
1.66e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 161 ILSRYPHQLSGGMRQRVMIAMALScRPAVL-IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
Cdd:PRK13409 446 LLDKNVKDLSGGELQRVAIAACLS-RDADLyLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
....*..
gi 1134749654 240 LVmYQGE 246
Cdd:PRK13409 525 MV-FEGE 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-252 |
1.73e-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: 54.57 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRhvrgadmamiFQ 111
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----------LNIAKIGLHDLR----------FK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EPMTSLNPVFTVGeqiaeSIRLHQNASREEAMVEAKRMLDqvrIPEAQTILSRYP----HQ-------LSGGMRQRVMIA 180
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVWWALE---LAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEAVETGT 252
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT--VLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
344-587 |
1.77e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 344 SFDLWPGETLSLVGESGSGKSTTGRAL---LRLVEsqgGEIIFNGQRIDTLSPGKLQALRRDIqfiFQD---PYASLDP- 416
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALageLPLLS---GERQSQFSHITRLSFEQLQKLVSDE---WQRnntDMLSPGEd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 ------RQTIGDSIIEPLRVHGLlpgkEAVARVAWLLERvgllpehawRYPHeFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:PRK10938 97 dtgrttAEIIQDEVKDPARCEQL----AQQFGITALLDR---------RFKY-LSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN---PQHPYTRKLL-AA 566
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQalvAQLAHSEQLEgVQ 241
|
250 260
....*....|....*....|.
gi 1134749654 567 VPVAEPSRQRPQrvlLSDDLP 587
Cdd:PRK10938 242 LPEPDEPSARHA---LPANEP 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-256 |
2.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRHVRGadmaMIFQepm 114
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----------CDISKFGLMDLRKVLG----IIPQ--- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 115 tslNPVFTVGeqiaeSIRL-------HQNASREEAMvEAKRMLDQVRIP----EAQtiLSRYPHQLSGGMRQRVMIAMAL 183
Cdd:PLN03130 1321 ---APVLFSG-----TVRFnldpfneHNDADLWESL-ERAHLKDVIRRNslglDAE--VSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLVMYQGEAVETGTVEQI 256
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
336-543 |
4.09e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqaLRRDIQFIFQDpyASLD 415
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREAVAIVPEG--RRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 416 PRQTIGdsiiEPLRVHGLLPGKEAV-ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:PRK11614 93 SRMTVE----ENLAMGGFFAERDQFqERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1134749654 495 DVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
Cdd:PRK11614 169 APIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
341-541 |
4.78e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.57 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 341 EKVSFDLWPGETLSLVGESGSGKSTtgraLLR----LVESQGGEIIFNGQRIDTLSPgklqALRRDIQFIFQdpYASLDP 416
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTS----LLRilagLARPDAGEVLWQGEPIRRQRD----EYHQDLLYLGH--QPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 417 RQTIgdsiIEPLR----VHGllPGKEAVARVAwlLERVGLLP-EHAwryP-HEFSGGQRQRICIARALALNPKVIIADEA 490
Cdd:PRK13538 88 ELTA----LENLRfyqrLHG--PGDDEALWEA--LAQVGLAGfEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1134749654 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMavvERISHRVAVMYLGQ 541
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQDL---PVASDKVRKLRLGQ 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-255 |
5.14e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 36 SFSLQR------GETLAIVGESGSGKSvTALALMrlleqAGGLVqcdKMLLRRRS----RDVIELSEQSAAQ--MRHVRG 103
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKS-TALKIL-----AGKLK---PNLGKFDDppdwDEILDEFRGSELQnyFTKLLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 ADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMveaKRMldqvripEAQTILSRYPHQLSGGMRQRVMIAMAL 183
Cdd:cd03236 85 GDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELV---DQL-------ELRHVLDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYqGEAVETGTVEQ 255
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY-GEPGAYGVVTL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-261 |
5.73e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRDVielseqSAAQMRHVRgADMAMIFQ 111
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI-------RVNGREI------GAYGLRELR-RQFSMIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 EPMtslnpVFTvgeqiaESIRLHQNASREEAMVEAKRMLDQVRI-----PEAQTILSRYPH---QLSGGMRQRVMIAMAL 183
Cdd:PTZ00243 1392 DPV-----LFD------GTVRQNVDPFLEASSAEVWAALELVGLrervaSESEGIDSRVLEggsNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 184 SCRPAVLI-ADEPTT----ALDVTIQAqilqliKVLQKEMSMGVIFITHDMGVVAEIaDRVLVMYQGEAVETGTVEQIFH 258
Cdd:PTZ00243 1461 LKKGSGFIlMDEATAnidpALDRQIQA------TVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVM 1533
|
...
