|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-552 |
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: 869.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIELGGTDLNDL 82
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQ 162
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 163 KQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADA 242
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 243 RTFFERPRHPYARELFEAIPTFAKRgrplsaqgraadqgkAAPEAGAVVLDVQDLLVHYPVRKGVLRRVAAWVEAVNGVT 322
Cdd:COG4172 242 AELFAAPQHPYTRKLLAAEPRGDPR---------------PVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 323 FTLRAGETLALLGESGCGKTTTGKALLRLVEGarvQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPFASLDPRMRVGD 402
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALLRLIPS---EGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 403 ILEEGIASLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQ 482
Cdd:COG4172 384 IIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 483 ILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRLR 552
Cdd:COG4172 464 ILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-552 |
0e+00 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 629.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDVAGesGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIvGGQIELGGTDLNDLSE 84
Cdd:COG1123 2 TPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 85 RamrgVRGGRIGIIFQEPATSLNPVmRVGDQIVETLAAHTpLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQ 164
Cdd:COG1123 79 A----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLG-LSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 165 RLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADART 244
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 245 FFERPRhpyareLFEAIPTFAKRGRPLSAqgraadqgkaAPEAGAVVLDVQDLLVHYPVRKGvlrrvaAWVEAVNGVTFT 324
Cdd:COG1123 230 ILAAPQ------ALAAVPRLGAARGRAAP----------AAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 325 LRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPFASLDPRMRVGDIL 404
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGLLR--PTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDII 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 405 EEGIASLRpELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQIL 484
Cdd:COG1123 366 AEPLRLHG-LLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 485 DLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRLR 552
Cdd:COG1123 445 NLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLD 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-546 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 540.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRI-VGGQIELGGTDLND 81
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 82 LSERAMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGG 161
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESAD 241
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 242 ARTFFERPRHPYARELFEAIPTfakrGRPLsaqgraadqgkAAPEAGAVVLDVQDLLVHYPVRKGVLRRVAAWVEAVNGV 321
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPS----GDPV-----------PLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 322 TFTLRAGETLALLGESGCGKTTTGKALLRLVegaRVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPFASLDPRMRVG 401
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSTTGLALLRLI---NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 402 DILEEGIASLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQA 481
Cdd:PRK15134 383 QIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 482 QILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLA 546
Cdd:PRK15134 463 QILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-549 |
2.69e-169 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 493.99 E-value: 2.69e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrivgGQIELGG---------- 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAG----GLVQCDKmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 77 TDLNDLSERAMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPF 156
Cdd:PRK10261 88 IELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 237 VESADARTFFERPRHPYARELFEAIPTFAK-------RGRPLSAQGRAADQGKAAPE----AGAVVLDVQDLLVHYPVRK 305
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVPQLGAmkgldypRRFPLISLEHPAKQEPPIEQdtvvDGEPILQVRNLVTRFPLRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 306 GVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRLRQDIQI 385
Cdd:PRK10261 328 GLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ--GGEIIFNGQRIDTLSPGKLQALRRDIQF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 386 VFQDPFASLDPRMRVGDILEEGIaSLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKV 465
Cdd:PRK10261 406 IFQDPYASLDPRQTVGDSIMEPL-RVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLL 545
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
....
gi 490704625 546 AAVP 549
Cdd:PRK10261 565 AAVP 568
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-273 |
8.50e-141 |
|
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: 409.83 E-value: 8.50e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrIVGGQIELGGTDLNDLSERA 86
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRL 166
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260
....*....|....*....|....*..
gi 490704625 247 ERPRHPYARELFEAIPTFAKRGRPLSA 273
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIP 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
285-551 |
5.61e-136 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 397.95 E-value: 5.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 285 PEAGAVVLDVQDLLVHYPVRKGVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLD 364
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PTSGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 365 GHDLLGASRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEE-----GIASlRPELAASARRaravgLLERVGLPADTPT 439
Cdd:COG4608 79 GQDITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEplrihGLAS-KAERRERVAE-----LLELVGLRPEHAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 440 RYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMH 519
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260 270
....*....|....*....|....*....|..
gi 490704625 520 GGRIVEMGPADTVLHAPRHEMTQRLLAAVPRL 551
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSAVPVP 264
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
291-552 |
1.77e-128 |
|
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: 378.24 E-value: 1.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGVLRrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE-GARVQGRAMLDGHDLL 369
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPpPGITSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 370 GASRRELRRLR-QDIQIVFQDPFASLDPRMRVGDILEEGIASLRPeLAASARRARAVGLLERVGL--PADTPTRYPHEFS 446
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLpdPERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 447 GGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEM 526
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260
....*....|....*....|....*.
gi 490704625 527 GPADTVLHAPRHEMTQRLLAAVPRLR 552
Cdd:COG0444 233 GPVEELFENPRHPYTRALLSSIPRLD 258
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
291-527 |
7.56e-112 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 332.16 E-value: 7.56e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGvlrrvaaWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLveGARVQGRAMLDGHDLLG 370
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL--LKPTSGSIIFDGKDLLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIASLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQR 450
Cdd:cd03257 72 LSRRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 451 QRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
287-551 |
7.20e-106 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 320.76 E-value: 7.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 287 AGAVVLDVQDLLVHYPVRKGVLRRvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKaLLRLVEgARVQGRAMLDGH 366
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKP-ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLAR-LLTMIE-TPTGGELYYQGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 367 DLLGASRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIAsLRPELAASARRARAVGLLERVGLPADTPTRYPHEFS 446
Cdd:PRK11308 78 DLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLL-INTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 447 GGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEM 526
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK 236
|
250 260
....*....|....*....|....*
gi 490704625 527 GPADTVLHAPRHEMTQRLLAAVPRL 551
Cdd:PRK11308 237 GTKEQIFNNPRHPYTQALLSATPRL 261
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-240 |
5.70e-100 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 301.73 E-value: 5.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLNDLSERa 86
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDwLRRVGIPEPERRIDDYPFQFSGGQKQRL 166
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVL-LLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESA 240
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
290-549 |
9.90e-98 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 300.08 E-value: 9.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 290 VVLDVQDLLVHYPVRKGvlrrvAAW-------VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAM 362
Cdd:PRK15079 7 VLLEVADLKVHFDIKDG-----KQWfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT--DGEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 363 LDGHDLLGASRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIASLRPELAASARRARAVGLLERVGLPADTPTRYP 442
Cdd:PRK15079 80 WLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 443 HEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGR 522
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260
....*....|....*....|....*..
gi 490704625 523 IVEMGPADTVLHAPRHEMTQRLLAAVP 549
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
292-552 |
9.36e-97 |
|
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: 294.40 E-value: 9.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRKGvlrrvaaWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlga 371
Cdd:COG1124 2 LEVRNLSVSYGQGGR-------RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW--SGEVTFDGRPV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIASLRpelaASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQ 451
Cdd:COG1124 70 TRRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG----LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADT 531
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
250 260
....*....|....*....|.
gi 490704625 532 VLHAPRHEMTQRLLAAVPRLR 552
Cdd:COG1124 226 LLAGPKHPYTRELLAASLAFE 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-262 |
4.88e-91 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 282.78 E-value: 4.88e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVD-------VAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVggqi 72
Cdd:COG4608 1 AAMAEPLLEVRDLKKHfpvrgglFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEIL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 73 eLGGTDLNDLSERAMRGVRGgRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPePERrID 152
Cdd:COG4608 77 -FDGQDITGLSGRELRPLRR-RMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PEH-AD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMR 232
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260 270
....*....|....*....|....*....|
gi 490704625 233 GGEIVESADARTFFERPRHPYARELFEAIP 262
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSAVP 262
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-265 |
2.16e-88 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 275.85 E-value: 2.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIELGGTDLNDLSERA 86
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRL 166
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250
....*....|....*....
gi 490704625 247 ERPRHPYARELFEAIPTFA 265
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFA 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-262 |
2.91e-88 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 275.45 E-value: 2.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIvGGQIELGGTDLN 80
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI-GGSATFNGREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 DLSERAMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSG 160
Cdd:PRK09473 85 NLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESA 240
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
250 260
....*....|....*....|..
gi 490704625 241 DARTFFERPRHPYARELFEAIP 262
Cdd:PRK09473 245 NARDVFYQPSHPYSIGLLNAVP 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-267 |
2.67e-77 |
|
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: 244.33 E-value: 2.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrivgGQIELGGTDLNDLSERA 86
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS----GEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGvrggRIGIIFQEPATSLNPVMRVGDQIVETLAAHtplRGAAARERAIDWLRRVGIPEPERriDDYPFQFSGGQKQRL 166
Cdd:COG1124 77 FRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPPSFL--DRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 490704625 247 ERPRHPYARELFEAIPTFAKR 267
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-264 |
5.66e-75 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 240.96 E-value: 5.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIELGGTDLNDLSER 85
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTpLRG------AAARERAIDWLRRVGIPEPERRIDDYPFQFS 159
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWT-FKGkwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 160 GGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260
....*....|....*....|....*
gi 490704625 240 ADARTFFERPRHPYARELFEAIPTF 264
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDF 265
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
290-558 |
5.71e-75 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 241.17 E-value: 5.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 290 VVLDVQDLLVHYPVRKGVlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEG-ARVQGRAMLDGHDL 368
Cdd:PRK09473 11 ALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAnGRIGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 LGASRRELRRLR-QDIQIVFQDPFASLDPRMRVGDILEEgIASLRPELAASARRARAVGLLERVGLPADTP--TRYPHEF 445
Cdd:PRK09473 84 LNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLME-VLMLHKGMSKAEAFEESVRMLDAVKMPEARKrmKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260 270
....*....|....*....|....*....|...
gi 490704625 526 MGPADTVLHAPRHEMTQRLLAAVPRLrfGAENE 558
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRL--DAEGE 273
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
292-547 |
1.64e-74 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 237.43 E-value: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRKGVLRRVAawVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLlga 371
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFRRQQ--FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIE--PTSGEILINGHKL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIaSLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQ 451
Cdd:COG4167 78 EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPL-RLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADT 531
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*.
gi 490704625 532 VLHAPRHEMTQRLLAA 547
Cdd:COG4167 237 VFANPQHEVTKRLIES 252
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-260 |
1.28e-73 |
|
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: 234.19 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIELGGTDLNDLSeramrgVRGGRIGIIFQEPATS 105
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 186 TALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARELFEA 260
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
292-550 |
3.89e-64 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 218.42 E-value: 3.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPvRKGVLRRVaawveaVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARV---QGRAMLDGHDL 368
Cdd:PRK15134 6 LAIENLSVAFR-QQQTVRTV------VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVvypSGDIRFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 LGASRRELRRLRQD-IQIVFQDPFASLDPRMRVGDILEEgIASLRPELAASARRARAVGLLERVGL--PADTPTRYPHEF 445
Cdd:PRK15134 79 LHASEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYE-VLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|....*
gi 490704625 526 MGPADTVLHAPRHEMTQRLLAAVPR 550
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-262 |
3.97e-64 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 212.64 E-value: 3.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEPATS 105
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVGDQIVETLAAHTP-LRGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEP 184
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTYHPkLSRQEVKDRVKAMMLKVGLLP--NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 185 TTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARELFEAIP 262
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
291-548 |
3.72e-63 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 208.12 E-value: 3.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYpvRKGVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLG 370
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA--QGTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIASLRpELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQR 450
Cdd:TIGR02769 78 LDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLT-SLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 451 QRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAd 530
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV- 235
|
250
....*....|....*...
gi 490704625 531 TVLHAPRHEMTQRLLAAV 548
Cdd:TIGR02769 236 AQLLSFKHPAGRNLQSAV 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-262 |
4.41e-63 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 209.82 E-value: 4.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEPAT 104
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKS----TLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQ-KIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGI-PEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:PRK11308 104 SLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARELFEAIP 262
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATP 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-260 |
1.43e-60 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 200.70 E-value: 1.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGEsgvthAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIELGGTDLndlserAM 87
Cdd:PRK10418 5 IELRNIALQAAQP-----LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPV------AP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 RGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAhtpLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRLM 167
Cdd:PRK10418 74 CALRGRKIATIMQNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 168 IAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFE 247
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250
....*....|...
gi 490704625 248 RPRHPYARELFEA 260
Cdd:PRK10418 231 APKHAVTRSLVSA 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
294-556 |
1.40e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.07 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 294 VQDLLVHYPVRKGVlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGA 371
Cdd:COG1135 4 LENLSKTFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLLERptSGSVLVDGVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLRQDIQIVFQDpFASLDPRMRVGDI---LEegIASLRPElaasaRRARAVG-LLERVGLpADTPTRYPHEFSG 447
Cdd:COG1135 73 SERELRAARRKIGMIFQH-FNLLSSRTVAENValpLE--IAGVPKA-----EIRKRVAeLLELVGL-SDKADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 448 GQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
250 260
....*....|....*....|....*....
gi 490704625 528 PADTVLHAPRHEMTQRLLAAVPRLRFGAE 556
Cdd:COG1135 224 PVLDVFANPQSELTRRFLPTVLNDELPEE 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-276 |
6.43e-59 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 198.87 E-value: 6.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIELGGTDLNDLSER 85
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTP-----LRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSG 160
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYkgrwwQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESA 240
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 490704625 241 DARTFFERPRHPYARELFEAIPTFakrGRPLSAQGR 276
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIPDF---GSAMPHKSR 274
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-558 |
7.29e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 196.83 E-value: 7.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYpvRKGVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGA 371
Cdd:PRK10419 4 LNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS--QGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIASLRpELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQ 451
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLL-SLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVE---MGP 528
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGD 238
|
250 260 270
....*....|....*....|....*....|
gi 490704625 529 ADTVLHAPRHEMTQRLLAAVPRLRFGAENE 558
Cdd:PRK10419 239 KLTFSSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
291-547 |
6.38e-58 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 194.24 E-value: 6.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGVLRRvaAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlg 370
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT--SGELLIDDHPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 aSRRELRRLRQDIQIVFQDPFASLDPRMRVGDILEEGIaSLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQR 450
Cdd:PRK15112 78 -HFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPL-RLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 451 QRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*..
gi 490704625 531 TVLHAPRHEMTQRLLAA 547
Cdd:PRK15112 236 DVLASPLHELTKRLIAG 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-265 |
5.75e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 194.14 E-value: 5.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGRIVggqieLGGTDLNDL 82
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-T---LIRCInllerPTSGSVL-----VDGVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAMRGVRGgRIGIIFQepatSLNPVMR--VGDQIvetlaAHtPLR-----GAAARERAIDWLRRVGIpepERRIDDYP 155
Cdd:COG1135 73 SERELRAARR-KIGMIFQ----HFNLLSSrtVAENV-----AL-PLEiagvpKAEIRKRVAELLELVGL---SDKADAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 156 FQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
250 260 270
....*....|....*....|....*....|
gi 490704625 236 IVESADARTFFERPRHPYARELFEAIPTFA 265
Cdd:COG1135 219 IVEQGPVLDVFANPQSELTRRFLPTVLNDE 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
315-551 |
1.08e-55 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 197.77 E-value: 1.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE--GARVQGRAMLDGH------DLLGASRRELRRLR-QDIQI 385
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqaGGLVQCDKMLLRRrsrqviELSEQSAAQMRHVRgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 386 VFQDPFASLDPRMRVGDILEEGIaSLRPELAASARRARAVGLLERVGLPADTP--TRYPHEFSGGQRQRIAIARALAVEP 463
Cdd:PRK10261 109 IFQEPMTSLNPVFTVGEQIAESI-RLHQGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQR 543
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRA 267
|
....*...
gi 490704625 544 LLAAVPRL 551
Cdd:PRK10261 268 LLAAVPQL 275
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
300-548 |
3.03e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 186.93 E-value: 3.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 300 HYPVRKGvlrrvaaWVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELR 377
Cdd:PRK11153 10 VFPQGGR-------TIHALNNVSLHIPAGEIFGVIGASGAGKST----LIRCINLleRPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 378 RLRQDIQIVFQDpFASLDPRMRVGDI---LEegIASLRPELAASARRAravgLLERVGLpADTPTRYPHEFSGGQRQRIA 454
Cdd:PRK11153 79 KARRQIGMIFQH-FNLLSSRTVFDNValpLE--LAGTPKAEIKARVTE----LLELVGL-SDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 455 IARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLH 534
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
250
....*....|....
gi 490704625 535 APRHEMTQRLLAAV 548
Cdd:PRK11153 231 HPKHPLTREFIQST 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
315-537 |
6.41e-54 |
|
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: 182.40 E-value: 6.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDpFA 392
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINGleRPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDI---LEegIASLRPELAASARRAravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:cd03258 93 LLSSRTVFENValpLE--IAGVPKAEIEERVLE----LLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-253 |
6.20e-52 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 178.20 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEGLDVDVAGEsgvtHAVKRLQLAVAQGETFALVGESGSGKSmTALALL--RLLPDAGRIVGGQIELGGTDLND 81
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKT-TLLNALsaRLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 82 LSERAMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSGG 161
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDA--ARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESAD 241
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250
....*....|..
gi 490704625 242 ARTFFERPRHPY 253
Cdd:PRK11701 236 TDQVLDDPQHPY 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
291-549 |
1.94e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 179.17 E-value: 1.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGVLRrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE-GARVQGRAM-LDGHDL 368
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLeFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 LGASRRELRRL-RQDIQIVFQDPFASLDPRMRVGDILEEGIaSLRPELAASARRARAVGLLERVGLPaDTPTR---YPHE 444
Cdd:PRK11022 76 QRISEKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAI-KVHQGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250 260
....*....|....*....|....*
gi 490704625 525 EMGPADTVLHAPRHEMTQRLLAAVP 549
Cdd:PRK11022 234 ETGKAHDIFRAPRHPYTQALLRALP 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-547 |
2.12e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 183.30 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGrivggQIELGGTD 78
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKS-T---LMKILsgvyqPDSG-----EILLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 79 LNDLSERAMRgvRGGrIGIIFQEPatSLNPVMRVGDQIvetLAAHTPLRG-----AAARERAIDWLRRVGIPE-PERRID 152
Cdd:COG1129 68 VRFRSPRDAQ--AAG-IAIIHQEL--NLVPNLSVAENI---FLGREPRRGglidwRAMRRRARELLARLGLDIdPDTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DYpfqfSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMR 232
Cdd:COG1129 140 DL----SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 233 GGEIVESADARTFFErprhpyaRELFEAIPtfakrGRPLSAQgraadQGKAAPEAGAVVLDVQDLlvhypVRKGVLRrva 312
Cdd:COG1129 215 DGRLVGTGPVAELTE-------DELVRLMV-----GRELEDL-----FPKRAAAPGEVVLEVEGL-----SVGGVVR--- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 313 awveavnGVTFTLRAGETLALLGESGCGKTttgkALLRLVEGAR--VQGRAMLDGHDLLGASRRElrRLRQDIQIVFQDp 390
Cdd:COG1129 270 -------DVSFSVRAGEILGIAGLVGAGRT----ELARALFGADpaDSGEIRLDGKPVRIRSPRD--AIRAGIAYVPED- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 fasldpRMRVGDILEEGIA-----------SLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARAL 459
Cdd:COG1129 336 ------RKGEGLVLDLSIRenitlasldrlSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 460 AVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIV-EMgpadtvlhaPRH 538
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIVgEL---------DRE 479
|
570
....*....|
gi 490704625 539 EMTQ-RLLAA 547
Cdd:COG1129 480 EATEeAIMAA 489
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
315-548 |
2.89e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 175.57 E-value: 2.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG-ARVQ-GRAMLDGHDLlGASRRELRRLRQDIQIVFQDpFa 392
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINLlEEPDsGTITVDGEDL-TDSKKDINKLRRKVGMVFQQ-F- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDILEEG-IASLRpeLAASARRARAVGLLERVGLP--ADtptRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:COG1126 87 NLFPHLTVLENVTLApIKVKK--MSKAEAEERAMELLERVGLAdkAD---AYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 470 EPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAV 548
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-238 |
4.78e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 174.46 E-value: 4.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIVggqieLGGTDLNDL 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPTSGEVL-----IDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAMRGVRGGRIGIIFQEPAtsLNPVMRVGDQIveTLAAH-TPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGG 161
Cdd:COG1136 76 SERELARLRRRHIGFVFQFFN--LLPELTALENV--ALPLLlAGVSRKERRERARELLERVGLGD---RLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRnVAHHVALMRGGEIVE 238
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-260 |
6.03e-51 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 175.80 E-value: 6.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGESG-----VTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAGRI--VGGQIELGGTD 78
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKS----TLAKML--AGIIepTSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 79 LN--DLSERAMRgvrggrIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGI-PEperRIDDYP 155
Cdd:COG4167 77 LEygDYKYRCKH------IRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE---HANFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 156 FQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
250 260
....*....|....*....|....*
gi 490704625 236 IVESADARTFFERPRHPYARELFEA 260
Cdd:COG4167 228 VVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-250 |
1.11e-50 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 173.92 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIvggqiELGGTDLNDLSE 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLerPTSGSV-----LVDGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 85 RAMRGVRGgRIGIIFQEpatslnpvmrvgdqiVETLAAHT-------PLR-----GAAARERAIDWLRRVGIpepERRID 152
Cdd:cd03258 75 KELRKARR-RIGMIFQH---------------FNLLSSRTvfenvalPLEiagvpKAEIEERVLELLELVGL---EDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMR 232
Cdd:cd03258 136 AYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVME 215
|
250
....*....|....*...
gi 490704625 233 GGEIVESADARTFFERPR 250
Cdd:cd03258 216 KGEVVEEGTVEEVFANPQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
315-537 |
1.82e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.21 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG-ARV-QGRAMLDGHDLLG--ASRRelrrlrqDIQIVFQDp 390
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAGfETPdSGRILLDGRDVTGlpPEKR-------NVGMVFQD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FAsLDPRMRVgdilEEGIA-SLRPELAASARRARAVG-LLERVGLP--ADtptRYPHEFSGGQRQRIAIARALAVEPKVL 466
Cdd:COG3842 86 YA-LFPHLTV----AENVAfGLRMRGVPKAEIRARVAeLLELVGLEglAD---RYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGvvE--YLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE--EalALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-533 |
2.15e-50 |
|
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: 181.15 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESgvthAVKRLQLAVAQGETFALVGESGSGKSMTaLALLRLL----PDAGRIV--------------- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyePTSGRIIyhvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 69 ----------GGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEpATSLNPVMRVGDQIVETLAaHTPLRGAAARERAIDW 138
Cdd:TIGR03269 76 skvgepcpvcGGTLEPEEVDFWNLSDKLRRRIRK-RIAIMLQR-TFALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 139 LRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL 218
Cdd:TIGR03269 153 IEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 219 AVVRNVAHHVALMRGGEIVESADARTFFERprhpyareLFEAIPTFAKrgrplsaqgraadqgKAAPEAGAVVLDVQDLL 298
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVAV--------FMEGVSEVEK---------------ECEVEVGEPIIKVRNVS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 299 VHY-PVRKGVlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE--GARVQGRAMLDGHDLLGASRRE 375
Cdd:TIGR03269 287 KRYiSVDRGV-------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNVRVGDEWVDMTKPGPDG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 376 LRRLRQDIQIVFQDpfASLDPRMRVGDILEEGIaSLrpELAASARRARAVGLLERVGLPADTPT----RYPHEFSGGQRQ 451
Cdd:TIGR03269 360 RGRAKRYIGILHQE--YDLYPHRTVLDNLTEAI-GL--ELPDELARMKAVITLKMVGFDEEKAEeildKYPDELSEGERH 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADT 531
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
..