gi 1134749654 259 APQ 261
Cdd:PTZ00243 1534 NRQ 1536
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
290-553 |
5.78e-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: 53.03 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 290 ISLEHPAKQAPPIEQKTVVDGEPvlrvrNLVTrfpLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRA 369
Cdd:TIGR00957 612 IFLSHEELEPDSIERRTIKPGEG-----NSIT---VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 370 LLRLVESQGGEIIFNGQRIDTLSPGKLQ--ALRRDIQF--IFQDPYAsldpRQTIgdsiieplrvhgllpgkEAVArvaw 445
Cdd:TIGR00957 684 LLAEMDKVEGHVHMKGSVAYVPQQAWIQndSLRENILFgkALNEKYY----QQVL-----------------EACA---- 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 446 LLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDF-GIAYLFI 520
Cdd:TIGR00957 739 LLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILV 818
|
250 260 270
....*....|....*....|....*....|...
gi 1134749654 521 SHDMAVVERISHrVAVMYLGQIVEIGPRRAVFE 553
Cdd:TIGR00957 819 THGISYLPQVDV-IIVMSGGKISEMGSYQELLQ 850
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-240 |
6.35e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 11 NVLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQcdkmllrrrSRDVIEL 90
Cdd:PRK15064 318 NALEVENLTKGF--DNGPL--FKNLNLLLEAGERLAIIGENGVGKT----TLLRTL--VGELEP---------DSGTVKW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSA----AQmrhvrgaDMAMIFQEPMTslnpVFtvgeqiaESIRLHQNASREEAMVEAK--RML---DQVRIPeaqti 161
Cdd:PRK15064 379 SENANigyyAQ-------DHAYDFENDLT----LF-------DWMSQWRQEGDDEQAVRGTlgRLLfsqDDIKKS----- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 lsryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLikvlqkEMSMG-VIFITHDMGVVAEIADRV 239
Cdd:PRK15064 436 ----VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIESLNMAL------EKYEGtLIFVSHDREFVSSLATRI 505
|
.
gi 1134749654 240 L 240
Cdd:PRK15064 506 I 506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-262 |
6.76e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 25 DQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALmrlleqAGGLVQCDKMLLRRRSRDVIELSEQsaaqMRHVRGa 104
Cdd:TIGR00956 70 DTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTI------ASNTDGFHIGVEGVITYDGITPEEI----KKHYRG- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 105 DMAMIFQepmTSLN-PVFTVGEQIAESIRLH------QNASREEamvEAKRMLDQV------RIPEAQTILSRYPHQLSG 171
Cdd:TIGR00956 139 DVVYNAE---TDVHfPHLTVGETLDFAARCKtpqnrpDGVSREE---YAKHIADVYmatyglSHTRNTKVGNDFVRGVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 172 GMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSmgvifITHDMGVVA---------EIADRVLVM 242
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLD---SATALEFIRALKTSAN-----ILDTTPLVAiyqcsqdayELFDKVIVL 284
|
250 260
....*....|....*....|
gi 1134749654 243 YQGeavetgtvEQIFHAPQH 262
Cdd:TIGR00956 285 YEG--------YQIYFGPAD 296
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
158-523 |
7.48e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIAD 237
Cdd:PRK10636 139 SNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWL-KSYQGTLILISHDRDFLDPIVD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 238 RVLVMYQGEAVE-TGTV----------------------EQIFHApQHPYTRALLAAVPQLGAMKGLDYPRRFPLISleh 294
Cdd:PRK10636 215 KIIHIEQQSLFEyTGNYssfevqratrlaqqqamyesqqERVAHL-QSYIDRFRAKATKAKQAQSRIKMLERMELIA--- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 295 PAKQAPPIeqktvvdgepvlrvrnlvtRFPLRS--GLLNRVTRevhaVEKVS-------------FDLWPGETLSLVGES 359
Cdd:PRK10636 291 PAHVDNPF-------------------HFSFRApeSLPNPLLK----MEKVSagygdriildsikLNLVPGSRIGLLGRN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 360 GSGKSTTGRALLRLVESQGGEI-IFNGQRIDTLSPGKLQALRRD---IQFIfqdpyASLDPRQT-------------IGD 422
Cdd:PRK10636 348 GAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADespLQHL-----ARLAPQELeqklrdylggfgfQGD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 SIIEPLRvhgllpgkeavarvawllervgllpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
Cdd:PRK10636 423 KVTEETR---------------------------------RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
410 420
....*....|....*....|.