gi 490704625 532 VL 533
Cdd:TIGR03269 515 IV 516
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
315-535 |
4.28e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 4.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLlgasRRELRRLRQDIQIVFQDPfaSL 394
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL--RPTSGEVRVLGEDV----ARDPAEVRRRIGYVPQEP--AL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEgIASLRPeLAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:COG1131 85 YPDLTVRENLRF-FARLYG-LPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 475 LDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHA 535
Cdd:COG1131 162 LDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
315-523 |
2.25e-49 |
|
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: 169.98 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLR-QDIQIVFQDPf 391
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILGGLDRptSGEVRVDGTDISKLSEKELAAFRrRHIGFVFQSF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 aSLDPRMRVGDILEegIASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:cd03255 92 -NLLPDLTALENVE--LPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYlADRIAVMHGGRI 523
Cdd:cd03255 168 TGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
314-549 |
4.54e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 172.78 E-value: 4.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 314 WVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLV-EGARVQG-RAMLDGHDLLGASRRELRRL-RQDIQIVFQDP 390
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkDNWHVTAdRFRWNGIDLLKLSPRERRKIiGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FASLDPRMRVGDILEEGIASLRPE----LAASARRARAVGLLERVGL--PADTPTRYPHEFSGGQRQRIAIARALAVEPK 464
Cdd:COG4170 99 SSCLDPSAKIGDQLIEAIPSWTFKgkwwQRFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRL 544
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKAL 258
|
....*
gi 490704625 545 LAAVP 549
Cdd:COG4170 259 LRSMP 263
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-236 |
5.75e-49 |
|
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: 168.82 E-value: 5.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIvggqiELGGTDLNDLSER 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLdrPTSGEV-----RVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGVRGGRIGIIFQEPatSLNPVMRVGDQiVETLAAHTPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQR 165
Cdd:cd03255 75 ELAAFRRRHIGFVFQSF--NLLPDLTALEN-VELPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRnVAHHVALMRGGEI 236
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
319-536 |
1.12e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 168.62 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLRQDIQIVFQDP--FASLDp 396
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS--GEILVDGQDITGLSEKELYELRRRIGMLFQGGalFDSLT- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 rmrvgdiLEEGIA-SLR--PELAASARRARAVGLLERVGLPaDTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:COG1127 99 -------VFENVAfPLRehTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 474 ALD-VSVqAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:COG1127 171 GLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-532 |
2.62e-48 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 175.22 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKS--MTALA-LLRllPDAGRI-VGGQ----------IELGgtdlndlseramrgvrggrIGI 97
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKStlMKILYgLYQ--PDSGEIlIDGKpvrirsprdaIALG-------------------IGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 98 IFQEPatSLNPVMRVGDQIVetLAAHTPLRG----AAARERAIDWLRRVGIP-EPERRIDDYPFqfsgGQKQRLMIAIAL 172
Cdd:COG3845 85 VHQHF--MLVPNLTVAENIV--LGLEPTKGGrldrKAARARIRELSERYGLDvDPDAKVEDLSV----GEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 173 AAEPKLLIADEPTTALdvTVQaQVLELLAGIQR--EMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFferpr 250
Cdd:COG3845 157 YRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 251 hpYARELfeaiptfAKR--GRPLSAQGRaadqgKAAPEAGAVVLDVQDLlvHYPVRKGVlrrvaawvEAVNGVTFTLRAG 328
Cdd:COG3845 229 --SEEEL-------AELmvGREVLLRVE-----KAPAEPGEVVLEVENL--SVRDDRGV--------PALKDVSLEVRAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 329 ETLALLGESGCGKTttgkALLRLVEGAR--VQGRAMLDGHDLLGASRRELRRLRqdIQIVFQDpfasldpRMRVGDILEE 406
Cdd:COG3845 285 EILGIAGVAGNGQS----ELAEALAGLRppASGSIRLDGEDITGLSPRERRRLG--VAYIPED-------RLGRGLVPDM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 407 GIA-------------SLRPELAASARRARAVGLLER--VGLP-ADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:COG3845 352 SVAenlilgryrrppfSRGGFLDRKAIRAFAEELIEEfdVRTPgPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQ 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTV 532
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-242 |
4.66e-48 |
|
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: 166.84 E-value: 4.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDLN 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLL--AGldRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 DLSERAMRGVRGGRIGIIFQE----PA-TSLNPVMrvgdqivetlaahTP--LRGAA-ARERAIDWLRRVGIPEperRID 152
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSfqllPTlTALENVM-------------LPleLAGRRdARARARALLERVGLGH---RLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMR 232
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLR 220
|
250
....*....|
gi 490704625 233 GGEIVESADA 242
Cdd:COG4181 221 AGRLVEDTAA 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
319-530 |
5.40e-48 |
|
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: 166.91 E-value: 5.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDP--FASL 394
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKST----LLRLIVGllRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGalFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIASLRPELAASARRAravglLERVGLPADTpTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIREIVLEK-----LEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 475 LDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-261 |
1.19e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 165.94 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGRIVggqieLGGTDLNDlSERAMRGVRGgRIG 96
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-T---LLRCInlleePDSGTIT-----VDGEDLTD-SKKDINKLRR-KVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 97 IIFQepatSLN--PVMRVGDQIveTLAahtPL--RG---AAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIA 169
Cdd:COG1126 81 MVFQ----QFNlfPHLTVLENV--TLA---PIkvKKmskAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 170 IALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|..
gi 490704625 250 RHPYARELFEAI 261
Cdd:COG1126 228 QHERTRAFLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
289-525 |
1.32e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.60 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 289 AVVLDVQDLLVHYPVRKGVlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGH 366
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE-------VTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILGGLDRptSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 367 DLLGASRRELRRLR-QDIQIVFQDP-----------------FASLDPRMRVGDILEegiaslrpelaasarraravgLL 428
Cdd:COG1136 71 DISSLSERELARLRrRHIGFVFQFFnllpeltalenvalpllLAGVSRKERRERARE---------------------LL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 429 ERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVV 508
Cdd:COG1136 130 ERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA 208
|
250
....*....|....*..
gi 490704625 509 EYlADRIAVMHGGRIVE 525
Cdd:COG1136 209 AR-ADRVIRLRDGRIVS 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
292-548 |
3.27e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 165.48 E-value: 3.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRKGVlrrvaawveavNGVTFTLRAGETLALLGESGCGKTTTGKAL-LRLVEGARVQGRAMLDG--HDL 368
Cdd:PRK11701 7 LSVRGLTKLYGPRKGC-----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYRMRDGqlRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 LGASRRELRRL-RQDIQIVFQDPFASLdpRMRV---GDILEEGIAS-------LRPElaasarrarAVGLLERVGLPADT 437
Cdd:PRK11701 76 YALSEAERRRLlRTEWGFVHQHPRDGL--RMQVsagGNIGERLMAVgarhygdIRAT---------AGDWLERVEIDAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 438 PTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAV 517
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|.
gi 490704625 518 MHGGRIVEMGPADTVLHAPRHEMTQRLLAAV 548
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
317-552 |
3.19e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 165.71 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLlgASRRELRRLRqdIQIVFQDPfaSL 394
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAGLETpdSGRIVLNGRDL--FTNLPPRERR--VGFVFQHY--AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIASLRPelAASARRARAVGLLERVGLP--ADtptRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:COG1118 87 FPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQLEglAD---RYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNFG-VVEyLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRL 551
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEeALE-LADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVL 240
|
.
gi 490704625 552 R 552
Cdd:COG1118 241 R 241
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-261 |
3.59e-46 |
|
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: 162.69 E-value: 3.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDVAGESGVthavKRLQLAVAQGETFALVGESGSGKSmTALALL--RLLPDAGRIVGGQIELGGTDLNDL 82
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGC----RDVSFDLYPGEVLGIVGESGSGKS-TLLGCLagRLAPDHGTATYIMRSGAELELYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAMRGVRGGRIGIIFQEPATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSGGQ 162
Cdd:TIGR02323 76 SEAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDP--TRIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 163 KQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADA 242
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLT 233
|
250
....*....|....*....
gi 490704625 243 RTFFERPRHPYARELFEAI 261
Cdd:TIGR02323 234 DQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
317-539 |
2.25e-45 |
|
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: 160.16 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDpfASLDP 396
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT--SGEIFIDGEDIREQDPVELRR---KIGYVIQQ--IGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVgdilEEGIAsLRPELA---ASARRARAVGLLERVGL-PADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:cd03295 89 HMTV----EENIA-LVPKLLkwpKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHE 539
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
315-527 |
2.54e-45 |
|
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: 158.84 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRelrrlRQDIQIVFQDPfa 392
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTT----LLRLIAGLERpdSGEILIDGRDVTGVPPE-----RRNIGMVFQDY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVgdilEEGIAS-LRPELAASARRARAVG-LLERVGLPADTPtRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:cd03259 82 ALFPHLTV----AENIAFgLKLRGVPKAEIRARVReLLELVGLEGLLN-RYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
315-537 |
2.98e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.42 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPFA 392
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKST----LLRLLNGllKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLdprmrVGDILEEGIA-SLR------PELAASARRaravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKV 465
Cdd:COG1122 87 QL-----FAPTVEEDVAfGPEnlglprEEIRERVEE-----ALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
308-522 |
9.31e-45 |
|
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: 156.19 E-value: 9.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 308 LRRVAAW---VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLlGASRRELRRLRQDIQ 384
Cdd:cd03229 3 LKNVSKRygqKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE--PDSGSILIDGEDL-TDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 385 IVFQDPfaSLDPRMRVGDILEEGIaslrpelaasarraravgllervglpadtptryphefSGGQRQRIAIARALAVEPK 464
Cdd:cd03229 80 MVFQDF--ALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGR 522
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
25-257 |
9.96e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 161.51 E-value: 9.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIVggqieLGGTDLNDLSERAMRGVRGgRIGIIFQEp 102
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLerPTSGRVL-----VDGQDLTALSEKELRKARR-QIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 atsLNpvmrvgdqiveTLAAHT-------PLRGAAARERAID-----WLRRVGIPEperRIDDYPFQFSGGQKQRLMIAI 170
Cdd:PRK11153 91 ---FN-----------LLSSRTvfdnvalPLELAGTPKAEIKarvteLLELVGLSD---KADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 171 ALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPR 250
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
....*..
gi 490704625 251 HPYAREL 257
Cdd:PRK11153 234 HPLTREF 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
310-547 |
2.60e-44 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 157.55 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 310 RVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEG--ARVQGRAMLDGHDLLGASRRElrrlrQDIQIVF 387
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvRQTAGRVLLDGKPVAPCALRG-----RKIATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 388 QDPFASLDPRMRVGD-ILEEGIASLRPelaasARRARAVGLLERVGL--PADTPTRYPHEFSGGQRQRIAIARALAVEPK 464
Cdd:PRK10418 86 QNPRSAFNPLHTMHThARETCLALGKP-----ADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRL 544
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
...
gi 490704625 545 LAA 547
Cdd:PRK10418 241 VSA 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-239 |
3.04e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.76 E-value: 3.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqiELGGTDLNDLSERAMRgvrggRIGIIFQ 100
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEV-----RVLGEDVARDPAEVRR-----RIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EPAtsLNPVMRVGdQIVETLAAHTPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLI 180
Cdd:COG1131 81 EPA--LYPDLTVR-ENLRFFARLYGLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 181 ADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
317-539 |
3.35e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 158.72 E-value: 3.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDpfASLDP 396
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIE--PTSGRILIDGEDIRDLDPVELRR---RIGYVIQQ--IGLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVgdilEEGIAsLRPELA---ASARRARAVGLLERVGLPADT-PTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:COG1125 90 HMTV----AENIA-TVPRLLgwdKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHE 539
Cdd:COG1125 165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPAND 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
287-525 |
5.90e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.79 E-value: 5.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 287 AGAVVLDVQDLLVHYPVRKGVlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLD 364
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGG-------VTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIAGleKPTSGEVLVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 365 GhdllgasrRELRRLRQDIQIVFQDPfaSLDPRMRVGDILEEG--IASLRPELAASARRAravgLLERVGLpADTPTRYP 442
Cdd:COG1116 72 G--------KPVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGleLRGVPKAERRERARE----LLELVGL-AGFEDAYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 443 HEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNfgvVE---YLADRIAVM- 518
Cdd:COG1116 137 HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDeavFLADRVVVLs 213
|
....*...
gi 490704625 519 -HGGRIVE 525
Cdd:COG1116 214 aRPGRIVE 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-269 |
1.28e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 156.00 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGGrIGIIFQEPATSLNPVMR 111
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKS----TLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 112 VGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPErrIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVT 191
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSV--LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 192 VQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESA---DARTFferpRHPYARELFEAI-PTFAKR 267
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQpvgDKLTF----SSPAGRVLQNAVlPAFPVR 261
|
..
gi 490704625 268 GR 269
Cdd:PRK10419 262 RR 263
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
32-269 |
5.90e-43 |
|
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: 154.19 E-value: 5.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEPATSLNPVMR 111
Cdd:TIGR02769 32 LSIEEGETVGLLGRSGCGKS----TLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRR-DVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 112 VGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPErrIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVT 191
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSED--ADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 192 VQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERpRHPYARELFEAI-PTFAKRGR 269
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVlPEHPVRRS 262
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-250 |
7.59e-43 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 152.87 E-value: 7.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGEsgvTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqiELGGTDLNDLSERA 86
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEV-----LVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGvrggRIGIIFQEPAtslnpvmrvgDQIVET-----LA---AHTPLRGAAARERAIDWLRRVGIPEPERRiddYPFQF 158
Cdd:COG1122 73 LRR----KVGLVFQNPD----------DQLFAPtveedVAfgpENLGLPREEIRERVEEALELVGLEHLADR---PPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|..
gi 490704625 239 SADARTFFERPR 250
Cdd:COG1122 215 DGTPREVFSDYE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
316-523 |
1.74e-42 |
|
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: 149.86 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLlgasRRELRRLRQDIQIVFQDPfaSLD 395
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--PDSGEIKVLGKDI----KKEPEEVKRRIGYLPEEP--SLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEegiaslrpelaasarraravgllervglpadtptrypheFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:cd03230 86 ENLTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490704625 476 DVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:cd03230 127 DPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
305-532 |
2.84e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.75 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 305 KGVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLRQD 382
Cdd:COG3638 6 RNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNGLVEptSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 383 IQIVFQDPfaSLDPRMRVgdiLEE----------GIASLRPeLAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQR 452
Cdd:COG3638 82 IGMIFQQF--NLVPRLSV---LTNvlagrlgrtsTWRSLLG-LFPPEDRERALEALERVGL-ADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 453 IAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTV 532
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
317-552 |
9.02e-42 |
|
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: 151.26 E-value: 9.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLR-QDIQIVFQDpFAsLD 395
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS--GKVLIDGQDIAAMSRKELRELRrKKISMVFQS-FA-LL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEG--IASLRPELAASARRARavglLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:cd03294 115 PHRTVLENVAFGleVQGVPRAEREERAAEA----LELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRLR 552
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRAK 268
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
292-525 |
1.18e-41 |
|
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: 149.16 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRKGvlrrvaaWVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGhdll 369
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIAGleRPTSGEVLVDG---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 370 gasrRELRRLRQDIQIVFQDPfaSLDPRMRVgdilEEGIAsLRPELAASARRARA---VGLLERVGLpADTPTRYPHEFS 446
Cdd:cd03293 66 ----EPVTGPGPDRGYVFQQD--ALLPWLTV----LDNVA-LGLELQGVPKAEAReraEELLELVGL-SGFENAYPHQLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 447 GGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHG--GRIV 524
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
.
gi 490704625 525 E 525
Cdd:cd03293 214 A 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
316-523 |
2.13e-41 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 148.45 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlGASRRELRRLRQDIQIVFQDpFaSLD 395
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD--SGTIIIDGLKL-TDDKKNINELRQKVGMVFQQ-F-NLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEGIASLRpELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:cd03262 89 PHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490704625 476 DVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:cd03262 167 DPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
317-522 |
2.15e-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: 148.38 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDPFASL 394
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKST----LLRLLNGllGPTSGEVLVDGKDLTKLSLKELRR---KVGLVFQNPDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 dprmrVGDILEEGIA-SLRPELAASARRARAV-GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:cd03225 89 -----FGPTVEEEVAfGLENLGLPEEEIEERVeEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490704625 473 SALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGR 522
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-258 |
2.95e-41 |
|
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: 148.97 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSMtalaLLRLL-----PDAGRIvggqiELGGT 77
Cdd:COG1127 1 MSEPMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSV----LLKLIigllrPDSGEI-----LVDGQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 78 DLNDLSERAMRGVRGgRIGIIFQEPA--TSLNpvmrVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRiddYP 155
Cdd:COG1127 68 DITGLSEKELYELRR-RIGMLFQGGAlfDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 156 FQFSGGQKQRLMIAIALAAEPKLLIADEPTTALD-VTVqAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGG 234
Cdd:COG1127 140 SELSGGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250 260
....*....|....*....|....
gi 490704625 235 EIVESADARTFFERPrHPYARELF 258
Cdd:COG1127 219 KIIAEGTPEELLASD-DPWVRQFL 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
291-548 |
3.35e-41 |
|
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: 149.04 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRkgvlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLG 370
Cdd:COG1120 1 MLEAENLSVGYGGR-----------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS--GEVLLDGRDLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRLrqdIQIVFQDPFASLDprMRVGDILEEGIASLRPELAASARRARAV--GLLERVGLpADTPTRYPHEFSGG 448
Cdd:COG1120 68 LSRRELARR---IAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSAEDREAveEALERTGL-EHLADRPVDELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 449 QRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGP 528
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
250 260
....*....|....*....|
gi 490704625 529 ADTVLhaprhemTQRLLAAV 548
Cdd:COG1120 222 PEEVL-------TPELLEEV 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-258 |
4.50e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 151.79 E-value: 4.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGRIVggqieLGGTD 78
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKT-T---LLRMIagfetPDSGRIL-----LDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 79 LNDLS--ERamrgvrggRIGIIFQEPAtsLNPVMRVGDQIVetlaahTPLR-----GAAARERAIDWLRRVGIPEPERRi 151
Cdd:COG3842 69 VTGLPpeKR--------NVGMVFQDYA--LFPHLTVAENVA------FGLRmrgvpKAEIRARVAELLELVGLEGLADR- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 152 ddYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHD----LAvvrnVAHH 227
Cdd:COG3842 132 --YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADR 205
|
250 260 270
....*....|....*....|....*....|.
gi 490704625 228 VALMRGGEIVESADARTFFERPRHPYARELF 258
Cdd:COG3842 206 IAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-256 |
1.62e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.54 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLLpdAG--RIVGGQIELGGTD 78
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-T---LLRLI--AGleKPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 79 LNDLseramrgvrGGRIGIIFQEPAtsLNPVMRVGDQIveTLAAhtPLRG---AAARERAIDWLRRVGIpepERRIDDYP 155
Cdd:COG1116 75 VTGP---------GPDRGVVFQEPA--LLPWLTVLDNV--ALGL--ELRGvpkAERRERARELLELVGL---AGFEDAYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 156 FQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL--AVVrnVAHHVALM-- 231
Cdd:COG1116 137 HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAVF--LADRVVVLsa 214
|
250 260
....*....|....*....|....*
gi 490704625 232 RGGEIVESADARtfFERPRHPYARE 256
Cdd:COG1116 215 RPGRIVEEIDVD--LPRPRDRELRT 237
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
291-549 |
1.92e-40 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 149.57 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGvlrrvaaWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLV-EGARVQG-RAMLDGHDL 368
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG-------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkDNWRVTAdRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 LGASRRELRRL-RQDIQIVFQDPFASLDPRMRVGDILEEGIASL----RPELAASARRARAVGLLERVGL--PADTPTRY 441
Cdd:PRK15093 76 LRLSPRERRKLvGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWtykgRWWQRFGWRKRRAIELLHRVGIkdHKDAMRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 442 PHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGG 521
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250 260
....*....|....*....|....*...
gi 490704625 522 RIVEMGPADTVLHAPRHEMTQRLLAAVP 549
Cdd:PRK15093 236 QTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-237 |
2.47e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 146.74 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGEsgvTHAVKRLQLAVAQGETFALVGESGSGKSMtalaLLRLLPDAGRIVGGQIELGGTDLNDLSER 85
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNGLVEPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGVRGgRIGIIFQEPAtsLNPVMRVgdqiVE-----TLAAHTPLRG------AAARERAIDWLRRVGIPE-PERRIDd 153
Cdd:COG3638 74 ALRRLRR-RIGMIFQQFN--LVPRLSV----LTnvlagRLGRTSTWRSllglfpPEDRERALEALERVGLADkAYQRAD- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 154 ypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRG 233
Cdd:COG3638 146 ---QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
....
gi 490704625 234 GEIV 237
Cdd:COG3638 223 GRVV 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
317-530 |
3.02e-40 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 145.84 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDL--LGASRRElrrlrqdIQIVFQDpFA 392
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIAGFETptSGEILLDGKDItnLPPHKRP-------VNTVFQN-YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 sLDPRMRVgdilEEGIA-SLRPELAASARRARAVG-LLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:cd03300 83 -LFPHLTV----FENIAfGLRLKKLPKAEIKERVAeALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG-PAD 530
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGtPEE 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
283-554 |
4.65e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 145.95 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 283 AAPEAGAVVLDVQDLLVHYPVRKgvlrrvaawveAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLR-------LVEGA 355
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ-----------ALKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 356 RVQGRAMLDGHDLLgASRRELRRLRQDIQIVFQ--DPFA-------SLDPRMR-------VGDILEEgiaSLRpelaasa 419
Cdd:COG1117 68 RVEGEILLDGEDIY-DPDVDVVELRRRVGMVFQkpNPFPksiydnvAYGLRLHgikskseLDEIVEE---SLR------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 420 rrarAVGLLERVglpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALD-VSVqAQILDLLRDLQAELGIay 498
Cdd:COG1117 137 ----KAALWDEV---KDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKDYTI-- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 499 LFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAvprlRFG 554
Cdd:COG1117 207 VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITG----RFG 258
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
317-537 |
4.83e-40 |
|
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: 145.56 E-value: 4.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDllgASRRELRRlRQdIQIVFQDpfASL 394
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTT----LLRLIAGLErpDSGTILFGGED---ATDVPVQE-RN-VGFVFQH--YAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDI----LEEGIASLRPElaASARRARAVGLLERVGLP--ADtptRYPHEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:cd03296 86 FRHMTVFDNvafgLRVKPRSERPP--EAEIRAKVHELLKLVQLDwlAD---RYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-263 |
9.30e-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: 145.86 E-value: 9.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSER 85
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCINRLIEPTSGKVLIDGQDIAAMSRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGVRGGRIGIIFQEPAtsLNPVMRVGDQIVETLAahtpLRG---AAARERAIDWLRRVGIpepERRIDDYPFQFSGGQ 162
Cdd:cd03294 95 ELRELRRKKISMVFQSFA--LLPHRTVLENVAFGLE----VQGvprAEREERAAEALELVGL---EGWEHKYPDELSGGM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 163 KQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADA 242
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
250 260
....*....|....*....|.
gi 490704625 243 RTFFERPRHPYARELFEAIPT 263
Cdd:cd03294 246 EEILTNPANDYVREFFRGVDR 266
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-236 |
1.17e-39 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 143.44 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDlSERAMRGVRGgRIGIIFQE 101
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQ-KVGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 paTSLNPVMRVGDQIVEtlaAHTPLRG---AAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:cd03262 85 --FNLFPHLTVLENITL---APIKVKGmskAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
316-532 |
1.28e-39 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 143.86 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRL---VEGARVQGRAMLDGHDLLGASRRELRrLRQDIQIVFQ--DP 390
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlIPGAPDEGEVLLDGKDIYDLDVDVLE-LRRRVGMVFQkpNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FasldpRMRVGDILEEGiASLRPELAASARRARAVGLLERVGLPADTPTR-YPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:cd03260 93 F-----PGSIYDNVAYG-LRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTV 532
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-235 |
1.83e-39 |
|
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: 142.99 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 20 ESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIF 99
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKS-T---LLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR----KVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEPATSLnpVM-RVGDQIVETLAaHTPLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:cd03225 82 QNPDDQF--FGpTVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
315-533 |
2.13e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 143.84 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDllgaSRRELRRLRQDIQIVFQDPFasL 394
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGED----VRKEPREARRQIGVLPDERG--L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEgIASLRPeLAASARRARAVGLLERVGLPADTPTRYpHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:COG4555 86 YDRLTVRENIRY-FAELYG-LFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 475 LDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:COG4555 163 LDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-237 |
3.90e-39 |
|
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: 143.65 E-value: 3.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTAL-ALLRLLPDAGrivgGQIELGGTDLNDLSER 85
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLKPSS----GEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AmrgvRGGRIGIIFQEPATSLNpvMRVGDqIVET-LAAHTPLRGAAARE--RAIDW-LRRVGIPE-PERRIDdypfQFSG 160
Cdd:COG1120 72 E----LARRIAYVPQEPPAPFG--LTVRE-LVALgRYPHLGLFGRPSAEdrEAVEEaLERTGLEHlADRPVD----ELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
315-525 |
4.42e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.50 E-value: 4.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLRQDIQIVFQDpFA 392
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYGEERptSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPR---------MRVGDILEEGIASLRPELaasarraravglLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEP 463
Cdd:COG2884 90 LLPDRtvyenvalpLRVTGKSRKEIRRRVREV------------LDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQAeLGIAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
24-338 |
5.55e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 5.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMtalaLLRLL-----PDAGRIVggqieLGGTDLN-DLS--ERamrgvrggRI 95
Cdd:COG1118 15 FTLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIagletPDSGRIV-----LNGRDLFtNLPprER--------RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 96 GIIFQEPAtsLNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAE 175
Cdd:COG1118 78 GFVFQHYA--LFPHMTVAENIAFGLRVRPPSK-AEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYAR 255
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 256 ELFEAIPTF--AKRGRPLSAQGRAADQGKAAPEAGAVVL----DVQdlLVHYPVRKGVLrrvAAWVEAVNGVTFTLRAge 329
Cdd:COG1118 232 RFLGCVNVLrgRVIGGQLEADGLTLPVAEPLPDGPAVAGvrphDIE--VSREPEGENTF---PATVARVSELGPEVRV-- 304
|
....*....
gi 490704625 330 TLALLGESG 338
Cdd:COG1118 305 ELKLEDGEG 313
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-237 |
5.91e-39 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 142.71 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVdvaGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAM 87
Cdd:cd03256 1 IEVENLSK---TYPNGKKALKDVSLSINPGEFVALIGPSGAGKS----TLLRCLNGLVEPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 RGVRGgRIGIIFQEPAtsLNPVMRVGDQI-VETLAAHTPLRG------AAARERAIDWLRRVGIPE-PERRIDdypfQFS 159
Cdd:cd03256 74 RQLRR-QIGMIFQQFN--LIERLSVLENVlSGRLGRRSTWRSlfglfpKEEKQRALAALERVGLLDkAYQRAD----QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 160 GGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
292-522 |
1.08e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 139.44 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPvrkgvlrrvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGarVQGRAMLDGHDLLGA 371
Cdd:cd03228 1 IEFKNVSFSYP---------GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP--TSGEILIDGVDLRDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLrqdIQIVFQDPFasldprmrvgdILEegiASLRPELaasarraravgllervglpadtptrypheFSGGQRQ 451
Cdd:cd03228 70 DLESLRKN---IAYVPQDPF-----------LFS---GTIRENI-----------------------------LSGGQRQ 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEyLADRIAVMHGGR 522
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
321-530 |
1.79e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 141.30 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTtgkaLLR---LVEGARvQGRAMLDGH--DLLGA-SRRELRRLRQDIQIVFQDpfASL 394
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSS----LLRvlnLLEMPR-SGTLNIAGNhfDFSKTpSDKAIRELRRNVGMVFQQ--YNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEgiASLR-PELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK11124 94 WPHLTVQQNLIE--APCRvLGLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 474 ALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:PRK11124 171 ALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-238 |
2.86e-38 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 139.96 E-value: 2.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDLNDLSer 85
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLI--AGleRPDSGEILIDGRDVTGVP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 amrgVRGGRIGIIFQEPAtsLNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQR 165
Cdd:cd03259 69 ----PERRNIGMVFQDYA--LFPHLTVAENIAFGLKLRGVPK-AEIRARVRELLELVGLEGLLNR---YPHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
319-523 |
5.87e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.80 E-value: 5.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDPFAsldPRM 398
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT--SGEIYLDGKPLSAMPPPEWRR---QVAYVPQEPAL---WGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 399 RVGDILEEgIASLRPElaaSARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVS 478
Cdd:COG4619 89 TVRDNLPF-PFQLRER---KFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490704625 479 VQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:COG4619 165 NTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-238 |
9.45e-38 |
|
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: 138.76 E-value: 9.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDLNDlser 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRII--AGleRPTSGEVLVDGEPVTG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 amrgvRGGRIGIIFQEPAtsLNPVMRVGDQIVETLAAHtPLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQR 165
Cdd:cd03293 71 -----PGPDRGYVFQQDA--LLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL--AVVrnVAHHVALM--RGGEIVE 238
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAVF--LADRVVVLsaRPGRIVA 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
315-530 |
1.32e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 138.85 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPfaSL 394
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS--GSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIASLRP------ELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:cd03256 90 IERLSVLENVLSGRLGRRStwrslfGLFPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
321-536 |
1.83e-37 |
|
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: 141.78 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG-ARV-QGRAMLDGHDLLGASRR-----ELRRlrqdIQIVFQDpfAS 393
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTT----LLRAIAGlERPdSGRIRLGGEVLQDSARGiflppHRRR----IGYVFQE--AR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDILEEGIASLRPELAASARRaravGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:COG4148 88 LFPHLSVRGNLLYGRKRAPRAERRISFD----EVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
316-551 |
3.67e-37 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 137.62 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDllgASRRELRRlrQDIQIVFQDpfAS 393
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKST----LLRIIAGLEqpDSGRIRLNGQD---ATRVHARD--RKIGFVFQH--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDILEEGIASLRPELAASARRARAvgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEE--LLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRL 551
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
32-256 |
4.25e-37 |
|
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: 137.25 E-value: 4.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSMtalaLLRLL-----PDAGrivggQIELGGTDLNDLSERAMRGVRGgRIGIIFQEPA--T 104
Cdd:cd03261 21 LDVRRGEILAIIGPSGSGKST----LLRLIvgllrPDSG-----EVLIDGEDISGLSEAELYRLRR-RMGMLFQSGAlfD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNpvmrVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLLIADEP 184
Cdd:cd03261 91 SLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 185 TTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPrHPYARE 256
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQ 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-236 |
6.55e-37 |
|
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: 134.83 E-value: 6.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqiELGGTDLNDLSERAMRgvrggRIGIIFQ 100
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEI-----KVLGKDIKKEPEEVKR-----RIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EPatSLNPVMRVGDQIvetlaahtplrgaaareraidwlrrvgipeperriddypfQFSGGQKQRLMIAIALAAEPKLLI 180
Cdd:cd03230 81 EP--SLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 181 ADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-258 |
1.11e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 136.28 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVggqieLGGTDLNDLSERAMRgvRggRIGIIFQ 100
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGEIF-----IDGEDIREQDPVELR--R--KIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EpaTSLNPVMRVGDQI--VETLAAHTPlrgAAARERAIDWLRRVGIPEPERRiDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:cd03295 83 Q--IGLFPHMTVEENIalVPKLLKWPK---EKIRERADELLALVGLDPAEFA-DRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARELF 258
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-547 |
1.27e-36 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 142.76 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 21 SGVThAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDA---GRIVGGQIELGGTDLNDlSERAmrgvrggRIGI 97
Cdd:PRK13549 16 GGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyeGEIIFEGEELQASNIRD-TERA-------GIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 98 IFQEPAtsLNPVMRVGDQIvetLAAHTPLRG-----AAARERAIDWLRRVGIP-EPERRIDDYpfqfSGGQKQRLMIAIA 171
Cdd:PRK13549 87 IHQELA--LVKELSVLENI---FLGNEITPGgimdyDAMYLRAQKLLAQLKLDiNPATPVGNL----GLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 172 LAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP-- 249
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDii 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 250 RHPYARELFEAIPtfakrgrplsaqgraadqgKAAPEAGAVVLDVQDLLVHYPVRKGVLRrvaawveaVNGVTFTLRAGE 329
Cdd:PRK13549 237 TMMVGRELTALYP-------------------REPHTIGEVILEVRNLTAWDPVNPHIKR--------VDDVSFSLRRGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 330 TLALLGESGCGKTTTGKALLRLVEGaRVQGRAMLDGHDLlgASRRELRRLRQDIQIVFQDpfasldpRMRVGDILEEGIA 409
Cdd:PRK13549 290 ILGIAGLVGAGRTELVQCLFGAYPG-RWEGEIFIDGKPV--KIRNPQQAIAQGIAMVPED-------RKRDGIVPVMGVG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 410 -----------SLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVS 478
Cdd:PRK13549 360 knitlaaldrfTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 479 VQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIvemgPADTvlhaPRHEMTQ-RLLAA 547
Cdd:PRK13549 440 AKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL----KGDL----INHNLTQeQVMEA 500
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
318-545 |
1.87e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 136.03 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKA--LLRLVEGARVQ-GRAMLDGHDLLGASRRELRRLRQDIQIVFQDpfASL 394
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDTARSLSQQKGLIRQLRQHVGFVFQN--FNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIASLRPELAASARRARAvGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATARAR-ELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 475 LDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLL 545
Cdd:PRK11264 175 LDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
318-473 |
2.25e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.39 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPFasLDPR 397
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT--EGTILLDGQDL---TDDERKSLRKEIGYVFQDPQ--LFPR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 398 MRVGDILEEGIASLRPELAASARRARAVglLERVGLP---ADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKDARAEEA--LEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
318-527 |
2.70e-36 |
|
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: 133.33 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRLrqdIQIVFQdpfasldpr 397
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS--SGEILLDGKDLASLSPKELARK---IAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 mrvgdileegiaslrpelaasarraravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:cd03214 81 -----------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490704625 478 SVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03214 131 AHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
316-533 |
3.91e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 143.44 E-value: 3.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRR----LRQDIQ------- 384
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT--SGRILIDGIDLRQIDPASLRRqigvVLQDVFlfsgtir 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 385 --IVFQDPFASLDprmrvgDILEegIASLrpelaasarraraVGLLERV-GLPA--DTP-----TRypheFSGGQRQRIA 454
Cdd:COG2274 567 enITLGDPDATDE------EIIE--AARL-------------AGLHDFIeALPMgyDTVvgeggSN----LSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 455 IARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEyLADRIAVMHGGRIVEMGPADTVL 533
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
315-545 |
4.03e-36 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 137.71 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDpFA 392
Cdd:TIGR02314 18 IQALNNVSLHVPAGQIYGVIGASGAGKST----LIRCVNLLErpTSGSVIVDGQDLTTLSNSELTKARRQIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDIleegiaSLRPELAASARR---ARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:TIGR02314 93 LLSSRTVFGNV------ALPLELDNTPKDeikRKVTELLALVGL-GDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLL 545
Cdd:TIGR02314 166 EATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKFI 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
315-530 |
5.61e-36 |
|
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: 133.65 E-value: 5.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlgasRRELRRLRQDIQIVFQDPfaSL 394
Cdd:cd03265 13 FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT--SGRATVAGHDV----VREPREVRRRIGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRM----------RV----GDILEEGIASLrpelaasarraravglLERVGLpADTPTRYPHEFSGGQRQRIAIARALA 460
Cdd:cd03265 85 DDELtgwenlyihaRLygvpGAERRERIDEL----------------LDFVGL-LEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-237 |
5.66e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 134.73 E-value: 5.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGEsgvTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERA 86
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKS----TLLRCINRLVEPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGVRGgRIGIIFQE-----PATSLNPVMrvgdqiVETLAAHTPLRG------AAARERAIDWLRRVGIPE-PERRIDdy 154
Cdd:TIGR02315 74 LRKLRR-RIGMIFQHynlieRLTVLENVL------HGRLGYKPTWRSllgrfsEEDKERALSALERVGLADkAYQRAD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 155 pfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGG 234
Cdd:TIGR02315 145 --QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
...
gi 490704625 235 EIV 237
Cdd:TIGR02315 223 EIV 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
317-522 |
7.36e-36 |
|
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: 131.21 E-value: 7.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQdpfasldp 396
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDI---AKLPLEELRRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 rmrvgdileegiaslrpelaasarraravgllervglpadtptrypheFSGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490704625 477 VSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGR 522
Cdd:cd00267 113 PASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
316-530 |
1.40e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLR---LVEGARvQGRAMLDGHDL---LGASRRELRRLRQDIQIVFQD 389
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSS----LLRvlnLLETPD-SGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 pfASLDPRMRVGDILEEgiASLR-PELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:COG4161 91 --YNLWPHLTVMENLIE--APCKvLGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-245 |
1.58e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 132.69 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVdvagESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRIVGGQIELGGTDLNDL 82
Cdd:cd03260 1 IELRDLNV----YYGDKHALKDISLDIPKGEITALIGPSGCGKS----TLLRLLnrlndLIPGAPDEGEVLLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAMRGVRggRIGIIFQEPatslNPV-MRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIP-EPERRIDdyPFQFSG 160
Cdd:cd03260 73 DVDVLELRR--RVGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRLH--ALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHVALMRGGEIVESA 240
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 490704625 241 DARTF 245
Cdd:cd03260 223 PTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-238 |
2.02e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.48 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEpaTS 105
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKS-T---LLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR-RIGVVFQD--FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVGDQIVETLAAhTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:COG2884 90 LLPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 186 TALDVTVQAQVLELLAGIQReMGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:COG2884 166 GNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
291-529 |
3.53e-35 |
|
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: 132.42 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGVLRrvaawveavnGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLLG 370
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALK----------NINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE--PSSGSILLEGTDITK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRLRQDIQIVFQDpfASLDPRMRVgdiLE-------------EGIASLRPElaasARRARAVGLLERVGLPADT 437
Cdd:TIGR02315 69 LRGKKLRKLRRRIGMIFQH--YNLIERLTV---LEnvlhgrlgykptwRSLLGRFSE----EDKERALSALERVGLADKA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 438 PTRyPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAV 517
Cdd:TIGR02315 140 YQR-ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVG 218
|
250
....*....|..
gi 490704625 518 MHGGRIVEMGPA 529
Cdd:TIGR02315 219 LKAGEIVFDGAP 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-236 |
5.12e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 5.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTAL-ALLRLLPdagrIVGGQIELGGTDLnd 81
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP----PTSGTVRLFGKPP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 82 lseramrGVRGGRIGIIFQEPATSLNPVMRVGDqIVET-LAAHTPL---RGAAARERAIDWLRRVGIPEPE-RRIDdypf 156
Cdd:COG1121 71 -------RRARRRIGYVPQRAEVDWDFPITVRD-VVLMgRYGRRGLfrrPSRADREAVDEALERVGLEDLAdRPIG---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
16-235 |
6.65e-35 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 129.61 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 16 DVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERamRGVRGGRI 95
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKS----TLLRCIAGLEEPDSGSILIDGEDLTDLEDE--LPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 96 GIIFQEPAtsLNPVMRVGDQIVETLaahtplrgaaareraidwlrrvgipeperriddypfqfSGGQKQRLMIAIALAAE 175
Cdd:cd03229 79 GMVFQDFA--LFPHLTVLENIALGL--------------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-186 |
8.11e-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: 128.15 E-value: 8.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrivgGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPatSL 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE----GTILLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 NPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIPE-PERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGLSK-REKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 490704625 186 T 186
Cdd:pfam00005 150 A 150
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-245 |
3.80e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 129.36 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGrivggQIELGGTDLN---DLSERAMRGVRGgRIG 96
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDSG-----QLNIAGHQFDfsqKPSEKAIRLLRQ-KVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 97 IIFQEpaTSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:COG4161 86 MVFQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 177 KLLIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTF 245
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-547 |
4.06e-34 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 135.34 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGriVGGQIELGGTDLndlSERAMRGVRGGRIGIIFQE 101
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT--WDGEIYWSGSPL---KASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 paTSLNPVMRVGDQIVetLAAHTPLRG-----AAARERAIDWLRRVGIPEPE--RRIDDYpfqfSGGQKQRLMIAIALAA 174
Cdd:TIGR02633 87 --LTLVPELSVAENIF--LGNEITLPGgrmayNAMYLRAKNLLRELQLDADNvtRPVGDY----GGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFErprhpya 254
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 255 relfEAIPTFAKrGRPLSAQgraadQGKAAPEAGAVVLDVQDLLVHYPVRKGVLRrvaawveaVNGVTFTLRAGETLALL 334
Cdd:TIGR02633 231 ----DDIITMMV-GREITSL-----YPHEPHEIGDVILEARNLTCWDVINPHRKR--------VDDVSFSLRRGEILGVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 335 GESGCGKTTTGKALLRLVEGaRVQGRAMLDGHDLlgASRRELRRLRQDIQIVFQD-PFASLDPRMRVGDILEegIASL-- 411
Cdd:TIGR02633 293 GLVGAGRTELVQALFGAYPG-KFEGNVFINGKPV--DIRNPAQAIRAGIAMVPEDrKRHGIVPILGVGKNIT--LSVLks 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 412 ---RPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLR 488
Cdd:TIGR02633 368 fcfKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 489 DLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIvemgPADTVlhapRHEMTQ-RLLAA 547
Cdd:TIGR02633 448 QLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL----KGDFV----NHALTQeQVLAA 498
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
317-533 |
4.57e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 130.26 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPFASL 394
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKST----LIQHLNGllKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 -------D----PRmRVGdiLEEGIASLRPElaasarraravGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEP 463
Cdd:TIGR04521 96 feetvykDiafgPK-NLG--LSEEEAEERVK-----------EALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-249 |
7.45e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 129.49 E-value: 7.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGrivggQIELGGTDLNDLSERAMRGVRGgRIGIIFQE 101
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNglLKPTSG-----TVTIDGRDITAKKKKKLKDLRK-KVGLVFQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 PAtslnpvmrvgDQIVETL----AAHTP----LRGAAARERAIDWLRRVGIPEperridDY----PFQFSGGQKQRLMIA 169
Cdd:TIGR04521 91 PE----------HQLFEETvykdIAFGPknlgLSEEEAEERVKEALELVGLDE------EYlersPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 170 IALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
315-537 |
9.76e-34 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 127.94 E-value: 9.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLRqdIQIVFQDP-- 390
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTT----LFNLISGFLRptSGSVLFDGEDITGLPPHEIARLG--IGRTFQIPrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FASLDPR--MRVG--DILEEGIASLRPELAASARRARAVGLLERVGLP--ADTPTRyphEFSGGQRQRIAIARALAVEPK 464
Cdd:cd03219 87 FPELTVLenVMVAaqARTGSGLLLARARREEREARERAEELLERVGLAdlADRPAG---ELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
315-538 |
1.11e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.96 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG-ARV-QGRAMLDGHDL--LGASRRelrrlrqDIQIVFQDp 390
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAGlEDPtSGEILIGGRDVtdLPPKDR-------NIAMVFQS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FAsLDPRMRVgdilEEGIAS-LRPELAASARRARAVG-LLERVGLPA--DtptRYPHEFSGGQRQRIAIARALAVEPKVL 466
Cdd:COG3839 84 YA-LYPHMTV----YENIAFpLKLRKVPKAEIDRRVReAAELLGLEDllD---RKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFgvVE--YLADRIAVMHGGRIVEMGPADTVLHAPRH 538
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ--VEamTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-547 |
1.26e-33 |
|
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: 127.84 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLlgasrRELRRLRQDIQIVFQDpfASLDPR 397
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSV----LLETIAGFIKpdSGKILLNGKDI-----TNLPPEKRDISYVPQN--YALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEEGiasLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:cd03299 86 MTVYKNIAYG---LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 478 SVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAA 547
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGF 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
300-536 |
1.49e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.99 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 300 HYPVRKGVLRRVAAWVeAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLLGASRRElr 377
Cdd:PRK11432 5 NFVVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAGLEkpTEGQIFIDGEDVTHRSIQQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 378 rlrQDIQIVFQDpfASLDPRMRVGDILEEGIASL---RPELAASARRAravglLERVGLpADTPTRYPHEFSGGQRQRIA 454
Cdd:PRK11432 78 ---RDICMVFQS--YALFPHMSLGENVGYGLKMLgvpKEERKQRVKEA-----LELVDL-AGFEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 455 IARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHN----FGVveylADRIAVMHGGRIVEMGPAD 530
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDqseaFAV----SDTVIVMNKGKIMQIGSPQ 222
|
....*.
gi 490704625 531 TVLHAP 536
Cdd:PRK11432 223 ELYRQP 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
291-533 |
1.67e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRkgvlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGhdllg 370
Cdd:COG1121 6 AIELENLTVSYGGR-----------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP--PTSGTVRLFG----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 asrRELRRLRQDIQIVFQdpFASLDPR--MRVGDILEEGIASLRPELAASARRARAV--GLLERVGLP--ADTPTRyphE 444
Cdd:COG1121 68 ---KPPRRARRRIGYVPQ--RAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAvdEALERVGLEdlADRPIG---E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
....*....
gi 490704625 525 EmGPADTVL 533
Cdd:COG1121 219 H-GPPEEVL 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
315-527 |
1.92e-33 |
|
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: 126.60 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTgkalLRLVEGARV--QGRAMLDGHDL--LGASRRelrrlrqDIQIVFQDp 390
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEptSGRIYIGGRDVtdLPPKDR-------DIAMVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FAsLDPRMRVGDILEEGIASLRPELAASARRARAVGLLERVGLPADtptRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:cd03301 81 YA-LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLD---RKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
315-524 |
1.92e-33 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 124.85 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLRqdIQIVFQdpfa 392
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKST----LMKILSGLYKpdSGEILVDGKEVSFASPRDARRAG--IAMVYQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 sldprmrvgdileegiaslrpelaasarraravgllervglpadtptrypheFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:cd03216 83 ----------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490704625 473 SALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
305-544 |
2.66e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.13 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 305 KGVLRRVAAwVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRElRRLRQD 382
Cdd:PRK09493 5 KNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCINKLEEitSGDLIVDGLKVNDPKVDE-RLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 383 IQIVFQDpFaSLDPRMRVGDILEEGIASLRpELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVE 462
Cdd:PRK09493 79 AGMVFQQ-F-YLFPHLTALENVMFGPLRVR-GASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 463 PKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRhemTQ 542
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP---SQ 230
|
..
gi 490704625 543 RL 544
Cdd:PRK09493 231 RL 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
315-547 |
4.64e-33 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.84 E-value: 4.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLR-------------LVEGARVQGRAMLDGHdLLGASRRELRRLRQ 381
Cdd:COG4598 21 LEVLKGVSLTARKGDVISIIGSSGSGKST----FLRcinlletpdsgeiRVGGEEIRLKPDRDGE-LVPADRRQLQRIRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 382 DIQIVFQDpFaSLDPRMRV-GDILEEGIASLRpeLAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALA 460
Cdd:COG4598 96 RLGMVFQS-F-NLWSHMTVlENVIEAPVHVLG--RPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEM 540
Cdd:COG4598 171 MEPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSER 249
|
....*..