gi 1134749654 503 INLLLdlqrDFGIAYLFISHD 523
Cdd:PRK10636 470 TEALI----DFEGALVVVSHD 486
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
42-265 |
7.96e-07 |
|
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: 50.68 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 42 GETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrdvIELSEQSAAQMRhvrgADMAMIFQEPMTslnpvf 121
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG----------IDISKLPLHTLR----SRLSIILQDPIL------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 122 tvgeqIAESIRLHQNAsreEAMVEAKRMLDQVRIPEAQTILSRYPHQL-----------SGGMRQRVMIAMALSCRPAVL 190
Cdd:cd03288 107 -----FSGSIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 191 IADEPTTALDVTIQaQILQLIkVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGTVEQIFHAPQHPYT 265
Cdd:cd03288 179 IMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-256 |
8.16e-07 |
|
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: 52.61 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRdvIELSEQSAAQMrhvrgadmamifq 111
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------KHSGR--ISFSPQTSWIM------------- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 112 ePMTslnpvftvgeqIAESI--RLHQNASREEAMVEAKRM-LDQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
Cdd:TIGR01271 500 -PGT-----------IKDNIifGLSYDEYRYTSVIKACQLeEDIALFPEKdKTVLGEGGITLSGGQRARISLARAVYKDA 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 188 AVLIADEPTTALDVTIQAQILQliKVLQKEMSMGV-IFITHDMGVVAEiADRVLVMYQGEAVETGTVEQI 256
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFE--SCLCKLMSNKTrILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
169-251 |
9.90e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIA--MALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVM-- 242
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLH---QQDINQLLEVIKGLIDLGntVILIEHNLDVLSS-ADWIIDFgp 163
|
90
....*....|...
gi 1134749654 243 ----YQGEAVETG 251
Cdd:cd03238 164 gsgkSGGKVVFSG 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-257 |
1.06e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 10 GNVLAVENLNIAFMQDQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrdvie 89
Cdd:TIGR00957 634 GNSITVHNATFTWARDLP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---------------- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 lseqsaaqmrHVRGAdMAMIFQEPMT---SLNPVFTVGEQIAESirlhqnasREEAMVEAKRMLDQVRI-PEA-QTILSR 164
Cdd:TIGR00957 696 ----------HMKGS-VAYVPQQAWIqndSLRENILFGKALNEK--------YYQQVLEACALLPDLEIlPSGdRTEIGE 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQkemSMGV------IFITHDMGVVAEIaDR 238
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--HVIG---PEGVlknktrILVTHGISYLPQV-DV 830
|
250
....*....|....*....
gi 1134749654 239 VLVMYQGEAVETGTVEQIF 257
Cdd:TIGR00957 831 IIVMSGGKISEMGSYQELL 849
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
332-546 |
1.72e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 332 RVTREVHAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ--GGEIIFNGQRIDTLSP------GKLQALRRD 402
Cdd:PRK09580 8 HVSVEDKAILRgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPedrageGIFMAFQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 403 I-------QFIFQDPYASLdpRQTIGDSIIEPLRVHGLLPGKEAVARV-AWLLER---VGllpehawrypheFSGGQRQR 471
Cdd:PRK09580 88 VeipgvsnQFFLQTALNAV--RSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRsvnVG------------FSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 472 ICIARALALNPKVIIADEAVSALDV---SIRGQIINLLLDLQRDFGIaylfISHDMAVVERIS-HRVAVMYLGQIVEIG 546
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKRSFII----VTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-522 |
2.34e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRdiQFIFQDPYASLDPRQT 419
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQK--QLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIEPLRVHGLLPGKEAVARVAWLlervgllpEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDvSI 498
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLFSL--------EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-EL 161
|
170 180
....*....|....*....|....