gi 490704625 541 TQRLLAA 547
Cdd:COG4598 250 LRQFLSS 256
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
323-527 |
4.91e-33 |
|
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: 125.49 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 323 FTLRA-----GETLALLGESGCGKTTtgkaLLRLVEGA--------RVQGRAMLDGHDLLGASRRElRRlrqdIQIVFQD 389
Cdd:cd03297 13 FTLKIdfdlnEEVTGIFGASGAGKST----LLRCIAGLekpdggtiVLNGTVLFDSRKKINLPPQQ-RK----IGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 pfASLDPRMRVGDILEEGIASLRPELAASARRAravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:cd03297 84 --YALFPHLNVRENLAFGLKRKRNREDRISVDE----LLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
322-545 |
9.35e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 9.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 322 TFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGA--SRRElrrlrqdIQIVFQDP--FASLD 395
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKST----LLNLIAGflPPDSGRILWNGQDLTALppAERP-------VSMLFQENnlFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 prmrvgdiLEEGIA-SLRPELAASARRARAV-GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:COG3840 88 --------VAQNIGlGLRPGLKLTAEQRAQVeQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLL 545
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-245 |
9.40e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.51 E-value: 9.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGR--IVGGQIELGgtdlNDLSERAMRGVRGgRIGI 97
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRSGTlnIAGNHFDFS----KTPSDKAIRELRR-NVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 98 IFQEpaTSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:PRK11124 87 VFQQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTF 245
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
300-533 |
1.13e-32 |
|
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: 125.34 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 300 HYPVRKGVlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLlgaSRRELRRL 379
Cdd:cd03249 9 RYPSRPDV--------PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYD--PTSGEILLDGVDI---RDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 380 RQDIQIVFQDP--FA-SLDPRMRVGD---ILEEGIASLRPELAASARRARAVGLLERVGlpadtptryPH--EFSGGQRQ 451
Cdd:cd03249 76 RSQIGLVSQEPvlFDgTIAENIRYGKpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVG---------ERgsQLSGGQKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQI---LDllrdlQAELGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGP 528
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVqeaLD-----RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
....*
gi 490704625 529 ADTVL 533
Cdd:cd03249 221 HDELM 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
32-237 |
1.15e-32 |
|
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: 124.75 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQepATSLNPVMR 111
Cdd:TIGR02982 26 LEINPGEIVILTGPSGSGKT----TLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRR-RIGYIFQ--AHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 112 VGDQIVETLAAHTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVT 191
Cdd:TIGR02982 99 ARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490704625 192 VQAQVLELLAGIQREMGMAVLLITHDLAVVrNVAHHVALMRGGEIV 237
Cdd:TIGR02982 176 SGRDVVELMQKLAKEQGCTILMVTHDNRIL-DVADRILQMEDGKLL 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-543 |
1.19e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.80 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE---GARVQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDPF 391
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypEARVSGEVYLDGQDIFKMDVIELRR---RVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 A----SLDPRMRVGDILEEGIASLRPELAASARRARAVGLLERVGLPADTPTrypHEFSGGQRQRIAIARALAVEPKVLI 467
Cdd:PRK14247 93 PipnlSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPA---GKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 468 CDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQR 543
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-552 |
1.54e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.89 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARVQ--GRAMLDGHDLLGASRRELRrlrqdIQIVFQDpfASLDP 396
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTT----LLRIIAGLEHQtsGHIRFHGTDVSRLHARDRK-----VGFVFQH--YALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEEGIASL--RPELAASARRARAVGLLERVGLP--ADtptRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PRK10851 88 HMTVFDNIAFGLTVLprRERPNAAAIKAKVTQLLEMVQLAhlAD---RYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRLR 552
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQ 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-237 |
2.15e-32 |
|
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: 122.54 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 9 RIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTAL-ALLRLLPDAGrivgGQIELGGTDLNDLSERAm 87
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPSS----GEILLDGKDLASLSPKE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 rgvRGGRIGIIFQepatslnpvmrvgdqivetlaahtplrgaaareraidWLRRVGIPE-PERRIDdypfQFSGGQKQRL 166
Cdd:cd03214 71 ---LARKIAYVPQ-------------------------------------ALELLGLAHlADRPFN----ELSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-542 |
2.45e-32 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 130.29 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQ---LAVAQGETFALVGESGSGKSmtalALLRLL----PdAGRiVGGQIELGGT-----DLNDlSERamrgvRGgr 94
Cdd:NF040905 14 VKALDdvnLSVREGEIHALCGENGAGKS----TLMKVLsgvyP-HGS-YEGEILFDGEvcrfkDIRD-SEA-----LG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 95 IGIIFQEPAtsLNPVMRVGDQIVetLAAHTPLRGA----AARERAIDWLRRVGIPE-PERRIDDYpfqfsGGQKQRLM-I 168
Cdd:NF040905 80 IVIIHQELA--LIPYLSIAENIF--LGNERAKRGVidwnETNRRARELLAKVGLDEsPDTLVTDI-----GVGKQQLVeI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 169 AIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARtffer 248
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCR----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 249 prhpyARELFEAIPTFAKRGRPLSAqgRAADQgkaAPEAGAVVLDVQDLLVHYPVRKGvlRRVaawveaVNGVTFTLRAG 328
Cdd:NF040905 225 -----ADEVTEDRIIRGMVGRDLED--RYPER---TPKIGEVVFEVKNWTVYHPLHPE--RKV------VDDVSLNVRRG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 329 ETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDLlgasrrELRRLRQDIQ----IVFQDpfasldpRMRVGDIL 404
Cdd:NF040905 287 EIVGIAGLMGAGRTELAMSVFGRSYGRNISGTVFKDGKEV------DVSTVSDAIDaglaYVTED-------RKGYGLNL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 405 EEGI------ASLRpelaasarraravGLLERVGLPADTPTRYPHEF------------------SGGQRQRIAIARALA 460
Cdd:NF040905 354 IDDIkrnitlANLG-------------KVSRRGVIDENEEIKVAEEYrkkmniktpsvfqkvgnlSGGNQQKVVLSKWLF 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV-EMgpadtvlhaPRHE 539
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITgEL---------PREE 490
|
...
gi 490704625 540 MTQ 542
Cdd:NF040905 491 ASQ 493
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-257 |
2.87e-32 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 124.90 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIV--GGQIELGgtdlnDLSERAMRgvrggrIGIIFQEP 102
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLidDHPLHFG-----DYSYRSQR------IRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGI-PEperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:PRK15112 97 STSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPD---HASYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYAREL 257
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRL 249
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
333-553 |
3.05e-32 |
|
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: 126.45 E-value: 3.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 333 LLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLgasrrELRRLRQDIQIVFQDpfASLDPRMRVgdilEEGIA- 409
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAGFEQpdSGSIMLDGEDVT-----NVPPHLRHINMVFQS--YALFPHMTV----EENVAf 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 410 SLRPELAASARRARAV-GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLR 488
Cdd:TIGR01187 66 GLKMRKVPRAEIKPRVlEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 489 DLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAVPRLRF 553
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEA 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
32-259 |
3.25e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQepATSLNPV 109
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRVGDITIDTARSLSQQKGLIRQLRQ-HVGFVFQ--NFNLFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVGDQIVE--TLAAHTPLRGAAARERAIdwLRRVGIPEPErriDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTA 187
Cdd:PRK11264 100 RTVLENIIEgpVIVKGEPKEEATARAREL--LAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 188 LDVTVQAQVLELLAGIQREMGMAVlLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARELFE 259
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
285-530 |
4.82e-32 |
|
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: 123.31 E-value: 4.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 285 PEAGAVVLDVQDLLVHYPVRKGVLrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAM 362
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGEL-------TILKGISLEVEAGESVAIVGASGSGKST----LLGLLAGLDRptSGTVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 363 LDGHDLLGASRRELRRLR-QDIQIVFQDpFaSLDPRM----RVGDILEE-GIASLRPELAAsarraravgLLERVGLpAD 436
Cdd:COG4181 71 LAGQDLFALDEDARARLRaRHVGFVFQS-F-QLLPTLtaleNVMLPLELaGRRDARARARA---------LLERVGL-GH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 437 TPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNfgvvEYLA---D 513
Cdd:COG4181 139 RLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD----PALAarcD 214
|
250
....*....|....*..
gi 490704625 514 RIAVMHGGRIVEMGPAD 530
Cdd:COG4181 215 RVLRLRAGRLVEDTAAT 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
316-528 |
5.66e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.99 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDL--LGASRRelrrlrqDIQIVFQDpF 391
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAGFETpdSGRIMLDGQDIthVPAENR-------HVNTVFQS-Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 AsLDPRMRVGDILEEGiasLRPELAASARRARAV-GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:PRK09452 96 A-LFPHMTVFENVAFG---LRMQKTPAAEITPRVmEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGP 528
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
316-528 |
1.02e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.13 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgarVQ-GRAMLDGHDLLGASRRELRRLrqdIQIVFQDPF--- 391
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD---PTsGRILIDGVDIRDLTLESLRRQ---IGVVPQDTFlfs 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLDPRMRVGDI---LEEGIASLRpelaasarrarAVGLLERV-GLPA--DTP-----TRypheFSGGQRQRIAIARALA 460
Cdd:COG1132 428 GTIRENIRYGRPdatDEEVEEAAK-----------AAQAHEFIeALPDgyDTVvgergVN----LSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEyLADRIAVMHGGRIVEMGP 528
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDDGRIVEQGT 557
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-256 |
1.13e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.51 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 16 DVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLND--LSERAMRGvrgg 93
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 94 RIGIIFQE----PA-TSLNPVM----RVgdqivetlaahtplRGA---AARERAIDWLRRVGIPEperRIDDYPFQFSGG 161
Cdd:PRK09493 78 EAGMVFQQfylfPHlTALENVMfgplRV--------------RGAskeEAEKQARELLAKVGLAE---RAHHYPSELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESAD 241
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
250
....*....|....*
gi 490704625 242 ARTFFERPRHPYARE 256
Cdd:PRK09493 220 PQVLIKNPPSQRLQE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-523 |
1.53e-31 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 127.86 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 21 SGVThAVKRLQLAVAQGETFALVGESGSGKS--MTALALLrLLPDagrivGGQIELGGTDLNDLSEramrgVRGGRIGI- 97
Cdd:PRK15439 22 SGVE-VLKGIDFTLHAGEVHALLGGNGAGKStlMKIIAGI-VPPD-----SGTLEIGGNPCARLTP-----AKAHQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 98 -IFQEPAtsLNPVMRVGDQIVETLAAHtplrgAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:PRK15439 90 lVPQEPL--LFPNLSVKENILFGLPKR-----QASMQKMKQLLAALGC---QLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 177 KLLIADEPTTALdvtVQAQVLELLAGIQ--REMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERprhpya 254
Cdd:PRK15439 160 RILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 255 rELFEAIpTFAKRGRPLSAQ---GRAADQGKAAPEAGAVVLDVQDLlvhypvrKGvlrrvaawvEAVNGVTFTLRAGETL 331
Cdd:PRK15439 231 -DIIQAI-TPAAREKSLSASqklWLELPGNRRQQAAGAPVLTVEDL-------TG---------EGFRNISLEVRAGEIL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 332 ALLGESGCGKTTTGKAL--LRLVEGarvqGRAMLDGHDLLGASRRElrRLRQDIQIVFQDPFAS---LDPRMRVGdilee 406
Cdd:PRK15439 293 GLAGVVGAGRTELAETLygLRPARG----GRIMLNGKEINALSTAQ--RLARGLVYLPEDRQSSglyLDAPLAWN----- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 407 gIASL---RPELAASARRARAVglLER----VGLP---ADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:PRK15439 362 -VCALthnRRGFWIKPARENAV--LERyrraLNIKfnhAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 490704625 477 VSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:PRK15439 436 VSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
315-537 |
1.69e-31 |
|
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: 122.45 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLRqdiqIV--FQDP 390
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLITGFYRptSGRILFDGRDITGLPPHRIARLG----IArtFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 --FASLDPR--MRVG-------DILEEGIASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARAL 459
Cdd:COG0411 89 rlFPELTVLenVLVAaharlgrGLLAALLRLPRARREEREARERAEELLERVGL-ADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 460 AVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
315-525 |
1.72e-31 |
|
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: 121.30 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRRLR-QDIQIVFQdpF 391
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKST----LLHLLGGLDNptSGEVLFNGQSLSKLSSNERAKLRnKKLGFIYQ--F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLDPRMRVgdiLEE-GIASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:TIGR02211 92 HHLLPDFTA---LENvAMPLLIGKKSVKEAKERAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLaDRIAVMHGGRIVE 525
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-258 |
1.79e-31 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 123.66 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALL-RLL-PDAGRIvggqiELGGTDLNDLSERAMRgvRggRIGIIF 99
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRMInRLIePTSGRI-----LIDGEDIRDLDPVELR--R--RIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEpaTSLNPVMRVGDQIvetlaAHTP-LRG---AAARERAIDWLRRVGIPePERRIDDYPFQFSGGQKQRLMIAIALAAE 175
Cdd:COG1125 83 QQ--IGLFPHMTVAENI-----ATVPrLLGwdkERIRARVDELLELVGLD-PEEYRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL--AVVrnVAHHVALMRGGEIVESADARTFFERPRHPY 253
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIdeALK--LGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*
gi 490704625 254 ARELF 258
Cdd:COG1125 233 VADFV 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
271-535 |
3.25e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.57 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 271 LSAQGRAADQG-KAAPEAGAVVLDVQDLLVHYPVRKGVLrrvaawveavNGVTFTLRAGETLALLGESGCGKTTTGKALL 349
Cdd:COG4988 315 LDAPEPAAPAGtAPLPAAGPPSIELEDVSFSYPGGRPAL----------DGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 350 RLVEGArvQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDP--FAsldprmrvgDILEEGIASLRPELAASARRA--RAV 425
Cdd:COG4988 385 GFLPPY--SGSILINGVDLSDLDPASWRRQ---IAWVPQNPylFA---------GTIRENLRLGRPDASDEELEAalEAA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 426 GLLERV-GLPA--DTP-----TRypheFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIa 497
Cdd:COG4988 451 GLDEFVaALPDglDTPlgeggRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV- 525
|
250 260 270
....*....|....*....|....*....|....*...
gi 490704625 498 yLFITHNFGVVEyLADRIAVMHGGRIVEMGPADTVLHA 535
Cdd:COG4988 526 -ILITHRLALLA-QADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-253 |
3.41e-31 |
|
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: 124.38 E-value: 3.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEGLDVDVagesGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLS 83
Cdd:TIGR03265 1 SSPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKT----TLLRIIAGLERQTAGTIYQGGRDITRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 ERAmrgvRGgrIGIIFQEPAtsLNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQK 163
Cdd:TIGR03265 73 PQK----RD--YGIVFQSYA--LFPNLTVADNIAYGLKNRGMGR-AEVAERVAELLDLVGLPGSERK---YPGQLSGGQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 164 QRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADAR 243
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQ 220
|
250
....*....|
gi 490704625 244 TFFERPRHPY 253
Cdd:TIGR03265 221 EIYRHPATPF 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-526 |
3.69e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 126.82 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGldvdVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSER 85
Cdd:PRK09700 4 PYISMAG----IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSGIHEPTKGTITINNINYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 --AMRGvrggrIGIIFQEPAT----SLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFS 159
Cdd:PRK09700 76 laAQLG-----IGIIYQELSVidelTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 160 GGQKQRLMIAIALAAEPKLLIADEPTTALdvtVQAQVLELLAGIQ--REMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 238 ESADAR--TFFERPRHPYARELFEAIPtfakrgrplsaqgraADQGKAAPEAGAVVLDVQDLLVHYPVRkgvlrrvaawv 315
Cdd:PRK09700 225 CSGMVSdvSNDDIVRLMVGRELQNRFN---------------AMKENVSNLAHETVFEVRNVTSRDRKK----------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 eaVNGVTFTLRAGETLALLGESGCGKTTTGKALLrlveGA--RVQGRAMLDGHDLlgASRRELRRLRQDIQIVFQD---- 389
Cdd:PRK09700 279 --VRDISFSVCRGEILGFAGLVGSGRTELMNCLF----GVdkRAGGEIRLNGKDI--SPRSPLDAVKKGMAYITESrrdn 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 ---PFASLDPRMRVGDILEE-------GIASLRPELAASARRAravgllERVGLPADTPTRYPHEFSGGQRQRIAIARAL 459
Cdd:PRK09700 351 gffPNFSIAQNMAISRSLKDggykgamGLFHEVDEQRTAENQR------ELLALKCHSVNQNITELSGGNQQKVLISKWL 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 460 AVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEM 526
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
317-534 |
3.91e-31 |
|
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: 120.30 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTgkalLRLVEGARV--QGRAMLDGHDLlgasRRELRRLRQDIQIVFQdpFASL 394
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTT----LKMLTGELRptSGTAYINGYSI----RTDRKAARQSLGYCPQ--FDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEgIASLRpELAASARRARAVGLLERVGLP--ADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:cd03263 87 FDELTVREHLRF-YARLK-GLPKSEIKEEVELLLRVLGLTdkANKRAR---TLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVMHGGRIVEMGpadTVLH 534
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIG---SPQE 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-236 |
8.07e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.15 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVTHavkrLQLAVAQGETFALVGESGSGKSMtalaLLRLLPDAGRIVGGQIELGGTDLNDLSERAM 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSP----VSLTLEAGECVAITGPSGSGKST----LLRALADLDPPTSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 RGvrggRIGIIFQEPAtsLNPvMRVGDQIVETLAAHtplRGAAARERAIDWLRRVGIPEP--ERRIDDypfqFSGGQKQR 165
Cdd:COG4619 73 RR----QVAYVPQEPA--LWG-GTVRDNLPFPFQLR---ERKFDRERALELLERLGLPPDilDKPVER----LSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-249 |
1.25e-30 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 119.26 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRIVggqieLGGTDLNDL--SERamrgvrggR 94
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIagfetPTSGEIL-----LDGKDITNLppHKR--------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 95 IGIIFQEPAtsLNPVMRVGDQIVETLAAHTpLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAA 174
Cdd:cd03300 74 VNTVFQNYA--LFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-252 |
1.42e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDVagesGVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLR-------LLPDAgRiVGGQIE 73
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKS-T---LLRclnrmndLIPGA-R-VEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 74 LGGTDLNDLSERAMRgVRGgRIGIIFQEPatslNPV-MRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGI-PEPERRI 151
Cdd:COG1117 75 LDGEDIYDPDVDVVE-LRR-RVGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 152 DDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHVALM 231
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|.
gi 490704625 232 RGGEIVESADARTFFERPRHP 252
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDK 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-234 |
1.86e-30 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 118.69 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmtalALLRL-----LPDAGRIV----GGQIelggtDLNDLSERAMRGVRGGRIG 96
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKS----TLLKCiygnyLPDSGSILvrhdGGWV-----DLAQASPREILALRRRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 97 IIFQepatSLNPVMRVG--DQIVETLAAhtplRG---AAARERAIDWLRRVGIPEpeRRIDDYPFQFSGGQKQRLMIAIA 171
Cdd:COG4778 97 YVSQ----FLRVIPRVSalDVVAEPLLE----RGvdrEEARARARELLARLNLPE--RLWDLPPATFSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 172 LAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGG 234
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-249 |
4.36e-30 |
|
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: 117.82 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMtalaLLRLL-----PDAGRIVggqieLGGTDLNDLSERaMRGvrggrIGIIFQE 101
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSV----LLETIagfikPDSGKIL-----LNGKDITNLPPE-KRD-----ISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 PAtsLNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:cd03299 80 YA--LFPHMTVYKNIAYGLKKRKVDK-KEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-235 |
5.95e-30 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 115.56 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 14 DVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqiELGGTDLNDLSERAMRGvrg 92
Cdd:cd03228 5 NVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEI-----LIDGVDLRDLDLESLRK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 93 gRIGIIFQEP---ATSlnpvmrVGDQIvetlaahtplrgaaareraidwlrrvgipeperriddypfqFSGGQKQRLMIA 169
Cdd:cd03228 77 -NIAYVPQDPflfSGT------IRENI-----------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 170 IALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVALMRGGE 235
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
321-536 |
1.88e-29 |
|
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: 119.45 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG-ARVQ-GRAMLDGHDLLGASRR-ELRRLRQDIQIVFQDpfASLDPR 397
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTT----LIRLIAGlTRPDeGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEEGIASLRPELAASARRAravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFER----VIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 478 SVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
309-527 |
2.31e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 115.54 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 309 RRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRLRqdiqiVFQ 388
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGFDVVKEPAEARRRLG-----FVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 389 DPFAsLDPRMRVGDILE--EGIASLRPELAASARRAravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVL 466
Cdd:cd03266 85 DSTG-LYDRLTARENLEyfAGLYGLKGDELTARLEE----LADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-537 |
2.70e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRREL--RR--LRQDIQIVFqdPF 391
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKST----LLRALSGelSPDSGEVRLNGRPLADWSPAELarRRavLPQHSSLSF--PF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 asldprmRVGDILEEGIASLRPELAASARRARAVglLERVGLpADTPTRYPHEFSGGQRQRIAIARALA------VEPKV 465
Cdd:PRK13548 92 -------TVEEVVAMGRAPHGLSRAEDDALVAAA--LAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPET 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
294-518 |
3.25e-29 |
|
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: 114.94 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 294 VQDLLVHYPVRkgvlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGhdllgasr 373
Cdd:cd03235 2 VEDLTVSYGGH-----------PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT--SGSIRVFG-------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 374 RELRRLRQDIQIVFQdpFASLDPRM--RVGDILEEGIASLRPELAASARRARAVGL--LERVGLpADTPTRYPHEFSGGQ 449
Cdd:cd03235 61 KPLEKERKRIGYVPQ--RRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKADKAKVDeaLERVGL-SELADRQIGELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 450 RQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVM 518
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
314-557 |
3.32e-29 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 118.25 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 314 WVE-AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRelrrlRQDIQIVFQDp 390
Cdd:NF040840 11 WKEfKLRDISLEVKEGEYFIILGPSGAGKTV----LLELIAGIWPpdSGKIYLDGKDITNLPPE-----KRGIAYVYQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 fASLDPRMRVGDILEEGIaSLR----PELAASARRaravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVL 466
Cdd:NF040840 81 -YMLFPHKTVFENIAFGL-KLRkvpkEEIERKVKE-----IMELLGI-SHLLHRKPRTLSGGEQQRVALARALIIEPKLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLa 546
Cdd:NF040840 153 LLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFV- 231
|
250
....*....|.
gi 490704625 547 avprlrfGAEN 557
Cdd:NF040840 232 -------GFEN 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-237 |
3.49e-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: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 37 GETFALVGESGSGKSMtalaLLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQEPAtsLNPVMRVGDQI 116
Cdd:cd03297 23 EEVTGIFGASGAGKST----LLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYA--LFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 117 VETLAAHtplRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQV 196
Cdd:cd03297 97 AFGLKRK---RNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490704625 197 LELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
271-536 |
3.81e-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: 121.41 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 271 LSAQGRAADQGKAAPEAGAVVLDVQDLLVHYPvrkgvlrrvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLR 350
Cdd:COG4987 313 LDAPPAVTEPAEPAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 351 LVEgaRVQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPF---ASLDPRMRVGDI---LEEGIASLRpelaasarrarA 424
Cdd:COG4987 384 FLD--PQSGSITLGGVDLRDLDEDDLRRR---IAVVPQRPHlfdTTLRENLRLARPdatDEELWAALE-----------R 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 425 VGLLERV-GLPA--DTPTrypHE----FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIa 497
Cdd:COG4987 448 VGLGDWLaALPDglDTWL---GEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV- 523
|
250 260 270
....*....|....*....|....*....|....*....
gi 490704625 498 yLFITHNFGVVEyLADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:COG4987 524 -LLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
316-548 |
4.46e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 115.71 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE---GARVQGRAMLDGHDLLGASRRELRrLRQDIQIVFQ--DP 390
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQypNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FASLDPRMRVGDILE-EGIASLRPELAASAR-RARAVGLLERVglpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:PRK14267 97 FPHLTIYDNVAIGVKlNGLVKSKKELDERVEwALKKAALWDEV---KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAV 548
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
321-547 |
4.49e-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: 118.56 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDLLGASRRelrrlRQDIQIVFQDpfASLDPRMRV 400
Cdd:TIGR03258 24 LSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLTGRIAIADRDLTHAPPH-----KRGLALLFQN--YALFPHLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 401 GDILEEGIASLRpeLAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQ 480
Cdd:TIGR03258 97 EDNVAFGLRAQK--MPKADIAERVADALKLVGL-GDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 481 AQILDLLRDLQAEL-GIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAA 547
Cdd:TIGR03258 174 ANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGA 241
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
26-225 |
4.82e-29 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 114.80 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLR-LLPDAGRIvGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQepat 104
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnYLPDSGRI-LVRHEGAWVDLAQASPREVLEVRRKTIGYVSQ---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNPVMRVGD-QIVETLAAHTPLRGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:TIGR02324 98 FLRVIPRVSAlEVVAEPLLERGVPREAARARARELLARLNIPE--RLWHLPPATFSGGEQQRVNIARGFIADYPILLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVA 225
Cdd:TIGR02324 176 PTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVA 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-251 |
5.13e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.87 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLLpdAG--RIVGGQIELGGTDLNDLSERAmrgvRGgrIGIIF 99
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKS-T---LLRMI--AGleDPTSGEILIGGRDVTDLPPKD----RN--IAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEPAtsLNPVMRVGDQIvetlaAHtPLR-----GAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAA 174
Cdd:COG3839 82 QSYA--LYPHMTVYENI-----AF-PLKlrkvpKAEIDRRVREAAELLGL---EDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRH 251
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-238 |
8.17e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.89 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTalalLRLLPDAGRIVGGQIELGGTDLNDL--SERamrgvrggRIGIIF 99
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEPTSGRIYIGGRDVTDLppKDR--------DIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEPAtsLNPVMRVGDQIvetlaAHtPLRGAAARERAIDwlRRV----GIPEPERRIDDYPFQFSGGQKQRLMIAIALAAE 175
Cdd:cd03301 79 QNYA--LYPHMTVYDNI-----AF-GLKLRKVPKDEID--ERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-252 |
1.33e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIV--GGQIEL---GGTDLNDLSERAMRGVRGgR 94
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLekPSEGSIVvnGQTINLvrdKDGQLKVADKNQLRLLRT-R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 95 IGIIFQEpaTSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERriDDYPFQFSGGQKQRLMIAIALAA 174
Cdd:PRK10619 94 LTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHP 252
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
316-532 |
1.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.14 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGaSRRELRRLRQDIQIVFQDPFASLD 395
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT--SGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDI--------LEEGIASLRpelaasarrarAVGLLERVGLPADT-PTRYPHEFSGGQRQRIAIARALAVEPKVL 466
Cdd:PRK13637 98 EETIEKDIafgpinlgLSEEEIENR-----------VKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTV 532
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-251 |
1.48e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.17 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL---PDAGriVGGQIELGGTDLNDLSERAMRGVRggRIGII 98
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelnEEAR--VEGEVRLFGRNIYSPDVDPIEVRR--EVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 99 FQEPatslNPVMRVgdQIVETLAAHTPLRGAAARERAID----W-LRRVGI-PEPERRIDDYPFQFSGGQKQRLMIAIAL 172
Cdd:PRK14267 91 FQYP----NPFPHL--TIYDNVAIGVKLNGLVKSKKELDerveWaLKKAALwDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 173 AAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRH 251
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-252 |
1.65e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 114.13 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIV--GGQIELGGTDLNDL---SERAMRGVRGgRIGIIFQepat 104
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKS-TFLRCINLLetPDSGEIRvgGEEIRLKPDRDGELvpaDRRQLQRIRT-RLGMVFQ---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLN--PVMRVGDQIVETlaahtPLR-----GAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:COG4598 103 SFNlwSHMTVLENVIEA-----PVHvlgrpKAEAIERAEALLAKVGLAD---KRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHP 252
Cdd:COG4598 175 VMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSE 248
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
316-546 |
1.72e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLV-------EGARV---QGRAMLDGHD--LLGASRRELRRLRQDI 383
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKST----FLRCInflekpsEGSIVvngQTINLVRDKDgqLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 384 QIVFQDpFASLDPRMRVGDILEEGIASLrpELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEP 463
Cdd:PRK10619 95 TMVFQH-FNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQR 543
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
...
gi 490704625 544 LLA 546
Cdd:PRK10619 251 FLK 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-525 |
1.76e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGRI-VGGQIELGG----TDLND---LSERAMRGVRG-----G 93
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKS-T---LLKILagelePDSGEVsIPKGLRIGYlpqePPLDDdltVLDTVLDGDAElraleA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 94 RIGIIFQEPATSLNPVMRVGDQIVETLAAHtplrGAAARERAIDWLRRVGIPE--PERRIDDypfqFSGGQKQRLMIAIA 171
Cdd:COG0488 95 ELEELEAKLAEPDEDLERLAELQEEFEALG----GWEAEARAEEILSGLGFPEedLDRPVSE----LSGGWRRRVALARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 172 LAAEPKLLIADEPTTALDvtvqAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI----------VESAD 241
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLtlypgnysayLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 242 ARtfFERPRHPYA------RELFEAIPTFAKRGRPLS-AQGR--AAD----------------QGKAAPEAGAVVLDVQD 296
Cdd:COG0488 243 ER--LEQEAAAYAkqqkkiAKEEEFIRRFRAKARKAKqAQSRikALEklereepprrdktveiRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 297 LLVHYPVRKgVLRrvaawveavnGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRamldghdllgasrr 374
Cdd:COG0488 321 LSKSYGDKT-LLD----------DLSLRIDRGDRIGLIGPNGAGKST----LLKLLAGelEPDSGT-------------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 375 elRRLRQDIQIVF--QDpFASLDPRMRVgdiLEEgIASLRPELAASARRaravGLLERVGLPADTPTRYPHEFSGGQRQR 452
Cdd:COG0488 372 --VKLGETVKIGYfdQH-QEELDPDKTV---LDE-LRDGAPGGTEQEVR----GYLGRFLFSGDDAFKPVGVLSGGEKAR 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 453 IAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQaelGiAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-523 |
2.25e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 118.57 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGesgvthaVKRL---QLAVAQGETFALVGESGSGKSmtalALLRLLP-----DAGRIVggqiELGgt 77
Cdd:PRK10762 3 ALLQLKGIDKAFPG-------VKALsgaALNVYPGRVMALVGENGAGKS----TMMKVLTgiytrDAGSIL----YLG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 78 dlndlSERAMRGVRGGR---IGIIFQEpatsLNPVmrvgDQIveTLAAHTPL-RGAAARERAIDW----------LRRVG 143
Cdd:PRK10762 66 -----KEVTFNGPKSSQeagIGIIHQE----LNLI----PQL--TIAENIFLgREFVNRFGRIDWkkmyaeadklLARLN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 144 IPEPERRIDDypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVL----ELlagiqREMGMAVLLITHDLA 219
Cdd:PRK10762 131 LRFSSDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFrvirEL-----KSQGRGIVYISHRLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 220 VVRNVAHHVALMRGGE-IVESADARTFFERprhpyareLFEAIPtfakrGRPLSAQGRAADQgkaapEAGAVVLDVQDLl 298
Cdd:PRK10762 203 EIFEICDDVTVFRDGQfIAEREVADLTEDS--------LIEMMV-----GRKLEDQYPRLDK-----APGEVRLKVDNL- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 299 vhypvrKGvlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGA--RVQGRAMLDGHDLLGASRREl 376
Cdd:PRK10762 264 ------SG---------PGVNDVSFTLRKGEILGVSGLMGAGRTE----LMKVLYGAlpRTSGYVTLDGHEVVTRSPQD- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 377 rRLRQDIQIVFQDpfasldprmRVGDILEEGIA-----SLrPELAASARRARAVGLLERVGLPAD--------TPTRYPH 443
Cdd:PRK10762 324 -GLANGIVYISED---------RKRDGLVLGMSvkenmSL-TALRYFSRAGGSLKHADEQQAVSDfirlfnikTPSMEQA 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 444 --EFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGG 521
Cdd:PRK10762 393 igLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG 471
|
..
gi 490704625 522 RI 523
Cdd:PRK10762 472 RI 473
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-274 |
3.08e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.96 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGESgvTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRI-VGGQIelggtdlndLS 83
Cdd:PRK13635 4 EIIRVEHISFRYPDAA--TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTItVGGMV---------LS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 ERAMRGVRGgRIGIIFQEP------ATslnpvmrVGDQIVETLAAHTPLRGAAArERAIDWLRRVGIpepERRIDDYPFQ 157
Cdd:PRK13635 73 EETVWDVRR-QVGMVFQNPdnqfvgAT-------VQDDVAFGLENIGVPREEMV-ERVDQALRQVGM---EDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 158 FSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIV 237
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490704625 238 ESADARTFFERPRH--------PYARELFEAIptfAKRGRPLSAQ 274
Cdd:PRK13635 220 EEGTPEEIFKSGHMlqeigldvPFSVKLKELL---KRNGILLPNT 261
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
24-218 |
3.17e-28 |
|
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: 112.45 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAgriVGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQ--- 100
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNP---TSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQfhh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 --EPATSLNPVMR---VGDQIVETlaahtplrgaaARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAE 175
Cdd:TIGR02211 94 llPDFTALENVAMpllIGKKSVKE-----------AKERAYEMLEKVGL---EHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL 218
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL 202
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
291-528 |
3.60e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.96 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPvrkgvlrrvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLG 370
Cdd:PRK13635 5 IIRVEHISFRYP---------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA--GTITVGGMVLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRlrqDIQIVFQDPfaslDPRMrVGDILEEGIA-SL------RPELAASARRAravglLERVGLpADTPTRYPH 443
Cdd:PRK13635 74 ETVWDVRR---QVGMVFQNP----DNQF-VGATVQDDVAfGLenigvpREEMVERVDQA-----LRQVGM-EDFLNREPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 444 EFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYlADRIAVMHGGRI 523
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
....*
gi 490704625 524 VEMGP 528
Cdd:PRK13635 219 LEEGT 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
317-528 |
3.72e-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: 112.20 E-value: 3.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPF----- 391
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS--SGSILIDGVDI---SKIGLHDLRSRISIIPQDPVlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 --ASLDPRMRVGDilEEGIASLRpelaasarrarAVGLLERV-GLPADTPTRYPHE---FSGGQRQRIAIARALAVEPKV 465
Cdd:cd03244 94 irSNLDPFGEYSD--EELWQALE-----------RVGLKEFVeSLPGGLDTVVEEGgenLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNF-GVVEYlaDRIAVMHGGRIVEMGP 528
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLdTIIDS--DRILVLDKGRVVEFDS 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-237 |
3.94e-28 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 112.08 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGR-IVGGQielggtdlnDLSERAmRGVRGgRIGIIF 99
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRaTVAGH---------DVVREP-REVRR-RIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEPatSLNPVMrVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYpfqFSGGQKQRLMIAIALAAEPKLL 179
Cdd:cd03265 80 QDL--SVDDEL-TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
25-238 |
3.95e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 112.64 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLLpdAGRIVG--GQIELGGTDLNDLSERAMRgvrggRIGIIFQEP 102
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKT-T---LLRML--AGLLKPdsGSILIDGEDVRKEPREARR-----QIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 AtsLNPVMRVGDQIVETLAAHtPLRGAAARERAIDWLRRVGIPEP-ERRIDDypfqFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:COG4555 84 G--LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFlDRRVGE----LSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-261 |
4.18e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.29 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 20 ESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGRivgGQIELGGTDLNDLSERAMRGVRGGRIGIIF 99
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEPTR---GQVLIDGVDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEPAtsLNPVMRVGDQIvetlAAHTPLRGAAA---RERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:PRK10070 113 QSFA--LMPHMTVLDNT----AFGMELAGINAeerREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 177 KLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARE 256
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
|
....*
gi 490704625 257 LFEAI 261
Cdd:PRK10070 264 FFRGV 268
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-237 |
5.00e-28 |
|
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: 112.15 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTALALL--RLLPDAGRIVggqieLGGTDLNDLS-- 83
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFNLIsgFLRPTSGSVL-----FDGEDITGLPph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 ERAMRGvrggrIGIIFQEPA-----TSLNPVM--RVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIpepERRIDDYPF 156
Cdd:cd03219 71 EIARLG-----IGRTFQIPRlfpelTVLENVMvaAQARTGSGLLLARARREEREARERAEELLERVGL---ADLADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
.
gi 490704625 237 V 237
Cdd:cd03219 222 I 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
317-548 |
5.09e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.70 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLlgasrRELRRLRQDIQIVFQDpfASL 394
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGfeQPTAGQIMLDGVDL-----SHVPPYQRPINMMFQS--YAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVgdilEEGIA-SLRPELAASARRARAVG-LLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PRK11607 103 FPHMTV----EQNIAfGLKQDKLPKAEIASRVNeMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 473 SALDVSV----QAQILDLLRdlqaELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAV 548
Cdd:PRK11607 178 GALDKKLrdrmQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-543 |
5.75e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.83 E-value: 5.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 286 EAGAVVLDVQDL--LVHYPVRKGVLRrvaawveavnGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE----GARVQG 359
Cdd:PRK14246 2 EAGKSAEDVFNIsrLYLYINDKAILK----------DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydsKIKVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 360 RAMLDGHDLLgasRRELRRLRQDIQIVFQ--DPFASLDPRMRVGDILE-EGIASLRPELAASARRARAVGLLERVGLPAD 436
Cdd:PRK14246 72 KVLYFGKDIF---QIDAIKLRKEVGMVFQqpNPFPHLSIYDNIAYPLKsHGIKEKREIKKIVEECLRKVGLWKEVYDRLN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 437 TPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIA 516
Cdd:PRK14246 149 SPAS---QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVA 223
|
250 260
....*....|....*....|....*..
gi 490704625 517 VMHGGRIVEMGPADTVLHAPRHEMTQR 543
Cdd:PRK14246 224 FLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-239 |
5.77e-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: 111.86 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSMTALALLRL-LPDAGrivggQIELGGTDLNDLSERAMRGvrggRIGIIFQEP---A 103
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPTSG-----EILLDGVDIRDLNLRWLRS----QIGLVSQEPvlfD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRVG--DQIVETLAAhtplrgaAARERAIDWLRrVGIPEP-ERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLI 180
Cdd:cd03249 91 GTIAENIRYGkpDATDEEVEE-------AAKKANIHDFI-MSLPDGyDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 181 ADEPTTALDVTVQAQVLELLAgiQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVES 239
Cdd:cd03249 163 LDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
299-535 |
5.89e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 118.43 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 299 VHYPVRKG--VLRRVA-----AWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGarVQGRAMLDGHDLLGA 371
Cdd:TIGR03375 455 LHRPRLQGeiEFRNVSfaypgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQP--TEGSVLLDGVDIRQI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRlrqDIQIVFQDP---FASLdprmrvgdilEEGIASLRPEL--AASARRARAVGLLERVGLPADTPTRYPHE-- 444
Cdd:TIGR03375 533 DPADLRR---NIGYVPQDPrlfYGTL----------RDNIALGAPYAddEEILRAAELAGVTEFVRRHPDGLDMQIGErg 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 --FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEyLADRIAVMHGGR 522
Cdd:TIGR03375 600 rsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTSLLD-LVDRIIVMDNGR 676
|
250
....*....|...
gi 490704625 523 IVEMGPADTVLHA 535
Cdd:TIGR03375 677 IVADGPKDQVLEA 689
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-244 |
6.09e-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: 117.94 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEglDVDVAGESGVThAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqiELGGTDLND 81
Cdd:COG4988 332 AGPPSIELE--DVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSI-----LINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 82 LSERAMRGvrggRIGIIFQEP---ATSLNPVMRVGdqivetlaahtplRGAAARERAIDWLRRVGIPE--------PERR 150
Cdd:COG4988 404 LDPASWRR----QIAWVPQNPylfAGTIRENLRLG-------------RPDASDEELEAALEAAGLDEfvaalpdgLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 151 IDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVAL 230
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILV 543
|
250
....*....|....
gi 490704625 231 MRGGEIVESADART 244
Cdd:COG4988 544 LDDGRIVEQGTHEE 557
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
292-527 |
6.30e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 111.94 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPvrkgvlrrvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGA 371
Cdd:cd03251 1 VEFKNVTFRYP---------GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD--SGRILIDGHDVRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLrqdIQIVFQDPFAsldprmrVGDILEEGIASLRPELAAsarraravgllERVGLPADTPtrYPHEF------ 445
Cdd:cd03251 70 TLASLRRQ---IGLVSQDVFL-------FNDTVAENIAYGRPGATR-----------EEVEEAARAA--NAHEFimelpe 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 -------------SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYlA 512
Cdd:cd03251 127 gydtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-A 203
|
250
....*....|....*
gi 490704625 513 DRIAVMHGGRIVEMG 527
Cdd:cd03251 204 DRIVVLEDGKIVERG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
292-534 |
7.67e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 111.37 E-value: 7.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVrkgvlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLGA 371
Cdd:cd03224 1 LEVENLNAGYGK-----------SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL--PPRSGSIRFDGRDITGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRElrRLRQDIQIVFQDPfaSLDPRMRVGDILEEGiASLRPELAASARRARAVG----LLERVGLPADTptrypheFSG 447
Cdd:cd03224 68 PPHE--RARAGIGYVPEGR--RIFPELTVEENLLLG-AYARRRAKRKARLERVYElfprLKERRKQLAGT-------LSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 448 GQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
....*..
gi 490704625 528 PADTVLH 534
Cdd:cd03224 215 TAAELLA 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-239 |
1.13e-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: 117.63 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGRIvggqiELGGTDLNDLSERAMRGvrggRIGIIFQ 100
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKS-T---LLKLLlglyePTSGRI-----LIDGIDLRQIDPASLRR----QIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EP----ATslnpvmrvgdqIVETLAAHTPlrgAAARERAIDWLRRVGIPE-----P---ERRIDDYPFQFSGGQKQRLMI 168
Cdd:COG2274 557 DVflfsGT-----------IRENITLGDP---DATDEEIIEAARLAGLHDfiealPmgyDTVVGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 169 AIALAAEPKLLIADEPTTALDVTVQAQVLELLAgiQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVES 239
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLR--RLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVED 690
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
292-525 |
1.20e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.88 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRkgvlrrvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLL 369
Cdd:COG4525 4 LTVRHVSVRYPGG-------GQPQPALQDVSLTIESGEFVVALGASGCGKTT----LLNLIAGflAPSSGEITLDGVPVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 370 GASrrelrrlrQDIQIVFQDpfASLDPRMRVGDILEEG--IASLRPELAASARRAravgLLERVGLpADTPTRYPHEFSG 447
Cdd:COG4525 73 GPG--------ADRGVVFQK--DALLPWLNVLDNVAFGlrLRGVPKAERRARAEE----LLALVGL-ADFARRRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 448 GQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNfgvVE---YLADRIAVM--HGGR 522
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEealFLATRLVVMspGPGR 214
|
...
gi 490704625 523 IVE 525
Cdd:COG4525 215 IVE 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
16-253 |
1.46e-27 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 111.04 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 16 DVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSeramrgVRGGRI 95
Cdd:TIGR00968 5 NISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKS----TLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 96 GIIFQEPAtsLNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAE 175
Cdd:TIGR00968 75 GFVFQHYA--LFKHLTVRDNIAFGLEIRKHPK-AKIKARVEELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPY 253
Cdd:TIGR00968 149 PQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPF 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-248 |
1.58e-27 |
|
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: 111.75 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKS-----MTALallrLLPDAGRI-VGGqielggtdLNDLSERAMRGVRGgRIGIIF 99
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKStlaklLNGL----LLPTSGKVtVDG--------LDTLDEENLWEIRK-KVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QepatslNPvmrvGDQIVetlaahtplrGAAAREraiD---WLRRVGIPEPE--RRIDDY-------------PFQFSGG 161
Cdd:TIGR04520 84 Q------NP----DNQFV----------GATVED---DvafGLENLGVPREEmrKRVDEAlklvgmedfrdrePHLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESAD 241
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGT 219
|
....*..
gi 490704625 242 ARTFFER 248
Cdd:TIGR04520 220 PREIFSQ 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
32-252 |
1.80e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.61 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmTALALLrllpdAG--RIVGGQIELGGTDLNDLSErAMRGVrggriGIIFQEpaTSLNPV 109
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKS-TLLNLI-----AGflPPDSGRILWNGQDLTALPP-AERPV-----SMLFQE--NNLFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVGDQIveTLAAHTPLR-GAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTAL 188
Cdd:COG3840 86 LTVAQNI--GLGLRPGLKlTAEQRAQVEQALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 189 DVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHP 252
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-548 |
2.01e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 111.73 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 271 LSAQGRAADQGKAAPEAGAVVLDVQDllvhypVRKGVLRRVAawveavngVTFTLRAgeTLALLGESGCGKTTTGKALLR 350
Cdd:PRK14271 6 LGGQSGAADVDAAAPAMAAVNLTLGF------AGKTVLDQVS--------MGFPARA--VTSLMGPTGSGKTTFLRTLNR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 351 L---VEGARVQGRAMLDGHDLLgaSRRELRRLRQDIQIVFQDPfaslDP-RMRVGDILEEGIASL----RPELA-ASARR 421
Cdd:PRK14271 70 MndkVSGYRYSGDVLLGGRSIF--NYRDVLEFRRRVGMLFQRP----NPfPMSIMDNVLAGVRAHklvpRKEFRgVAQAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 422 ARAVGLLERVglpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFI 501
Cdd:PRK14271 144 LTEVGLWDAV---KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490704625 502 THNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAV 548
Cdd:PRK14271 219 THNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-235 |
2.06e-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: 108.10 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLNDLSERAMRgvrggrigiifqe 101
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 patslnpvmrvgdqivetlaahtplrgaaareraidwlRRVGipeperriddYPFQFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:cd00267 73 --------------------------------------RRIG----------YVPQLSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-236 |
2.45e-27 |
|
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: 109.42 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEpa 103
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRVGDQIVETLAAhTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:cd03292 87 FRLLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 184 PTTALDVTVQAQVLELLAGIQReMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-237 |
2.75e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 109.52 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 20 ESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLrllpdAGRIV--GGQIELGGTDLNDLSERAMRgvrggRIGI 97
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKML-----TGELRptSGTAYINGYSIRTDRKAARQ-----SLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 98 IFQEPA--TSLNPVmrvgdqivETLAAHTPLRG---AAARERAIDWLRRVGIPEPE-RRIDDYpfqfSGGQKQRLMIAIA 171
Cdd:cd03263 80 CPQFDAlfDELTVR--------EHLRFYARLKGlpkSEIKEEVELLLRVLGLTDKAnKRARTL----SGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 172 LAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
291-537 |
2.85e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.07 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVrkgvlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLG 370
Cdd:COG0410 3 MLEVENLHAGYGG-----------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL--PPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRL--------RQdiqiVFQD---------PFASLDPRMRVGDILEEgIASLRPELAasarraravgllERVGL 433
Cdd:COG0410 70 LPPHRIARLgigyvpegRR----IFPSltveenlllGAYARRDRAEVRADLER-VYELFPRLK------------ERRRQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 434 PADTptrypheFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLAD 513
Cdd:COG0410 133 RAGT-------LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIAD 204
|
250 260
....*....|....*....|....
gi 490704625 514 RIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:COG0410 205 RAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-231 |
2.87e-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: 109.16 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTAL-ALLRLLPDAGrivgGQIELGGTDLNDLSERamrgvrggrIGIIFQEPA 103
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLKPTS----GSIRVFGKPLEKERKR---------IGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRVGDQIVETLAAHTPLRG---AAARERAIDWLRRVGIPE-PERRIDdypfQFSGGQKQRLMIAIALAAEPKLL 179
Cdd:cd03235 79 IDRDFPISVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSElADRQIG----ELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALM 231
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-253 |
3.91e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 109.74 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRIVggqieLGGTDLNDLSeramrgVRGGRIGIIFQ 100
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKT----TLLRLIaglerPDSGTIL-----FGGEDATDVP------VQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EPAtsLNPVMRVGDQIVETL-AAHTPLRGAAA--RERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:cd03296 82 HYA--LFRHMTVFDNVAFGLrVKPRSERPPEAeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPY 253
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
291-527 |
4.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPvrKGVlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlG 370
Cdd:PRK13639 1 ILETRDLKYSYP--DGT--------EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT--SGEVLIKGEPI-K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRLRQDIQIVFQDP----FAsldPRmrvgdiLEEGIA--SLRPELAASARRARAVGLLERVGLpADTPTRYPHE 444
Cdd:PRK13639 68 YDKKSLLEVRKTVGIVFQNPddqlFA---PT------VEEDVAfgPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
...