gi 1134749654 499 RGQIINLLLDLQRDFGIAYLFISH 522
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
169-256 |
2.62e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.78 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVaEIADRVLVM- 242
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRLVDKGntVVVIEHNLDVI-KTADYIIDLg 905
|
90
....*....|....*....
gi 1134749654 243 -----YQGEAVETGTVEQI 256
Cdd:TIGR00630 906 peggdGGGTVVASGTPEEV 924
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-204 |
3.88e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 2 PH-SDELDAGNVLAVENLNIAFMQDQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlVQCDKMll 80
Cdd:TIGR01271 1206 PHaQKCWPSGGQMDVQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGV-- 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 81 rrrSRDVIELSEQSAAqmrhvrgadMAMIFQEpmtslnpVFTVGEQIAESIRLHQNASREEAMveakRMLDQVRIpeaQT 160
Cdd:TIGR01271 1281 ---SWNSVTLQTWRKA---------FGVIPQK-------VFIFSGTFRKNLDPYEQWSDEEIW----KVAEEVGL---KS 1334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 161 ILSRYPHQ-----------LSGGMRQRVMIAMALSCRPAVLIADEPTTALD-VTIQ 204
Cdd:TIGR01271 1335 VIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
162-240 |
4.11e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMAL---SCRPAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVaEIA 236
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHT---HDIKALIYVLQSLTHQGhtVVIIEHNMHVV-KVA 878
|
....
gi 1134749654 237 DRVL 240
Cdd:PRK00635 879 DYVL 882
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
343-506 |
4.26e-06 |
|
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: 48.03 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG---GEIIFNGQRIDtlspGKLQALRRDIQFIFQDP--YASLDPR 417
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYK----EFAEKYPGEIIYVSEEDvhFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIGDSiiepLRVHGllpgkEAVARVawllervgllpehawrypheFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
Cdd:cd03233 102 ETLDFA----LRCKG-----NEFVRG--------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
....*....
gi 1134749654 498 IRGQIINLL 506
Cdd:cd03233 153 TALEILKCI 161
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
353-435 |
4.69e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 46.18 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFngqrIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHG 432
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVF----VDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLLALA 83
|
...
gi 1134749654 433 LLP 435
Cdd:pfam13401 84 VAV 86
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
169-255 |
5.49e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYqGEAV 248
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEPG 150
|
....*..
gi 1134749654 249 ETGTVEQ 255
Cdd:cd03222 151 VYGIASQ 157
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
349-506 |
5.52e-06 |
|
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: 47.24 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTtgraLLRLV---ESQG---GEIIFNGQRIDtlspgklQALRRDIQFIFQDPyaSLDPRQTigd 422
Cdd:cd03232 32 PGTLTALMGESGAGKTT----LLDVLagrKTAGvitGEILINGRPLD-------KNFQRSTGYVEQQD--VHSPNLT--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 423 sIIEPLRVHGLLPGkeavarvawllervgllpehawrypheFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
Cdd:cd03232 96 -VREALRFSALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
....
gi 1134749654 503 INLL 506
Cdd:cd03232 148 VRFL 151
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-251 |
6.96e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqdqQKIAAVRNLSFSLQRGETLAIVGESGSGKSV--TALALMRLLEQAGGLVqcdkmllRRRSRDVIE 89
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlsATLAGREDYEVTGGTV-------EFKGKDLLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 LSEQSAAqmrhvrGADMAMIFQEPMTslnpVFTVGEQIAESIRLhqNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQL 169
Cdd:PRK09580 70 LSPEDRA------GEGIFMAFQYPVE----IPGVSNQFFLQTAL--NAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 170 ---------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIA-DRV 239
Cdd:PRK09580 138 ltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYV 216
|
250
....*....|..
gi 1134749654 240 LVMYQGEAVETG 251
Cdd:PRK09580 217 HVLYQGRIVKSG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
465-507 |
7.16e-06 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 47.08 E-value: 7.16e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1134749654 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCI 171
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-248 |
8.23e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.57 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRDVIELseQSAAQMRHvrgaDMA 107
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTT-------LLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMRE----AVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 108 MIFQepmtslnpvftvGEQIAESIRLHQN-------ASREEAMVEAKRMLDQvrIPEAQTILSRYPHQLSGGMRQRVMIA 180
Cdd:PRK11614 84 IVPE------------GRRVFSRMTVEENlamggffAERDQFQERIKWVYEL--FPRLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
349-536 |
1.13e-05 |
|
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: 45.83 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqrIDtlspgklqalrrdiqfifqdpyasldprqtiGDSIIEPL 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----ID-------------------------------GEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 429 rvhgllpgkeavarvawlleRVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII----- 503
Cdd:smart00382 46 --------------------LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 1134749654 504 NLLLDLQRDFGIAYLFISH------DMAVVERISHRVAV 536
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVL 144
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-204 |
1.25e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.16 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 13 LAVENLNIAFMQDQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlVQCDKMllrrrSRDVIELSE 92
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGV-----SWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 93 QSAAqmrhvrgadMAMIFQEpmtslnpVFTVGEQIAESIRLHQNASREEAMveakRMLDQVRIpeaQTILSRYPHQ---- 168
Cdd:cd03289 75 WRKA---------FGVIPQK-------VFIFSGTFRKNLDPYGKWSDEEIW----KVAEEVGL---KSVIEQFPGQldfv 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1134749654 169 -------LSGGMRQRVMIAMALSCRPAVLIADEPTTALD-VTIQ 204
Cdd:cd03289 132 lvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-538 |
1.99e-05 |
|
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: 46.59 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTTGRALlrlvesqGGEIIFNGQR----------IDTLSPGKLQ-----ALRRDIQFIFQDPYAS 413
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKfddppdwdeiLDEFRGSELQnyftkLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 414 LDPRQTIGdsiieplRVHGLLPGKEAVARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:cd03236 98 LIPKAVKG-------KVGELLKKKDERGKLDELVDQLEL--RHVLdRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1134749654 493 ALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMY 538
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
169-240 |
2.03e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 2.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVAeIADRVL 240
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHF---HDVKKLLEVLQRLVDKGntVVVIEHNLDVIK-CADWII 242
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
33-253 |
2.13e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSVTALALM------RLLEQAGglvqcdkMLLRRRsrdvieLSEQSAAQMRHVRGADM 106
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqrRYVESLS-------AYARQF------LGQMDKPDVDSIEGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 107 AMIFQEPMTSLNPVFTVGE--QIAESIRLHqnASReEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAMALS 184
Cdd:cd03270 79 AIAIDQKTTSRNPRSTVGTvtEIYDYLRLL--FAR-VGIRERLGFLVDVGLGYLT--LSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 185 CR-PAVL-IADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHDMGVVaEIADRVLVMYQGEAVETGTV 253
Cdd:cd03270 154 SGlTGVLyVLDEPSIGLH---PRDNDRLIETLKRLRDLGntVLVVEHDEDTI-RAADHVIDIGPGAGVHGGEI 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
343-411 |
2.69e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 2.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDPY 411
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQLFSAVFSDFH 416
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
169-256 |
3.62e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRP---AVLIADEPTTALDVtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVaEIADRVLVM- 242
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHF---EDIRKLLEVLHRLVDKGntVVVIEHNLDVI-KTADWIIDLg 906
|
90
....*....|....*....