gi 490704625 525 EMG 527
Cdd:PRK13639 217 KEG 219
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
317-515 |
8.62e-27 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 108.25 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLR--LVEGARVQGRAMLDGHDLLGASRRELRRLRQ-DIQIVFQdpFAS 393
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnyLPDSGRILVRHEGAWVDLAQASPREVLEVRRkTIGYVSQ--FLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDILEEgiaSLRPELAASARRARAVG-LLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:TIGR02324 101 VIPRVSALEVVAE---PLLERGVPREAARARAReLLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490704625 473 SALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRI 515
Cdd:TIGR02324 178 ASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
317-548 |
9.87e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.43 E-value: 9.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLR-QDIQIVFQDpFAsLD 395
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR--GQVLIDGVDIAKISDAELREVRrKKIAMVFQS-FA-LM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEGIAslRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:PRK10070 119 PHMTVLDNTAFGME--LAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 476 DVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRLLAAV 548
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
319-528 |
1.02e-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: 108.47 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgarVQ-GRAMLDGHDLlgasrRE--LRRLRQDIQIVFQD------ 389
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD---VSsGSILIDGQDI-----REvtLDSLRRAIGVVPQDtvlfnd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 ----------PFASlDPRM----RVGDILEEgIASLrPElaasaRRARAVGllERvGLpadtptryphEFSGGQRQRIAI 455
Cdd:cd03253 90 tigynirygrPDAT-DEEVieaaKAAQIHDK-IMRF-PD-----GYDTIVG--ER-GL----------KLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 456 ARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVeYLADRIAVMHGGRIVEMGP 528
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGT 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
318-542 |
1.09e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.97 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE---GARVQGRAMLDGHDLLgASRRELRRLRQDIQIVFQDPfaSL 394
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesEVRVEGRVEFFNQNIY-ERRVNLNRLRRQVSMVHPKP--NL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPrMRVGDILEEG--IASLRPELAASarraravGLLERVGLPADTPTRYPH-------EFSGGQRQRIAIARALAVEPKV 465
Cdd:PRK14258 100 FP-MSVYDNVAYGvkIVGWRPKLEID-------DIVESALKDADLWDEIKHkihksalDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHG-----GRIVEMGPADTVLHAPRHEM 540
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSR 251
|
..
gi 490704625 541 TQ 542
Cdd:PRK14258 252 TR 253
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
291-551 |
1.25e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPvrkgvlrrvaAWVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDL 368
Cdd:PRK13636 5 ILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKST----LFQNLNGilKPSSGRILFDGKPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 lGASRRELRRLRQDIQIVFQDPfaslDPRMRVGDILEE-GIASLRPELAASARRARAVGLLERVGLP--ADTPTrypHEF 445
Cdd:PRK13636 71 -DYSRKGLMKLRESVGMVFQDP----DNQLFSASVYQDvSFGAVNLKLPEDEVRKRVDNALKRTGIEhlKDKPT---HCL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:PRK13636 143 SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
250 260
....*....|....*....|....*.
gi 490704625 526 MGPADTVLhaPRHEMTQRLLAAVPRL 551
Cdd:PRK13636 223 QGNPKEVF--AEKEMLRKVNLRLPRI 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-217 |
2.00e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.41 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRIVggqielggtdlndLS 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIAgfLAPSSGEIT-------------LD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 ERAMRGVRGGRiGIIFQEPAtsLNPVMRVGDQIVETLAahtpLRG---AAARERAIDWLRRVGIPEPERRiddYPFQFSG 160
Cdd:COG4525 68 GVPVTGPGADR-GVVFQKDA--LLPWLNVLDNVAFGLR----LRGvpkAERRARAEELLALVGLADFARR---RIWQLSG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHD 217
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
317-527 |
2.42e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGK---ALLRLVEGarvqgRAMLDGHDLLGASrrELRRLRQDIQIVFQDPFAS 393
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALLIPSEG-----KVYVDGLDTSDEE--NLWDIRNKAGMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LdprmrVGDILEEGIAsLRPE---LAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:PRK13633 98 I-----VATIVEEDVA-FGPEnlgIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFG-VVEylADRIAVMHGGRIVEMG 527
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEeAVE--ADRIIVMDSGKVVMEG 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
13-260 |
3.12e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 110.19 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 13 LDVDV-AGESGVThavkrlqlavaqgetfALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDLNDLSERAMRG 89
Cdd:COG4148 16 LDVDFtLPGRGVT----------------ALFGPSGSGKT----TLLRAI--AGleRPDSGRIRLGGEVLQDSARGIFLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 90 VRGGRIGIIFQEPatSLNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLrrvGIpepERRIDDYPFQFSGGQKQRLMIA 169
Cdd:COG4148 74 PHRRRIGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GI---GHLLDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 170 IALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
250
....*....|.
gi 490704625 250 RHPYARELFEA 260
Cdd:COG4148 226 DLLPLAGGEEA 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
292-532 |
3.14e-26 |
|
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: 106.84 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPvRKGVLRrvaawveavnGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGA 371
Cdd:TIGR03410 1 LEVSNLNVYYG-QSHILR----------GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKS--GSIRLDGEDITKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRElrRLRQDIQIVFQ--DPFasldPRMRVGDILEEGIASLRPELAAsarraravgllervgLPADTPTRYP--HEF-- 445
Cdd:TIGR03410 68 PPHE--RARAGIAYVPQgrEIF----PRLTVEENLLTGLAALPRRSRK---------------IPDEIYELFPvlKEMlg 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 ------SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMH 519
Cdd:TIGR03410 127 rrggdlSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVME 206
|
250
....*....|...
gi 490704625 520 GGRIVEMGPADTV 532
Cdd:TIGR03410 207 RGRVVASGAGDEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
317-533 |
3.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.77 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDP---Fas 393
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ--SGEIKIDGITI---SKENLKEIRKKIGIIFQNPdnqF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 ldprmrVGDILEEGIA-SLRPELAASARRARAV-GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK13632 97 ------IGATVEDDIAfGLENKKVPPKKMKDIIdDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVeYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
316-524 |
6.58e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.42 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGhdllgaSRRELRRLRQDIQIVFQDP----- 390
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK--ESSGSILLNG------KPIKAKERRKSIGYVMQDVdyqlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FASLDPRMRVG-DILEEGIASLRpelaasarraravGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:cd03226 86 TDSVREELLLGlKELDAGNEQAE-------------TVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-251 |
6.79e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.67 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLRLLP--DAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPAT 104
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SlnPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGI-PEPERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:PRK14246 102 F--PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRH 251
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-246 |
8.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.17 E-value: 8.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVGGQIELggtdLNDLSERAMRGVRGgRIGIIFQEPAT 104
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDDITI----THKTKDKYIRPVRK-RIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNpvmrvgDQIVETLAAHTP----LRGAAARERAIDWLRRVGIPepeRRI-DDYPFQFSGGQKQRLMIAIALAAEPKLL 179
Cdd:PRK13646 97 QLF------EDTVEREIIFGPknfkMNLDEVKNYAHRLLMDLGFS---RDVmSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
316-533 |
9.65e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 105.65 E-value: 9.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLGASRRELRRlrqDIQIVFQ------- 388
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY--VPENGRVLVDGHDLALADPAWLRR---QVGVVLQenvlfnr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 389 ---DPFASLDPRMRVGDILE--------EGIASLrPELAASARRARAVGLlervglpadtptryphefSGGQRQRIAIAR 457
Cdd:cd03252 91 sirDNIALADPGMSMERVIEaaklagahDFISEL-PEGYDTIVGEQGAGL------------------SGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 458 ALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPADTVL 533
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
317-533 |
1.09e-25 |
|
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: 105.39 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPFasldp 396
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ--KGQILIDGIDIRDISRKSLRSM---IGVVLQDTF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 rMRVGDILEE-GIASLRPELAASARRARAVGLLERV-GLPADTPTrYPHE----FSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:cd03254 88 -LFSGTIMENiRLGRPNATDEEVIEAAKEAGAHDFImKLPNGYDT-VLGEnggnLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPADTVL 533
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
288-523 |
1.11e-25 |
|
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: 103.67 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 288 GAVVLDVQDLLVHYpvrkgvlrrvaawveAVNGVTFTLRAGETLALLGESGCGKTttgkALLRLVEGAR--VQGRAMLDG 365
Cdd:cd03215 1 GEPVLEVRGLSVKG---------------AVRDVSFEVRAGEIVGIAGLVGNGQT----ELAEALFGLRppASGEITLDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 366 HDLLGASRRELRRLRqdIQIVFQDpfasldpRMRVGDILEEGIAslrpelaasarraravgllERVGLPadtptrypHEF 445
Cdd:cd03215 62 KPVTRRSPRDAIRAG--IAYVPED-------RKREGLVLDLSVA-------------------ENIALS--------SLL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-264 |
1.60e-25 |
|
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: 107.19 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 42 LVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLndlSERA--MRGvrggrIGIIFQEPAtsLNPVMRVGDQIVET 119
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLAGFEQPDSGSIMLDGEDV---TNVPphLRH-----INMVFQSYA--LFPHMTVEENVAFG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 120 LAahtpLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLEL 199
Cdd:TIGR01187 67 LK----MRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 200 LAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYARELFEAIPTF 264
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVF 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-275 |
1.60e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKS--MTALALLrLLPDAGRI--VGGQIELggtdlnDLSERAMRGVRGgRIGIIFQEPATS 105
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKStlMQHFNAL-LKPSSGTItiAGYHITP------ETGNKNLKKLRK-KVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 L--NPVMrvgdQIVETLAAHTPLRGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:PRK13641 98 LfeNTVL----KDVEFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRhpYARELFEAIPT 263
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE--WLKKHYLDEPA 248
|
250
....*....|..
gi 490704625 264 FAKRGRPLSAQG 275
Cdd:PRK13641 249 TSRFASKLEKGG 260
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
318-523 |
1.66e-25 |
|
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: 103.06 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDpfasld 395
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKST----LARLILGLLrpTSGRVRLDGADI---SQWDPNELGDHVGYLPQD------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 prmrvgDILEEGiaSLRPELaasarraravgllervglpadtptrypheFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:cd03246 85 ------DELFSG--SIAENI-----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490704625 476 DVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEyLADRIAVMHGGRI 523
Cdd:cd03246 128 DVEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
315-524 |
2.17e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.21 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDP---F 391
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT--SGSVLLDGTDIRQLDPADLRR---NIGYVPQDVtlfY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLdprmrvgdilEEGIASLRPElaasARRARAVGLLERVGLPADTPtRYPHEF-----------SGGQRQRIAIARALA 460
Cdd:cd03245 92 GTL----------RDNITLGAPL----ADDERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEyLADRIAVMHGGRIV 524
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
315-522 |
2.48e-25 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 104.44 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLR--LVEGARVQGRAMLDGHDLLGASRRELRRLRQD-IQIVFQdpF 391
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPDSGSILVRHDGGWVDLAQASPREILALRRRtIGYVSQ--F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLDPRMRVGDI-----LEEGIAslRPELAASARRaravgLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVL 466
Cdd:COG4778 102 LRVIPRVSALDVvaeplLERGVD--REEARARARE-----LLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGR 522
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-259 |
2.65e-25 |
|
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: 109.86 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEglDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLS 83
Cdd:COG4987 330 GGPSLELE--DVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 ERAMRGvrggRIGIIFQEP---ATSLNPVMRVGdqivetlaahtplRGAAARERAIDWLRRVGIPE-----PER---RID 152
Cdd:COG4987 404 EDDLRR----RIAVVPQRPhlfDTTLRENLRLA-------------RPDATDEELWAALERVGLGDwlaalPDGldtWLG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVALMR 232
Cdd:COG4987 467 EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLE 543
|
250 260
....*....|....*....|....*..
gi 490704625 233 GGEIVESADARTFFErpRHPYARELFE 259
Cdd:COG4987 544 DGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-242 |
2.66e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.05 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVagesGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLS--ER 85
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPphER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGvrggrIGIIFQEPAtsLNPVMRVGDQIVetLAAHTplRGAAARERAIDWLRRVgIPEPERRIDDYPFQFSGGQKQR 165
Cdd:cd03224 73 ARAG-----IGYVPEGRR--IFPELTVEENLL--LGAYA--RRRAKRKARLERVYEL-FPRLKERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADA 242
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
321-527 |
2.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTTGK---ALLRLVEGARVQGRAMLDGhdllGASRRELRRLRQDIQIVFQDPFASLDPR 397
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQhlnGLLQPTSGTVTIGERVITA----GKKNKKLKPLRKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDIL----------EEGIASLRPelaasarraravgLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLI 467
Cdd:PRK13634 102 TVEKDICfgpmnfgvseEDAKQKARE-------------MIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 468 CDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-237 |
4.67e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.19 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGrivggQIELGGTDLNDLSERamrgvrggRIGIIFQEP 102
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSG-----EVLWDGEPLDPEDRR--------RIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 atSLNPVMRVGDQIVeTLAAhtpLRG---AAARERAIDWLRRVGIPE-PERRIDDypfqFSGGQKQRLMIAIALAAEPKL 178
Cdd:COG4152 81 --GLYPKMKVGEQLV-YLAR---LKGlskAEAKRRADEWLERLGLGDrANKKVEE----LSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 179 LIADEPTTALD-VTVQAQVLELLAgiQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:COG4152 151 LILDEPFSGLDpVNVELLKDVIRE--LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-239 |
4.78e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.10 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALL-RLLPdagrIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEP-- 102
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKS-TLVNLLlRFYD----PTSGRILIDGVDIRDLTLESLRR----QIGVVPQDTfl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 --ATslnpvmrVGDQIveTLAahtplRGAAARERAIDWLRRVGIpepERRIDDYPFQF-----------SGGQKQRLMIA 169
Cdd:COG1132 426 fsGT-------IRENI--RYG-----RPDATDEEVEEAAKAAQA---HEFIEALPDGYdtvvgergvnlSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 170 IALAAEPKLLIADEPTTALDVTVQAQVLEllaGIQREM-GMAVLLITHDLAVVRNvAHHVALMRGGEIVES 239
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQE---ALERLMkGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
291-542 |
4.82e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKgvlrrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALLR---LVEGARVQGRAMLDGHD 367
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPEVTITGSIVYNGHN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 368 LLGaSRRELRRLRQDIQIVFQ--DPFASldprmrvgDILEEGIASLRpeLAASARRARAVGLLERVGLPA---DTPTRYP 442
Cdd:PRK14239 74 IYS-PRTDTVDLRKEIGMVFQqpNPFPM--------SIYENVVYGLR--LKGIKDKQVLDEAVEKSLKGAsiwDEVKDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 443 HE----FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVM 518
Cdd:PRK14239 143 HDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFF 220
|
250 260
....*....|....*....|....
gi 490704625 519 HGGRIVEMGPADTVLHAPRHEMTQ 542
Cdd:PRK14239 221 LDGDLIEYNDTKQMFMNPKHKETE 244
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
283-527 |
6.22e-25 |
|
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: 108.63 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 283 AAPEAGAVVLDvqDLLVHYPVRKGVLrrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAM 362
Cdd:TIGR02204 331 PVPLRGEIEFE--QVNFAYPARPDQP--------ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQ--SGRIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 363 LDGHDLLGASRRELRrlrQDIQIVFQDP---FASLDPRMRVG-------DILEEGIASLRPELAASARRARAVGLLER-V 431
Cdd:TIGR02204 399 LDGVDLRQLDPAELR---ARMALVPQDPvlfAASVMENIRYGrpdatdeEVEAAARAAHAHEFISALPEGYDTYLGERgV 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 432 GLpadtptryphefSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYl 511
Cdd:TIGR02204 476 TL------------SGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK- 540
|
250
....*....|....*.
gi 490704625 512 ADRIAVMHGGRIVEMG 527
Cdd:TIGR02204 541 ADRIVVMDQGRIVAQG 556
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-236 |
6.42e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.36 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQepA 103
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKS----TLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRVgdqiVETLAahTPL-----RGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:PRK11629 96 HHLLPDFTA----LENVA--MPLligkkKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVAlMRGGEI 236
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
318-530 |
8.95e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.17 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALL-RLVEGARVQGRAMLDGHDLLGASRrELRRlrqdIQIVFQDPFasLDP 396
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAFSASGEVLLNGRRLTALPA-EQRR----IGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEEGiasLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:COG4136 90 HLSVGENLAFA---LPPTIGRAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490704625 477 VSVQAQILDLLRDLQAELGIAYLFITHnfgvveylaDRIAVMHGGRIVEMGPAD 530
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTH---------DEEDAPAAGRVLDLGNWQ 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
318-540 |
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 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGhdllgasrRELRRLRQDIQIVFQDpfASLD 395
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST----LLNLISGLAqpTSGGVILEG--------KQITEPGPDRMVVFQN--YSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEGIASLRPELAASARRARAVGLLERVGLPAdTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTE-AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 476 DVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTV-LHAPRHEM 540
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDRL 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-237 |
9.45e-25 |
|
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: 101.95 E-value: 9.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 9 RIEGLDVdvaGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNdlseramR 88
Cdd:cd03226 1 RIENISF---SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKT----TLAKILAGLIKESSGSILLNGKPIK-------A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 89 GVRGGRIGIIFQEPATSLNPVmRVGDQIVETLAAhtplrGAAARERAIDWLRRVGIPEPErriDDYPFQFSGGQKQRLMI 168
Cdd:cd03226 67 KERRKSIGYVMQDVDYQLFTD-SVREELLLGLKE-----LDAGNEQAETVLKDLDLYALK---ERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 169 AIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
317-527 |
9.78e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.12 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDP--FA-S 393
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ--SGRILIDGTDIRTVTRASLRR---NIAVVFQDAglFNrS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVG--DILEEgiaslrpELAASARRARAVGLLERVGLPADTPT-RYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:PRK13657 425 IEDNIRVGrpDATDE-------EMRAAAERAQAHDFIERKPDGYDTVVgERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMG 527
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
317-532 |
1.03e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.42 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRR------ELRRLRqdiqivfqdp 390
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD--SGEVLWDGEPLDPEDRRrigylpEERGLY---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 fasldPRMRVGDIL-----------EEGIASLRpelaasarraravGLLERVGLP--ADTPTRyphEFSGGQRQRIAIAR 457
Cdd:COG4152 84 -----PKMKVGEQLvylarlkglskAEAKRRAD-------------EWLERLGLGdrANKKVE---ELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 458 ALAVEPKVLICDEPTSALD-VSVQAqILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTV 532
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
27-230 |
1.16e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.79 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGRIVGGQIELGGTDLNDLSERAmrgvRggRIGIIFQEPAtsL 106
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIAGTLSPAFSASGEVLLNGRRLTALPAEQ----R--RIGILFQDDL--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 NPVMRVGDQIVETLAAHTPlrGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTT 186
Cdd:COG4136 88 FPHLSVGENLAFALPPTIG--RAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490704625 187 ALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-264 |
1.17e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGEsgvtHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDL 82
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 S--ERAmrgvrggrIGIIFQEPAtsLNPVMRVGDQIVETLAaHTPLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSG 160
Cdd:PRK11607 87 PpyQRP--------INMMFQSYA--LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQV-LELLAGIQReMGMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|....*
gi 490704625 240 ADARTFFERPRHPYARELFEAIPTF 264
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGSVNVF 256
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
307-523 |
1.21e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 102.10 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 307 VLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLRQDIQIV 386
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDVSDLRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 387 FQDpFASLDPR---------MRVGDILEEGIASLRPELaasarraravglLERVGLpADTPTRYPHEFSGGQRQRIAIAR 457
Cdd:cd03292 84 FQD-FRLLPDRnvyenvafaLEVTGVPPREIRKRVPAA------------LELVGL-SHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 458 ALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
315-527 |
1.23e-24 |
|
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: 101.97 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLRQDiqivfqdpfASL 394
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS--GEVLFDGKPLDIAARNRIGYLPEE---------RGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEgIASLRpELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:cd03269 82 YPKMKVIDQLVY-LAQLK-GLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 475 LDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
278-528 |
1.26e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 107.88 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 278 ADQGKAAPEAGAVVLDVQDLLVHYPVRKgvlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArv 357
Cdd:TIGR02203 317 KDTGTRAIERARGDVEFRNVTFRYPGRD---------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 358 QGRAMLDGHDLLGASRRELRR----LRQDIqIVFQDPFASldpRMRVGDILEEGIASLRPELAASARRAravgLLERVGL 433
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRqvalVSQDV-VLFNDTIAN---NIAYGRTEQADRAEIERALAAAYAQD----FVDKLPL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 434 PADTPT-RYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYlA 512
Cdd:TIGR02203 458 GLDTPIgENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-A 534
|
250
....*....|....*.
gi 490704625 513 DRIAVMHGGRIVEMGP 528
Cdd:TIGR02203 535 DRIVVMDDGRIVERGT 550
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-527 |
1.27e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.80 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 324 TLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGA--SRRELRRLRQDIQI-----VFQDPFASL 394
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKST----LLNLIAGFETpqSGRVLINGVDVTAAppADRPVSMLFQENNLfahltVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIAslrpelaasarraravGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:cd03298 96 SPGLKLTAEDRQAIE----------------VALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 475 LDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
317-549 |
1.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKaLLR--LVEGARVQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPfasl 394
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISK-LINglLLPDDNPNSKITVDGITL---TAKTVWDIREKVGIVFQNP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMrVGDILEEGIA-------SLRPELAASARRaravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLI 467
Cdd:PRK13640 94 DNQF-VGATVGDDVAfglenraVPRPEMIKIVRD-----VLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 468 CDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEyLADRIAVMHGGRIVEMG-PADTVlhaPRHEMTQRLLA 546
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGsPVEIF---SKVEMLKEIGL 242
|
...
gi 490704625 547 AVP 549
Cdd:PRK13640 243 DIP 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-237 |
1.58e-24 |
|
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: 101.59 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGrivggQIELGGTDLNDLSERamrgvrggRIGIIFQ 100
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSG-----EVLFDGKPLDIAARN--------RIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EpaTSLNPVMRVGDQIVeTLAAHTPLRGAAARERAIDWLRRVGIPE-PERRIDdypfQFSGGQKQRLMIAIALAAEPKLL 179
Cdd:cd03269 78 E--RGLYPKMKVIDQLV-YLAQLKGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 180 IADEPTTALDVtVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03269 151 ILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
30-217 |
2.20e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.78 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGrivGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQepATSLNPV 109
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS---SGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQ--SFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVgdqiVETLAAHTPLRGAA---ARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTT 186
Cdd:PRK10584 103 LNA----LENVELPALLRGESsrqSRNGAKALLEQLGLGK---RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 490704625 187 ALDVTVQAQVLELLAGIQREMGMAVLLITHD 217
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
30-217 |
3.66e-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: 100.25 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSMtalaLLRLLpdAG--RIVGGQIELGGTDLNDLSERAmrgvrGGRIGIIFQEPAtsLN 107
Cdd:COG4133 21 LSFTLAAGEALALTGPNGSGKTT----LLRIL--AGllPPSAGEVLWNGEPIRDAREDY-----RRRLAYLGHADG--LK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 108 PVMRVgdqiVETLAAHTPLRGAAARERAID-WLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTT 186
Cdd:COG4133 88 PELTV----RENLRFWAALYGLRADREAIDeALEAVGL---AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|.