gi 1134749654 243 -----YQGEAVETGTVEQI 256
Cdd:PRK00349 907 peggdGGGEIVATGTPEEV 925
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
157-228 |
5.21e-05 |
|
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: 44.52 E-value: 5.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749654 157 EAQTILSRYPHQLSGGMRQ------RVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLIKVLQKEMSMGVIFITHD 228
Cdd:cd03240 104 ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
349-538 |
6.72e-05 |
|
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: 45.93 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 349 PGETLSLVGESGSGKSTTGRALlrlvesqGGEIIFNGQRIDTlSPGKLQALRR----DIQFIFQDPY-----ASLDPrQT 419
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIL-------SGELKPNLGDYDE-EPSWDEVLKRfrgtELQDYFKKLAngeikVAHKP-QY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IgDSIiePLRVHG----LLPGKEAVARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
Cdd:COG1245 169 V-DLI--PKVFKGtvreLLEKVDERGKLDELAEKLGL--ENILdRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1134749654 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMY 538
Cdd:COG1245 244 DIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
162-365 |
7.12e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQLSGGMRQRVMIAMAL-SCRPAVL-IADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiAD 237
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLH---QRDNRRLINTLKRLRDLGntLIVVEHDEDTIRA-AD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 238 RVLVM------YQGEAVETGTVEQIFhAPQHPYTRALLAavpqlGAMKgldyprrfplisLEHPAKQAPPIEQKTVVDGE 311
Cdd:TIGR00630 558 YVIDIgpgageHGGEVVASGTPEEIL-ANPDSLTGQYLS-----GRKK------------IEVPAERRPGNGKFLTLKGA 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 312 PVLRVRNLVTRFPLrsGLLNRVTrevhavekvsfdlwpgetlslvGESGSGKST 365
Cdd:TIGR00630 620 RENNLKNITVSIPL--GLFTCIT----------------------GVSGSGKST 649
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
336-504 |
1.20e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL-RLVESQGGEIIFNGQridtlspgklQALRRDIQFIFQdpyasl 414
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVIRGT----------VAYVPQVSWIFN------ 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 dprQTIGDSII-----EPLRVhgllpgkEAVARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVI 485
Cdd:PLN03130 693 ---ATVRDNILfgspfDPERY-------ERAIDVTALQHDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVY 762
|
170
....*....|....*....
gi 1134749654 486 IADEAVSALDVSIRGQIIN 504
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFD 781
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
338-546 |
1.44e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 338 HAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVesqGGEIIFNGQRIDTLSPGKLQALRrdiqfifqdpyASLDPR 417
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKST----LSNLI---AGVTMPNKGTVDIKGSAALIAIS-----------SGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 418 QTIgdsiIEPLRVHGLLPG--KEAVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
Cdd:PRK13545 100 LTG----IENIELKGLMMGltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1134749654 496 VSirgqIINLLLDLQRDF---GIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
Cdd:PRK13545 176 QT----FTKKCLDKMNEFkeqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
303-548 |
1.60e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 303 EQKTVVDGEPVLRVRNLVTRFPLRSGLLNRVTREVHAVEKvsfdlwPGETLSLVGESGSGKSTtgraLLRLVESQ----- 377
Cdd:TIGR00956 46 YQPTFPNALLKILTRGFRKLKKFRDTKTFDILKPMDGLIK------PGELTVVLGRPGSGCST----LLKTIASNtdgfh 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 378 ---GGEIIFNGQRIDTLSPGKlqalRRDIQFIfqdpyASLD---PRQTIGDSIIEPLRVHG------LLPGKEAVARVAW 445
Cdd:TIGR00956 116 igvEGVITYDGITPEEIKKHY----RGDVVYN-----AETDvhfPHLTVGETLDFAARCKTpqnrpdGVSREEYAKHIAD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 446 LLERV-GLLPEHAWRYPHEF----SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfgiaylfI 520
Cdd:TIGR00956 187 VYMATyGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAN--------I 258
|
250 260 270
....*....|....*....|....*....|....*..