gi 490704625 187 ALDVTVQAQVLELLAGiQREMGMAVLLITHD 217
Cdd:COG4133 161 ALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
317-527 |
4.46e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 100.35 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGeTLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLLgASRRELRRLrqdIQIVFQDPfaSL 394
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTT----LMRILATLTppSSGTIRIDGQDVL-KQPQKLRRR---IGYLPQEF--GV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEgIASLRpELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:cd03264 84 YPNFTVREFLDY-IAWLK-GIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 475 LDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-249 |
4.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.41 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRI-VGGQIELGGTDLNDLseRAMRGvrggRIGIIFQEP 102
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKS-TLLQHLNglLQPTSGTVtIGERVITAGKKNKKL--KPLRK----KVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLNpvmrvgDQIVETLAAHTPL----RGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:PRK13634 95 EHQLF------EETVEKDICFGPMnfgvSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-261 |
5.65e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.69 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGrivggQIELGGTDLnDLSERAMRGVRGgRIGIIFQEP 102
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSG-----EVLIKGEPI-KYDKKSLLEVRK-TVGIVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 atslnpvmrvGDQI----VETLAAHTPLRGAAARE----RAIDWLRRVGIPEPERRIddyPFQFSGGQKQRLMIAIALAA 174
Cdd:PRK13639 88 ----------DDQLfaptVEEDVAFGPLNLGLSKEevekRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP----- 249
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIetirk 233
|
250
....*....|....*
gi 490704625 250 ---RHPYARELFEAI 261
Cdd:PRK13639 234 anlRLPRVAHLIEIL 248
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-249 |
7.56e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRivGGQIELGGTDLNdlsERAMRGVRGgRIGIIFQEPA 103
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKS-TISKLINglLLPDDNP--NSKITVDGITLT---AKTVWDIRE-KVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLnpvmrVGDQIVETLAAHTPLRGAAaRERAI----DWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPKLL 179
Cdd:PRK13640 95 NQF-----VGATVGDDVAFGLENRAVP-RPEMIkivrDVLADVGMLD---YIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVrNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-251 |
9.69e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.37 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL---PDAGriVGGQIELGGTDLNDLSERAMRGvrggRIGII 98
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelyPEAR--VSGEVYLDGQDIFKMDVIELRR----RVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 99 FQEPatslNPVMRVgdQIVETLAAHTPL------------RGAAARERAIDWlrrvgiPEPERRIDDYPFQFSGGQKQRL 166
Cdd:PRK14247 88 FQIP----NPIPNL--SIFENVALGLKLnrlvkskkelqeRVRWALEKAQLW------DEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
....*
gi 490704625 247 ERPRH 251
Cdd:PRK14247 234 TNPRH 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-550 |
1.09e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.61 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEGLDVDVAGesgvthaVKRLQ---LAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLN 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG-------VKALDdisFDCRAGQVHALMGENGAGKS----TLLKILSGNYQPDAGSILIDGQEMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 DLSERAmrGVRGGrIGIIFQEpaTSLNPVMRVGDQIvetLAAHTPLRG-----AAARERAIDWLRRVGIP-EPERRIDDy 154
Cdd:PRK11288 70 FASTTA--ALAAG-VAIIYQE--LHLVPEMTVAENL---YLGQLPHKGgivnrRLLNYEAREQLEHLGVDiDPDTPLKY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 155 pfqFSGGQKQRLMIAIALAAEPKLLIADEPTTALdvtvQAQVLELLAGIQREM---GMAVLLITHdlavvrnvahhvalm 231
Cdd:PRK11288 141 ---LSIGQRQMVEIAKALARNARVIAFDEPTSSL----SAREIEQLFRVIRELraeGRVILYVSH--------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 232 RGGEIVESADARTFFERPRHpyarelfeaIPTFAK-----RGRPLSAQ-GRAADQ--GKAAPEAGAVVLDVQDLL---VH 300
Cdd:PRK11288 199 RMEEIFALCDAITVFKDGRY---------VATFDDmaqvdRDQLVQAMvGREIGDiyGYRPRPLGEVRLRLDGLKgpgLR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 301 YPvrkgvlrrvaawveavngVTFTLRAGETLALLGESGCGKTttgkALLRLVEGA--RVQGRAMLDGHDLLGASRRE--- 375
Cdd:PRK11288 270 EP------------------ISFSVRAGEIVGLFGLVGAGRS----ELMKLLYGAtrRTAGQVYLDGKPIDIRSPRDair 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 376 -----------------LRRLRQDIQIV---FQDPFASLDPRMRVGDILEEGIASLrpelaasarraravglleRVGLP- 434
Cdd:PRK11288 328 agimlcpedrkaegiipVHSVADNINISarrHHLRAGCLINNRWEAENADRFIRSL------------------NIKTPs 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 435 ADTPTRYpheFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADR 514
Cdd:PRK11288 390 REQLIMN---LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADR 465
|
570 580 590
....*....|....*....|....*....|....*..
gi 490704625 515 IAVMHGGRIvemgpADTVLHAPRHEmtQRLL-AAVPR 550
Cdd:PRK11288 466 IVVMREGRI-----AGELAREQATE--RQALsLALPR 495
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-529 |
1.11e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.59 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 17 VAGESGVTH------AVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIE-LGGtdlnDLSERAMRG 89
Cdd:NF033858 1 VARLEGVSHrygktvALDDVSLDIPAGCMVGLIGPDGVGKS----SLLSLIAGARKIQQGRVEvLGG----DMADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 90 VRGGRIGIIFQEPATSLNPVMRVgdqiVETLAAHTPLRGAAARERaidwlrrvgipepERRIDD-------YPF------ 156
Cdd:NF033858 73 AVCPRIAYMPQGLGKNLYPTLSV----FENLDFFGRLFGQDAAER-------------RRRIDEllratglAPFadrpag 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREM-GMAVLlithdlavvrnVA---------- 225
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVL-----------VAtaymeeaerf 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 226 HHVALMRGGEIVESADARTFFERPRHPYARELFEA-IPTFAKRG-RPLSAQGRAADQGKA-APEAgavvldvqdllvhyp 302
Cdd:NF033858 205 DWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAlLPEEKRRGhQPVVIPPRPADDDDEpAIEA--------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 303 vrKGVLRRVAAWVeAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLV---EG-ARVQGRAmLDGHDLlgASRR---- 374
Cdd:NF033858 270 --RGLTMRFGDFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLpasEGeAWLFGQP-VDAGDI--ATRRrvgy 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 375 ---------ELrRLRQDIQI---VFQDPFASLDPRMRvgdileegiaslrpelaasarraravGLLERVGLpADTPTRYP 442
Cdd:NF033858 344 msqafslygEL-TVRQNLELharLFHLPAAEIAARVA--------------------------EMLERFDL-ADVADALP 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 443 HEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAyLFI-THNFGVVEyLADRIAVMHGG 521
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAE-RCDRISLMHAG 473
|
....*....
gi 490704625 522 RIVEMG-PA 529
Cdd:NF033858 474 RVLASDtPA 482
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
316-527 |
1.27e-23 |
|
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: 98.83 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGhdllgasrrelrrlrqdiqivfQDPFASLD 395
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI--KPDSGEITFDG----------------------KSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEGIasLRPELAAS---ARRARAVGL--------LERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPK 464
Cdd:cd03268 70 ALRRIGALIEAPG--FYPNLTARenlRLLARLLGIrkkridevLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
316-527 |
2.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.47 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARVQ--GRAMLDGHDLLGASRR--ELRRLRQDIQIVFQDPF 391
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKST----MIQLTNGLIISetGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLdprmrVGDILEEGIASLRPELAASARRA--RAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:PRK13645 101 YQL-----FQETIEKDIAFGPVNLGENKQEAykKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
281-523 |
2.36e-23 |
|
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: 98.70 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 281 GKAAPEAGAVVLDVQDLLVHYPVRKGVLrrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGR 360
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTL--------VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ--GGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 361 AMLDGHDLlgaSRRELRRLRQDIQIVFQDP--FASldprmRVGDILEEGIASLR----PELAASARRARAVGLLERvGLP 434
Cdd:cd03248 71 VLLDGKPI---SQYEHKYLHSKVSLVGQEPvlFAR-----SLQDNIAYGLQSCSfecvKEAAQKAHAHSFISELAS-GYD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 435 ADTPTRyPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELgiAYLFITHNFGVVEYlADR 514
Cdd:cd03248 142 TEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQ 217
|
....*....
gi 490704625 515 IAVMHGGRI 523
Cdd:cd03248 218 ILVLDGGRI 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
319-530 |
2.38e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALLRLvEGARV-QGRAMLDGHDLLGASRRElrRLRQDIQIVFQDPFASldPR 397
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKYEVtSGSILLDGEDILELSPDE--RARAGIFLAFQYPVEI--PG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEEGIASLR-PELAASARRARAVGLLERVGLPADTPTRYPHE-FSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:COG0396 92 VSVSNFLRTALNARRgEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 476 DV-SVQ--AQILDLLRDlqAELGIayLFITHNFGVVEYL-ADRIAVMHGGRIVEMGPAD 530
Cdd:COG0396 172 DIdALRivAEGVNKLRS--PDRGI--LIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
305-524 |
2.92e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.56 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 305 KGVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGhdLLGASRRelRRLRQDIQ 384
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT--SGEVRVAG--LVPWKRR--KKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 385 IVF-QDPFASLDPRMRVGDILEEGIASLRPElAASARRARAVGLLErVGLPADTPTRyphEFSGGQRQRIAIARALAVEP 463
Cdd:cd03267 98 VVFgQKTQLWWDLPVIDSFYLLAAIYDLPPA-RFKKRLDELSELLD-LEELLDTPVR---QLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
3.26e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.40 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGESgvthAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPD--AGRIVGGQIELGGTDLn 80
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKT----VLDQVSMGFPARAVTSLMGPTGSGKT-TFLRTLNRMNDkvSGYRYSGDVLLGGRSI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 dLSERAMRGVRGgRIGIIFQEPatslNPV-MRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPER-RIDDYPFQF 158
Cdd:PRK14271 91 -FNYRDVLEFRR-RVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
250
....*....|...
gi 490704625 239 SADARTFFERPRH 251
Cdd:PRK14271 243 EGPTEQLFSSPKH 255
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-242 |
3.71e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.60 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGES---GVThavkrlqLAVAQGETFALVGESGSGKSMTALALlrllpdAGR----IVGGQIELGGTDLN 80
Cdd:COG0396 1 LEIKNLHVSVEGKEilkGVN-------LTIKPGEVHAIMGPNGSGKSTLAKVL------MGHpkyeVTSGSILLDGEDIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 DLS--ERAMRGvrggrIGIIFQepatslNPV----MRVGDQIVETLAAHT--PLRGAAARERAIDWLRRVGIPE--PERR 150
Cdd:COG0396 68 ELSpdERARAG-----IFLAFQ------YPVeipgVSVSNFLRTALNARRgeELSAREFLKLLKEKMKELGLDEdfLDRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 151 IDDypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVtvqaQVLELLA-GIQ--REMGMAVLLITHDLAVVR-NVAH 226
Cdd:COG0396 137 VNE---GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI----DALRIVAeGVNklRSPDRGILIITHYQRILDyIKPD 209
|
250
....*....|....*.
gi 490704625 227 HVALMRGGEIVESADA 242
Cdd:COG0396 210 FVHVLVDGRIVKSGGK 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
289-543 |
3.89e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 289 AVVLDVQDLLVHYPVRKGVLRRVAAW-----------VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGA-- 355
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKELllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKST----LLKLIAGIle 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 356 ------RVQGR--AMLD----------GHD-------LLGASRRELRRLRQDIQivfqDpFASLdprmrvGDILeegias 410
Cdd:COG1134 78 ptsgrvEVNGRvsALLElgagfhpeltGREniylngrLLGLSRKEIDEKFDEIV----E-FAEL------GDFI------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 411 lrpelaasarraravgllervglpaDTPTRYpheFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDL 490
Cdd:COG1134 141 -------------------------DQPVKT---YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 491 QAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQR 543
Cdd:COG1134 193 RES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGR 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-239 |
4.59e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.12 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGrivGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEP--- 102
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPQ---SGRILIDGTDIRTVTRASLRR----NIAVVFQDAglf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLNPVMRVGdqivETLAAHTPLRGAAARERAIDWLrrvgipepERRIDDYPF-------QFSGGQKQRLMIAIALAAE 175
Cdd:PRK13657 422 NRSIEDNIRVG----RPDATDEEMRAAAERAQAHDFI--------ERKPDGYDTvvgergrQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVALMRGGEIVES 239
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
315-551 |
6.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPfa 392
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKST----LFRHFNGilKPTSGSVLIRGEPITKENIREVRKF---VGLVFQNP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 slDPRMrVGDILEEGIA--SLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDE 470
Cdd:PRK13652 88 --DDQI-FSPTVEQDIAfgPINLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 471 PTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRL-LAAVP 549
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLdLPSLP 243
|
..
gi 490704625 550 RL 551
Cdd:PRK13652 244 KL 245
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
318-533 |
6.72e-23 |
|
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: 102.43 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGA--RVQGRAMLDGHDLLGASRRELRR----LRQDIQIvFQDPF 391
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKST----LARLIVGIwpPTSGSVRLDGADLKQWDRETFGKhigyLPQDVEL-FPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLDPRMRVGDILEEGIASLRpelaasarrarAVGLLErvgLPADTPTRYPHE-------FSGGQRQRIAIARALAVEPK 464
Cdd:TIGR01842 409 AENIARFGENADPEKIIEAAK-----------LAGVHE---LILRLPDGYDTVigpggatLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEyLADRIAVMHGGRIVEMGPADTVL 533
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVL 541
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
322-533 |
7.23e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 322 TFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDG--HDLLGASRRElrrlrqdIQIVFQDP--FASLD 395
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKST----LLNLIAGflTPASGSLTLNGqdHTTTPPSRRP-------VSMLFQENnlFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEGI---ASLRPELAAsarraravgLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PRK10771 88 VAQNIGLGLNPGLklnAAQREKLHA---------IARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
292-533 |
7.33e-23 |
|
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: 102.52 E-value: 7.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRKGVLrrvaawveaVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGA 371
Cdd:COG4618 331 LSVENLTVVPPGSKRPI---------LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA--GSVRLDGADLSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRR----LRQDIQIV----------FQDPfaslDPR------MRVGdiLEEGIASLrPElaasarraravGLLERV 431
Cdd:COG4618 400 DREELGRhigyLPQDVELFdgtiaeniarFGDA----DPEkvvaaaKLAG--VHEMILRL-PD-----------GYDTRI 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 432 GlPADTPtrypheFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEyL 511
Cdd:COG4618 462 G-EGGAR------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-A 532
|
250 260
....*....|....*....|..
gi 490704625 512 ADRIAVMHGGRIVEMGPADTVL 533
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
318-523 |
1.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTgkalLRLVEGARV--QGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPfaslD 395
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLLEaeSGQIIIDGDLL---TEENVWDIRHKIGMVFQNP----D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMrVGDILEEGIA-SLRPE-LAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK13650 92 NQF-VGATVEDDVAfGLENKgIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEyLADRIAVMHGGRI 523
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
317-532 |
1.25e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKaLLRLVEGARvQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDP---FAS 393
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-LMIGIEKVK-SGEIFYNNQAI---TDDNFEKLRKHIGIVFQNPdnqFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDILEEGIASLRPELAASARRARAVGLLERvglpADTPtryPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK13648 99 SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLER----ADYE---PNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAYLFITHNfgVVEYL-ADRIAVMHGGRIVEMGPADTV 532
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHD--LSEAMeADHVIVMNKGTVYKEGTPTEI 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-503 |
1.31e-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: 96.01 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLlgasRRELRRLRQDIQIVFQDPfaSLDPR 397
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTT----LLRILAGLLppSAGEVLWNGEPI----RDAREDYRRRLAYLGHAD--GLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEeGIASLRPELAASARRARavgLLERVGLP--ADTPTRYpheFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:COG4133 90 LTVRENLR-FWAALYGLRADREAIDE---ALEAVGLAglADLPVRQ---LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*...
gi 490704625 476 DVSVQAQILDLLRDLQAELGIAyLFITH 503
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAV-LLTTH 189
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
316-533 |
1.44e-22 |
|
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: 102.13 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPFasld 395
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR--SGEILLNGFSLKDIDRHTLRQF---INYLPQEPY---- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 prMRVGDILEEGIASLRPELAASARRARavglLERVGLPADT---PTRYPHEF-------SGGQRQRIAIARALAVEPKV 465
Cdd:TIGR01193 559 --IFSGSILENLLLGAKENVSQDEIWAA----CEIAEIKDDIenmPLGYQTELseegssiSGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAELGIaylFITHNFGVVEyLADRIAVMHGGRIVEMGPADTVL 533
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDKTII---FVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
321-525 |
1.65e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTTGK---ALLRLVEGARvqgrAMLDGHDLLGASRRELRRLRQDIQIVFQDPFASLDPR 397
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQhfnALLKPSSGTI----TIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILeegIASLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:PRK13641 102 TVLKDVE---FGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490704625 478 SVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-250 |
1.84e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.20 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDVagesGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLS- 83
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 -ERAMRGV------RGgrigiIFQEpatslnpvMRVGDQIVetLAAHTpLRGAAARERAIDWLRRVgIPEPERRIDDYPF 156
Cdd:COG0410 73 hRIARLGIgyvpegRR-----IFPS--------LTVEENLL--LGAYA-RRDRAEVRADLERVYEL-FPRLKERRRQRAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRI 214
|
250
....*....|....
gi 490704625 237 VESADARTFFERPR 250
Cdd:COG0410 215 VLEGTAAELLADPE 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
22-236 |
1.86e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRgvrggrIGIIFQE 101
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK------VGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 PAtsLNPVMRVGDQI---VETLAAHTPLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:PRK10851 83 YA--LFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-246 |
2.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 18 AGESGVTHAVKRLQLAVAQGETFALVGESGSGKS-----MTALallrLLPDAGR-IVGGqieLGGTDLNDLSEramrgVR 91
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKStiakhMNAL----LIPSEGKvYVDG---LDTSDEENLWD-----IR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 92 GgRIGIIFQepatslNPVMRVGDQIVETLAAHTP----LRGAAARERAIDWLRRVGIPEPERRIddyPFQFSGGQKQRLM 167
Cdd:PRK13633 85 N-KAGMVFQ------NPDNQIVATIVEEDVAFGPenlgIPPEEIRERVDESLKKVGMYEYRRHA---PHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 168 IAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESADARTFF 246
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
316-524 |
2.32e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.71 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPFAS 393
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICGIErpSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDILEEGIASLRPElaasARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGD----DIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490704625 474 ALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:PRK10908 167 NLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
316-527 |
3.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASR-RELRRLRQDIQIVFQDPFASL 394
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT--TGTVTVDDITITHKTKdKYIRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 dprmrVGDILEEGIAsLRPE---LAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK13646 99 -----FEDTVEREII-FGPKnfkMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
269-518 |
3.76e-22 |
|
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: 100.05 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 269 RPLSAQGRAADQGKAAPEAGAVVLDVQDLLVhyPVRKGVLRRVAAWVE-------------AVNGVTFTLRAGETLALLG 335
Cdd:TIGR02857 278 RQLGAQYHARADGVAAAEALFAVLDAAPRPL--AGKAPVTAAPASSLEfsgvsvaypgrrpALRPVSFTVPPGERVALVG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 336 ESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPFasldprMRVGDILEEgIASLRPEL 415
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFVDPTE--GSIAVNGVPLADADADSWRDQ---IAWVPQHPF------LFAGTIAEN-IRLARPDA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 416 AAS--ARRARAVGLLERV-GLPADTPTRY---PHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRD 489
Cdd:TIGR02857 424 SDAeiREALERAGLDEFVaALPQGLDTPIgegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
250 260
....*....|....*....|....*....
gi 490704625 490 LQAelGIAYLFITHNFGVVEyLADRIAVM 518
Cdd:TIGR02857 504 LAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
318-525 |
4.85e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.78 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRelrRLRQDIQIVFQDPfasldpr 397
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS--GTLLFEGEDISTLKPE---IYRQQVSYCAQTP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGD------ILEEGIASLRPELAASARRaravglLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK10247 91 TLFGDtvydnlIFPWQIRNQQPDPAIFLDD------LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYlADRIAVM--HGGRIVE 525
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHAGEMQE 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-246 |
6.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVGGQIELGGTDLNdlseraMRGVRGgRIGIIFQEP 102
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGVDITDKKVK------LSDIRK-KVGLVFQYP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLNpvmrvgDQIVETLAAHTP----LRGAAARERAIDWLRRVGIPEpERRIDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:PRK13637 93 EYQLF------EETIEKDIAFGPinlgLSEEEIENRVKRAMNIVGLDY-EDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
316-534 |
8.00e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 93.36 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDLLGASRRElrRLRQDIQIVFQDPFASld 395
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQYPPEI-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILeegiaslrpelaasarraravgllervglpadtptRYPHE-FSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:cd03217 90 PGVKNADFL-----------------------------------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 475 LDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYL-ADRIAVMHGGRIVEMGPADTVLH 534
Cdd:cd03217 135 LDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
317-554 |
8.87e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLR-------LVEGARVQGRAMLDGHDLLgASRRELRRLRQDIQIVFQ- 388
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKST----ILRcfnrlndLIPGFRVEGKVTFHGKNLY-APDVDPVEVRRRIGMVFQk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 389 -DPFA-------SLDPRMR--VGDILEEGIASLRpelaasarrarAVGLLERVglpADTPTRYPHEFSGGQRQRIAIARA 458
Cdd:PRK14243 100 pNPFPksiydniAYGARINgyKGDMDELVERSLR-----------QAALWDEV---KDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 459 LAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYLADRIAVMHG---------GRIVEMGPA 529
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRT 243
|
250 260
....*....|....*....|....*
gi 490704625 530 DTVLHAPRHEMTQRLLAAvprlRFG 554
Cdd:PRK14243 244 EKIFNSPQQQATRDYVSG----RFG 264
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-239 |
9.14e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 94.77 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAGRI---VGGQIEL-----GGT 77
Cdd:COG1119 2 PLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI--TGDLpptYGNDVRLfgerrGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 78 DLNDLseRAmrgvrggRIGIIFQEPATSLNPVMRVGDQIV----ETLAAHTPLrGAAARERAIDWLRRVGIpepERRIDD 153
Cdd:COG1119 72 DVWEL--RK-------RIGLVSPALQLRFPRDETVLDVVLsgffDSIGLYREP-TDEQRERARELLELLGL---AHLADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 154 YPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRG 233
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218
|
....*.
gi 490704625 234 GEIVES 239
Cdd:COG1119 219 GRVVAA 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
291-542 |
9.21e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.54 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVRKGVlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLLG 370
Cdd:PRK13642 4 ILEVENLVFKYEKESDV--------NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE--EFEGKVKIDGELLTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRlrqDIQIVFQDPFASLdprmrVGDILEEGIAslrpeLAASARRARAVGLLERV--GLPA----DTPTRYPHE 444
Cdd:PRK13642 74 ENVWNLRR---KIGMVFQNPDNQF-----VGATVEDDVA-----FGMENQGIPREEMIKRVdeALLAvnmlDFKTREPAR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYlADRIAVMHGGRIV 524
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
250
....*....|....*....