gi 1134749654 521 SHDMAVVE---------RISHRVAVMYLGQIVEIGPR 548
Cdd:TIGR00956 259 LDTTPLVAiyqcsqdayELFDKVIVLYEGYQIYFGPA 295
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-228 |
1.67e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 12 VLAVENLNIAFmqDQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLlrrrsrDVIEL 90
Cdd:PRK11147 319 VFEMENVNYQI--DGKQL--VKDFSAQVQRGDKIALIGPNGCGKT-TLLKLMlGQLQADSGRIHCGTKL------EVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 91 SEQSAAqmrhvrgadmamifqepmtsLNPVFTVGEQIAEsirlhqnaSREEAMVEA----------------KRMLDQVR 154
Cdd:PRK11147 388 DQHRAE--------------------LDPEKTVMDNLAE--------GKQEVMVNGrprhvlgylqdflfhpKRAMTPVK 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749654 155 ipeaqtilsryphQLSGGMRQRVMIAmALSCRPA-VLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHD 228
Cdd:PRK11147 440 -------------ALSGGERNRLLLA-RLFLKPSnLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-205 |
1.69e-04 |
|
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: 44.54 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 10 GNVLAVENLNIAFmQDQQKIaavRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLLEqagGLVQCDKMLLRrrSRDVIE 89
Cdd:TIGR03719 320 DKVIEAENLTKAF-GDKLLI---DDLSFKLPPGGIVGVIGPNGAGKST----LFRMIT---GQEQPDSGTIE--IGETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 90 LSeqSAAQMRhvrgadmamifqepmTSLNPVFTVGEQIAESirlhqnasreeamveakrmLDQVRIPEAQtILSR----- 164
Cdd:TIGR03719 387 LA--YVDQSR---------------DALDPNKTVWEEISGG-------------------LDIIKLGKRE-IPSRayvgr 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1134749654 165 ----------YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQA 205
Cdd:TIGR03719 430 fnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
169-258 |
2.00e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEMSMGV-IFITHDMGVVAEIaDRVLVMYQGEA 247
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELRGKTrVLVTNQLHFLSQV-DRIILVHEGMI 817
|
90
....*....|.
gi 1134749654 248 VETGTVEQIFH 258
Cdd:PLN03130 818 KEEGTYEELSN 828
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
439-496 |
2.19e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 2.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749654 439 AVARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
446-538 |
2.26e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 446 LLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDM 524
Cdd:PRK13409 196 VVERLGL--ENILdRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
90
....*....|....
gi 1134749654 525 AVVERISHRVAVMY 538
Cdd:PRK13409 272 AVLDYLADNVHIAY 285
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-268 |
3.76e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 33 RNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLLRRRSRDVIELSEQsaaqmrHVRGADMAmifQE 112
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKS-TILKLI-----SGELQPSSGTVFRSAKVRMAVFSQH------HVDGLDLS---SN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 113 PMTSLNPVFT-VGEQiaeSIRLHQNASREEAMVEAKRMldqvripeaqtilsrypHQLSGGMRQRVMIAMALSCRPAVLI 191
Cdd:PLN03073 591 PLLYMMRCFPgVPEQ---KLRAHLGSFGVTGNLALQPM-----------------YTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749654 192 ADEPTTALDVTIQAQILQLIKVLQKemsmGVIFITHDMGVVAEIADRVLVMYQGEAVEtgtveqiFHAPQHPYTRAL 268
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKVTP-------FHGTFHDYKKTL 716
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
162-256 |
3.98e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.85 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 162 LSRYPHQL----SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIAD 237
Cdd:TIGR01257 2060 LSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCT 2138
|
90
....*....|....*....
gi 1134749654 238 RVLVMYQGEAVETGTVEQI 256
Cdd:TIGR01257 2139 RLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-256 |
4.65e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE----QA---GGLVQCDKMLLRRRsrdVIELSeQSaaqmrhvrg 103
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPasegEAwlfGQPVDAGDIATRRR---VGYMS-QA--------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 104 admamiFqepmtSLNPVFTVGEQIAESIRL-HQNASREEAMVEAkrMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMA 182
Cdd:NF033858 348 ------F-----SLYGELTVRQNLELHARLfHLPAAEIAARVAE--MLERFDLADVADAL---PDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmsMGV-IFI-THDMGvVAEIADRVLVMYQGEAVETGTVEQI 256
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSRE--DGVtIFIsTHFMN-EAERCDRISLMHAGRVLASDTPAAL 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
465-504 |
6.17e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 6.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1134749654 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
169-256 |
6.49e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCR---PAVLIADEPTTAL---DvtiqaqILQLIKVLQKEMSMG--VIFITHDMGVVAeIADRVL 240
Cdd:COG0178 827 LSGGEAQRVKLASELSKRstgKTLYILDEPTTGLhfhD------IRKLLEVLHRLVDKGntVVVIEHNLDVIK-TADWII 899
|
90 100
....*....|....*....|..
gi 1134749654 241 VM------YQGEAVETGTVEQI 256
Cdd:COG0178 900 DLgpeggdGGGEIVAEGTPEEV 921
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
166-233 |
8.49e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 8.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134749654 166 PHQLSGGMRQrvMIAMALSC-----RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDMGVVA 233
Cdd:pfam13304 234 AFELSDGTKR--LLALLAALlsalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGA-QLILTTHSPLLLD 303
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
336-548 |
1.02e-03 |
|
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: 40.38 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 336 EVHAVEKVSFDLwPGETLSLV-GESGSGKSTtgrallrlvesqggeIIFngqriDTLSPGKLQALRRDIQFIFQDPYASL 414
Cdd:cd03238 7 NVHNLQNLDVSI-PLNVLVVVtGVSGSGKST---------------LVN-----EGLYASGKARLISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 415 DPRQTIGDSIIEPLRvhgllPGKEAvarvawllervgllpehawrypHEFSGGQRQRICIARALALNPK--VIIADEAVS 492
Cdd:cd03238 66 DQLQFLIDVGLGYLT-----LGQKL----------------------STLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749654 493 ALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHrvavmylgqIVEIGPR 548
Cdd:cd03238 119 GLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADW---------IIDFGPG 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-502 |
1.22e-03 |
|
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: 42.20 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqRIdTLSPgklqalrrdiQFIFQDPyasldprQT 419
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RI-SFSP----------QTSWIMP-------GT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 420 IGDSIIeplrvHGLLPGK---EAVARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVS 492
Cdd:TIGR01271 503 IKDNII-----FGLSYDEyryTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|
gi 1134749654 493 ALDVSIRGQI 502
Cdd:TIGR01271 578 HLDVVTEKEI 587
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-212 |
1.76e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 23 MQDQ----QKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalaLMRLL--EQAGGLVQCDkmllrrrsrdvIELSEQSAA 96
Cdd:PLN03140 883 MKEQgvteDRLQLLREVTGAFRPGVLTALMGVSGAGKTT----LMDVLagRKTGGYIEGD-----------IRISGFPKK 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 97 QMRHVRGADmamiFQEPMTSLNPVFTVGEQIAES--IRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYP--HQLSGG 172
Cdd:PLN03140 948 QETFARISG----YCEQNDIHSPQVTVRESLIYSafLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTE 1023
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1134749654 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK 212
Cdd:PLN03140 1024 QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
337-547 |
3.50e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 337 VHAVEKVSFDLWPGETLSLVGESGSGKST--------TGRalLRLVESQGGEI-IFNGQ-------RIDTLSPgklqALR 400
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaEGQ--RRYVESLSAYArQFLGQmdkpdvdSIEGLSP----AIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 401 RDIQFIfqdpyaSLDPRQTIGdSIIEPLRVHGLLPGKEA-VARVAWLLErVGLLPEHAWRYPHEFSGGQRQRICIARAL- 478
Cdd:cd03270 82 IDQKTT------SRNPRSTVG-TVTEIYDYLRLLFARVGiRERLGFLVD-VGLGYLTLSRSAPTLSGGEAQRIRLATQIg 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 479 -ALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHrvavmylgqIVEIGP 547
Cdd:cd03270 154 sGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADH---------VIDIGP 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
169-257 |
4.19e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEMSMGV-IFITHDMGVVAEIaDRVLVMYQGEA 247
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD--SCMKDELKGKTrVLVTNQLHFLPLM-DRIILVSEGMI 817
|
90
....*....|
gi 1134749654 248 VETGTVEQIF 257
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
445-538 |
5.29e-03 |
|
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: 38.32 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749654 445 WLLERVGLLPEHAwryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
Cdd:cd03222 58 WDGITPVYKPQYI-----DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
90
....*....|....
gi 1134749654 525 AVVERISHRVAVMY 538
Cdd:cd03222 133 AVLDYLSDRIHVFE 146
|
|
| |