gi 490704625 525 -EMGPADtvLHAPRHEMTQ 542
Cdd:PRK13642 220 kEAAPSE--LFATSEDMVE 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
317-527 |
1.05e-21 |
|
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: 92.38 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRelrrLRQDIQIVFQDPFasl 394
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKST----LLQLLTGDLKpqQGEITLDGVPVSDLEKA----LSSLISVLNQRPY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 dprmrvgdileegiaslrpelaasarrARAVGLLERVGLPadtptrypheFSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:cd03247 86 ---------------------------LFDTTLRNNLGRR----------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 475 LDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYlADRIAVMHGGRIVEMG 527
Cdd:cd03247 129 LDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-237 |
1.21e-21 |
|
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: 91.72 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLLpdAGRIV--GGQIELGGTDLNDLSERAMRgvrggRIGIif 99
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKS-T---LMKIL--SGLYKpdSGEILVDGKEVSFASPRDAR-----RAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 qepatslnpvmrvgdQIVetlaahtplrgaaareraidwlrrvgipeperriddypFQFSGGQKQRLMIAIALAAEPKLL 179
Cdd:cd03216 78 ---------------AMV--------------------------------------YQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
319-527 |
1.21e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 98.74 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgarVQ-GRAMLDGHDLlgasrRELRR--LRQDIQIVFQD------ 389
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD---VTsGRILIDGQDI-----RDVTQasLRAAIGIVPQDtvlfnd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 ----------PFASLDPRMRVGDI--LEEGIASLrPElaasaRRARAVGllERvGLpadtptryphEFSGGQRQRIAIAR 457
Cdd:COG5265 447 tiayniaygrPDASEEEVEAAARAaqIHDFIESL-PD-----GYDTRVG--ER-GL----------KLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 458 ALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAE---LGIAYLFIThnfgVVEylADRIAVMHGGRIVEMG 527
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGrttLVIAHRLST----IVD--ADEILVLEAGRIVERG 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
285-527 |
1.24e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 93.25 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 285 PEAGAVvlDVQDLLVHY-PVRKGVLRrvaawveavnGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAML 363
Cdd:cd03369 2 PEHGEI--EVENLSVRYaPDLPPVLK----------NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE--EGKIEI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 364 DGHDLlgaSRRELRRLRQDIQIVFQDP--FA-----SLDPRMRVGDilEEGIASLRpelaasarraravglLERVGLpad 436
Cdd:cd03369 68 DGIDI---STIPLEDLRSSLTIIPQDPtlFSgtirsNLDPFDEYSD--EEIYGALR---------------VSEGGL--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 437 tptryphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFG-VVEYlaDRI 515
Cdd:cd03369 125 -------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTI--LTIAHRLRtIIDY--DKI 193
|
250
....*....|..
gi 490704625 516 AVMHGGRIVEMG 527
Cdd:cd03369 194 LVMDAGEVKEYD 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
315-527 |
1.43e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGAR--VQGRAMLDGHDLLGASR---------RELRRLRQDI 383
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYgtIQVGDIYIGDKKNNHELitnpyskkiKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 384 QIVFQDPFASLDPRMRVGDILEEGIASLRPELAASARRARAvglLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEP 463
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFY---LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-254 |
1.91e-21 |
|
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: 95.95 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 35 AQGETfALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQEpaTSLNPVMRVGD 114
Cdd:TIGR02142 22 GQGVT-AIFGRSGSGKT----TLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 115 QIVETLAAHTPLRGAAARERAIDWLrrvGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQA 194
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELL---GI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 195 QVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYA 254
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-244 |
2.12e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 2 TASAPLLRIEGLDVdvAGESGVThAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDL 79
Cdd:COG3845 252 EPGEVVLEVENLSV--RDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQS----ELAEAL--AGlrPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 80 NDLSERAMRgvRGGrIGIIFQEP-ATSLNPVMRVGDQIVETLAAHTP------LRGAAARERAIDWLRRVGI--PEPERR 150
Cdd:COG3845 323 TGLSPRERR--RLG-VAYIPEDRlGRGLVPDMSVAENLILGRYRRPPfsrggfLDRKAIRAFAEELIEEFDVrtPGPDTP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 151 IDdypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGiQREMGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:COG3845 400 AR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAV 474
|
250
....*....|....
gi 490704625 231 MRGGEIVESADART 244
Cdd:COG3845 475 MYEGRIVGEVPAAE 488
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-237 |
2.12e-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: 92.56 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRIVggqieLGGTDLNdLSERAMRGVrggriGIIFQEp 102
Cdd:cd03298 12 EQPMHFDLTFAQGEITAIVGPSGSGKS-TLLNLIAgfETPQSGRVL-----INGVDVT-AAPPADRPV-----SMLFQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 aTSLNPVMRVGDQIveTLAAHTPLRGAAARERAID-WLRRVGIPEPERRIddyPFQFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:cd03298 79 -NNLFAHLTVEQNV--GLGLSPGLKLTAEDRQAIEvALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-242 |
2.14e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.20 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGEsgvtHAVKRLQLAVAQGETFALVGESGSGKSMTALALlrllpdAG----RIVGGQIELGGTDLNDLS 83
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI------MGhpkyEVTEGEILFKGEDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 84 --ERAMRGvrggrIGIIFQEPATslnpvmrvgdqivetlaahtpLRGAaareRAIDWLRRVGIpeperriddypfQFSGG 161
Cdd:cd03217 71 peERARLG-----IFLAFQYPPE---------------------IPGV----KNADFLRYVNE------------GFSGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITH--DLA--VVRNVAHhvaLMRGGEIV 237
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHyqRLLdyIKPDRVH---VLYDGRIV 184
|
....*
gi 490704625 238 ESADA 242
Cdd:cd03217 185 KSGDK 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-249 |
2.23e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.26 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDagrivGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPAtsl 106
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPT-----GGQVLLDGVPLVQYDHHYLHR----QVALVGQEPV--- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 npVMR--VGDQIVETL--AAHTPLRGAAARERAIDWlrrvgIPEPERRID----DYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:TIGR00958 566 --LFSgsVRENIAYGLtdTPDEEIMAAAKAANAHDF-----IMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 179 LIADEPTTALDVTVQAQVLELlagiQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESADARTFFERP 249
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQES----RSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
300-527 |
2.74e-21 |
|
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: 92.72 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 300 HYPVRKGVLRRVAAWVEA--VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGaRVQGRAMLDGHDLLGASRRELR 377
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTT----LLDAISG-RVEGGGTTSGQILFNGQPRKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 378 RLRQDIQIVFQD-------------PFAsldPRMRVGDILEEGIASLRPElaasarraraVGLLERVGLpadtpTRYPHE 444
Cdd:cd03234 78 QFQKCVAYVRQDdillpgltvretlTYT---AILRLPRKSSDAIRKKRVE----------DVLLRDLAL-----TRIGGN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 F----SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHG 520
Cdd:cd03234 140 LvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS 219
|
....*..
gi 490704625 521 GRIVEMG 527
Cdd:cd03234 220 GEIVYSG 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
25-240 |
2.97e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 91.89 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLNDLSERAmrgvrgGRIGIIFQEPAt 104
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSYQKNIEAL------RRIGALIEAPG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 sLNPVMRVGDQIvETLAahtplRGAAARERAID-WLRRVGIPE-PERRIDdypfQFSGGQKQRLMIAIALAAEPKLLIAD 182
Cdd:cd03268 83 -FYPNLTARENL-RLLA-----RLLGIRKKRIDeVLDVVGLKDsAKKKVK----GFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 183 EPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESA 240
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-528 |
3.02e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.77 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLLVHYPVR----------KGVLRRVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKAL---LRLVEG-AR 356
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgiLVPTSGeVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 357 VqgramlDGHDllgASRRElRRLRQDIQIVF------------QDPFasldpRM--RVGDILEEGIASLRPELaasarra 422
Cdd:COG4586 81 V------LGYV---PFKRR-KEFARRIGVVFgqrsqlwwdlpaIDSF-----RLlkAIYRIPDAEYKKRLDEL------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 423 raVGLLErVGLPADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFIT 502
Cdd:COG4586 139 --VELLD-LGELLDTPVR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTS 212
|
250 260
....*....|....*....|....*.
gi 490704625 503 HNFGVVEYLADRIAVMHGGRIVEMGP 528
Cdd:COG4586 213 HDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-237 |
3.07e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.49 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSE 84
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGCLDKPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 85 RAMRGVRGGRIGIIFQEpaTSLNPVMrVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQ 164
Cdd:PRK10535 78 DALAQLRREHFGFIFQR--YHLLSHL-TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 165 RLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVrNVAHHVALMRGGEIV 237
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
318-533 |
3.11e-21 |
|
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: 93.23 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG---ARVQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPFASL 394
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKST----LLSLITGdlpPTYGNDVRLFGERRGGEDVWELRKR---IGLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGI-ASL-RPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:COG1119 92 PRDETVLDVVLSGFfDSIgLYREPTDEQRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNfgvVEYLAD---RIAVMHGGRIVEMGPADTVL 533
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPgitHVLLLKDGRVVAAGPKEEVL 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
318-548 |
3.37e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLGASRRELRRlrqdiQIVFQdPFASLDPR 397
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL--TPQSGTVFLGDKPISMLSSRQLAR-----RLALL-PQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 -MRVGDILEEGIA---SLRPELAASARRARAVGLlERVGLP--ADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK11231 90 gITVRELVAYGRSpwlSLWGRLSAEDNARVNQAM-EQTRINhlADRRLT---DLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 472 TSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGpadtvlhAPRHEMTQRLLAAV 548
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLRTV 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-230 |
3.62e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.97 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 2 TASAPLLRIEGLDVDVAGEsgvTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrivgGQIELGGTDLND 81
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGR---RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE----GSIAVNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 82 LSERAMRGvrggRIGIIFQEPATslnpvmrVGDQIVETLAAHTPLRGAAARERAidwLRRVGIPE--------PERRIDD 153
Cdd:TIGR02857 389 ADADSWRD----QIAWVPQHPFL-------FAGTIAENIRLARPDASDAEIREA---LERAGLDEfvaalpqgLDTPIGE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 154 YPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:TIGR02857 455 GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
315-527 |
3.97e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.91 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDG---HDLLGASRrelrrlrqDIQIVFQD 389
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGleRITSGEIWIGGrvvNELEPADR--------DIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 pFAsLDPRMRVGDILEEG--IASL-RPELAasarraravgllERVGLPADTP------TRYPHEFSGGQRQRIAIARALA 460
Cdd:PRK11650 85 -YA-LYPHMSVRENMAYGlkIRGMpKAEIE------------ERVAEAARILelepllDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNfgVVE--YLADRIAVMHGGRIVEMG 527
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD--QVEamTLADRVVVMNGGVAEQIG 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-241 |
4.54e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.00 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKS-----MTALallrLLPDAGRIV-----------GGQIELGGTDLNdLSERAMRG 89
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNAL----LLPDTGTIEwifkdeknkkkTKEKEKVLEKLV-IQKTRFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 90 VRG-----GRIGIIFQEPATSLNpvmrvgDQIVETLAAHTPL----RGAAARERAIDWLRRVGIPEpeRRIDDYPFQFSG 160
Cdd:PRK13651 97 IKKikeirRRVGVVFQFAEYQLF------EQTIEKDIIFGPVsmgvSKEEAKKRAAKYIELVGLDE--SYLQRSPFELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESA 240
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
.
gi 490704625 241 D 241
Cdd:PRK13651 248 D 248
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-246 |
5.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLnDLSERAMRGVRGGrIGIIFQEPA 103
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGKPI-DYSRKGLMKLRES-VGMVFQDPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRVGDqiVETLAAHTPLRGAAARERAIDWLRRVGIpEPERRIDDYPFQFsgGQKQRLMIAIALAAEPKLLIADE 183
Cdd:PRK13636 93 NQLFSASVYQD--VSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSF--GQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-218 |
5.48e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.46 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESgvthAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSerA 86
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGSITLDGKPVEGPG--A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGVrggrigiIFQEPAtsLNPVMRVGDQIVETLAahtpLRGAAARER---AIDWLRRVGIPEPERRiddYPFQFSGGQK 163
Cdd:PRK11248 71 ERGV-------VFQNEG--LLPWRNVQDNVAFGLQ----LAGVEKMQRleiAHQMLKKVGLEGAEKR---YIWQLSGGQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 164 QRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL 218
Cdd:PRK11248 135 QRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
317-530 |
7.90e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 7.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASR-RELRRLRQDIQIVFQDPFAS 393
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKST----IMQLLNGLHVptQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDIL----------EEGIASLRPELAAsarraravgllerVGLPADTPTRYPHEFSGGQRQRIAIARALAVEP 463
Cdd:PRK13649 98 LFEETVLKDVAfgpqnfgvsqEEAEALAREKLAL-------------VGISESLFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG-PAD 530
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGkPKD 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-248 |
9.73e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 9.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRIVGGQIELGGTDLNdlseRAMRGVRGgRIGIIFQEPATSLNpv 109
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKS-TIMQLLNglHVPTQGSVRVDDTLITSTSKN----KDIKQIRK-KVGLVFQFPESQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 mrvgDQIVETLAAHTPLRGAAARE----RAIDWLRRVGIPEPERriDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:PRK13649 100 ----EETVLKDVAFGPQNFGVSQEeaeaLAREKLALVGISESLF--EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 186 TALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFER 248
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
316-546 |
1.11e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGarvqgramLD---GHDLLgASRRELRRLRQDIQIVFQDpfA 392
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLAG--------LEtpsAGELL-AGTAPLAEAREDTRLMFQD--A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDILEEGI-ASLRPELAASarraravglLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK11247 91 RLLPWKKVIDNVGLGLkGQWRDAALQA---------LAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIvemGPADTV-LHAPRHEMTQRLLA 546
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI---GLDLTVdLPRPRRRGSARLAE 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
332-536 |
1.47e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 332 ALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRR-----ELRRlrqdIQIVFQDpfASLDPRMRVGDIL 404
Cdd:PRK11144 28 AIFGRSGAGKTS----LINAISGLTRpqKGRIVLNGRVLFDAEKGiclppEKRR----IGYVFQD--ARLFPHYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 405 EEGIASLRPELAASArraraVGLLervGLpadTP--TRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQ 482
Cdd:PRK11144 98 RYGMAKSMVAQFDKI-----VALL---GI---EPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490704625 483 ILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-274 |
1.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRL-LPDAGRIvggqiELGGTDLNDLSERAMRGvrggRIGIIFQEP 102
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRV-----KVMGREVNAENEKWVRS----KVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 atslnpvmrvGDQI----VETLAAHTP----LRGAAARERAIDWLRRVGIPEPErriDDYPFQFSGGQKQRLMIAIALAA 174
Cdd:PRK13647 89 ----------DDQVfsstVWDDVAFGPvnmgLDKDEVERRVEEALKAVRMWDFR---DKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP----- 249
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDiveqa 234
|
250 260
....*....|....*....|....*..
gi 490704625 250 --RHPYARELFEAIPTFAKRGRPLSAQ 274
Cdd:PRK13647 235 glRLPLVAQIFEDLPELGQSKLPLTVK 261
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-236 |
1.67e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSE--RAMrgvrggrigiiFQEpaTS 105
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAGLETPSAGELLAGTAPLAEAREdtRLM-----------FQD--AR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVGDQIVETLAAHTplrgaaaRERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQW-------RDAALQALAAVGLAD---RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490704625 186 TALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-237 |
1.67e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSER 85
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 AMRGVRGgrigIIFQepATSLNPVMRVgDQIVETLAAhtPLRGAAARERAI--DWLRRVGIPEPERRidDYPfQFSGGQK 163
Cdd:PRK13548 73 ELARRRA----VLPQ--HSSLSFPFTV-EEVVAMGRA--PHGLSRAEDDALvaAALAQVDLAHLAGR--DYP-QLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 164 QRLMIAIALA------AEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK13548 141 QRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
319-530 |
1.75e-20 |
|
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: 95.41 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRlrqDIQIVFQDPfasldp 396
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKST----LLRLLLGfeTPESGSVFYDGQDLAGLDVQAVRR---QLGVVLQNG------ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEE--GIASLRPELAASArraravglLERVGLPADTpTRYP---H--------EFSGGQRQRIAIARALAVEP 463
Cdd:TIGR03797 537 RLMSGSIFENiaGGAPLTLDEAWEA--------ARMAGLAEDI-RAMPmgmHtvisegggTLSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLrdlqAELGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPAD 530
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYD 669
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-251 |
2.03e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.99 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 4 SAPLLRIEGLDVdvagESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLR---LLPDAgrIVGGQIELGG---- 76
Cdd:PRK14239 2 TEPILQVSDLSV----YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPEV--TITGSIVYNGhniy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 77 ---TDLNDLSERamrgvrggrIGIIFQEPatslNPV-MRVGDQIVETL-------------AAHTPLRGAAARERAIDwl 139
Cdd:PRK14239 76 sprTDTVDLRKE---------IGMVFQQP----NPFpMSIYENVVYGLrlkgikdkqvldeAVEKSLKGASIWDEVKD-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 140 rrvgipeperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMavLLITHDLA 219
Cdd:PRK14239 141 ----------RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQ 208
|
250 260 270
....*....|....*....|....*....|..
gi 490704625 220 VVRNVAHHVALMRGGEIVESADARTFFERPRH 251
Cdd:PRK14239 209 QASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-239 |
2.29e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.89 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLS--ERAMRGvrggrIGIIF 99
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP----VKSGSIRLDGEDITKLPphERARAG-----IAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QepatslnpvmrvGDQIVETLAAHTPLR-GAAAReraidwlrrvgiPEPERRIDDYPFQF---------------SGGQK 163
Cdd:TIGR03410 82 Q------------GREIFPRLTVEENLLtGLAAL------------PRRSRKIPDEIYELfpvlkemlgrrggdlSGGQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 164 QRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:TIGR03410 138 QQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVAS 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
281-544 |
2.86e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 281 GKAAPEAGAVVLDVQDLLVHYPVRKgvlrrvaawVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--Q 358
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQP---------QPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTRAWDpqQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 359 GRAMLDGHDLlgASRRElRRLRQDIQIVFQdpfasldprmRVgDILEegiASLRPELAASARRA---RAVGLLERVGLPA 435
Cdd:PRK11160 395 GEILLNGQPI--ADYSE-AALRQAISVVSQ----------RV-HLFS---ATLRDNLLLAAPNAsdeALIEVLQQVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 436 DTPTRYP---------HEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFG 506
Cdd:PRK11160 458 LLEDDKGlnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT 535
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490704625 507 VVEYLaDRIAVMHGGRIVEMGPADTVL--HAPRHEMTQRL 544
Cdd:PRK11160 536 GLEQF-DRICVMDNGQIIEQGTHQELLaqQGRYYQLKQRL 574
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
25-236 |
3.08e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 89.38 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVGGQIELGGTDLNDlseramrgvrggrIGIIFQEPA 103
Cdd:TIGR03740 14 TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILrPTSGEIIFDGHPWTRKDLHK-------------IGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRvgdqivETLAAHTPLRGAAaRERAIDWLRRVGIPEPERRIDDypfQFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:TIGR03740 81 LYENLTAR------ENLKVHTTLLGLP-DSRIDEVLNIVDLTNTGKKKAK---QFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:TIGR03740 151 PTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
34-248 |
3.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.95 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 34 VAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVggqielggTDLNDLSERAMRGVRGgRIGIIFQEPATSLnpvmrV 112
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQII--------IDGDLLTEENVWDIRH-KIGMVFQNPDNQF-----V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 113 GDQIVETLAAHTPLRGAA---ARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALD 189
Cdd:PRK13650 96 GATVEDDVAFGLENKGIPheeMKERVNEALELVGMQDFKER---EPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 190 VTVQAQVLELLAGIQREMGMAVLLITHDLAVVrNVAHHVALMRGGEIVESADARTFFER 248
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-257 |
4.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.56 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVGGQIELGGTDlndlSERAMRGVRGgRIGIIFQEP 102
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTS----KQKEIKPVRK-KVGVVFQFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLNpvmrvgDQIVETLAAHTPLRGAAARERA----IDWLRRVGIPEpeRRIDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:PRK13643 94 ESQLF------EETVLKDVAFGPQNFGIPKEKAekiaAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRHPYAREL 257
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
315-537 |
5.51e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDpfA 392
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLRAINGtlTPTAGTVLVAGDDVEALSARAASRR---VASVPQD--T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDILEEGIASLRPELAASARRARAV--GLLERVGLP--ADTPTRyphEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:PRK09536 87 SLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAveRAMERTGVAqfADRPVT---SLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-237 |
5.91e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDVaGESGVTHAvkrLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLN 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGY-GKYTVAEN---LTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 DLSERAMrgvrGGRIGIIFQEPATSlnpvmrvGDQIVETLAA-----HTPL--RGAAARERAID-WLRRVGIPEPERRID 152
Cdd:PRK10253 73 HYASKEV----ARRIGLLAQNATTP-------GDITVQELVArgrypHQPLftRWRKEDEEAVTkAMQATGITHLADQSV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMR 232
Cdd:PRK10253 142 D---TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALR 218
|
....*
gi 490704625 233 GGEIV 237
Cdd:PRK10253 219 EGKIV 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-239 |
6.93e-20 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 88.82 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDagrivGGQIELGGTDLNDLSERAMRgvrgGRIGIIFQEP- 102
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQ-----KGQILIDGIDIRDISRKSLR----SMIGVVLQDTf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 --ATSLNPVMRVGDQIvetlaahtplrgaAARERAIDWLRRVGI-PEPERRIDDYPFQ-------FSGGQKQRLMIAIAL 172
Cdd:cd03254 88 lfSGTIMENIRLGRPN-------------ATDEEVIEAAKEAGAhDFIMKLPNGYDTVlgenggnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 173 AAEPKLLIADEPTTALDV----TVQAQVLELLAgiqremGMAVLLITHDLAVVRNvAHHVALMRGGEIVES 239
Cdd:cd03254 155 LRDPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
317-527 |
7.57e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.16 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLlgasrRE--LRRLRQDIQIV------FQ 388
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID--EGEILLDGHDL-----RDytLASLRNQVALVsqnvhlFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 389 DPFASldprmrvgDIL--EEGIASlRPELAASARRARAVGLLERV--GLpaDTPTrypHE----FSGGQRQRIAIARALA 460
Cdd:PRK11176 431 DTIAN--------NIAyaRTEQYS-REQIEEAARMAYAMDFINKMdnGL--DTVI---GEngvlLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 461 VEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIayLFITHNFGVVEYlADRIAVMHGGRIVEMG 527
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
316-533 |
8.15e-20 |
|
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: 93.27 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRlrqDIQIVFQDPFasld 395
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQH--GQVLVDGVDLAIADPAWLRR---QMGVVLQENV---- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 prMRVGDIlEEGIASLRPELAAS--ARRARAVGLLERV-GLPADTPTRYPHE---FSGGQRQRIAIARALAVEPKVLICD 469
Cdd:TIGR01846 542 --LFSRSI-RDNIALCNPGAPFEhvIHAAKLAGAHDFIsELPQGYNTEVGEKganLSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAelGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPADTVL 533
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELL 679
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-238 |
8.26e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 88.44 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 14 DVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrgg 93
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 94 RIGIIFQEpatslnpVMRVGDQIVETLAAHTPlrgAAARERAIDWLRRVGIPE-----PE---RRIDDYPFQFSGGQKQR 165
Cdd:cd03251 77 QIGLVSQD-------VFLFNDTVAENIAYGRP---GATREEVEEAARAANAHEfimelPEgydTVIGERGVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
317-524 |
8.81e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGA-RV-QGRAMLDGHDLlgASRRELRRLRqDIQIVFQDPFASL 394
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAGSlPPdSGSILIDGKDV--TKLPEYKRAK-YIGRVFQDPMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVgdilEE--------------GIASLRPELAASARRARAVGL-LE-----RVGLpadtptrypheFSGGQRQRIA 454
Cdd:COG1101 94 APSMTI----EEnlalayrrgkrrglRRGLTKKRRELFRELLATLGLgLEnrldtKVGL-----------LSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 455 IARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNfgvVEY---LADRIAVMHGGRIV 524
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQaldYGNRLIMMHEGRII 228
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
323-530 |
9.15e-20 |
|
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: 88.37 E-value: 9.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 323 FTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGhdllgasrRELRRLRQDIQIVFQDPFASLDPRMRVGD 402
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLI--PPAKGTVKVAG--------ASPGKGWRHIGYVPQRHEFAWDFPISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 403 ILEEGIASL-----RPELAASARRARAvglLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:TIGR03771 71 TVMSGRTGHigwlrRPCVADFAAVRDA---LRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 478 SVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:TIGR03771 147 PTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQ 198
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
324-527 |
1.05e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.61 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 324 TLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGA--SRRELRRLRQDiqivfQDPFASLDPRMR 399
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKST----LLNLIAGfiEPASGSIKVNDQSHTGLapYQRPVSMLFQE-----NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 400 VGDILEEGIASLRPELAASARRARAVGLlervglpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSV 479
Cdd:TIGR01277 91 IGLGLHPGLKLNAEQQEKVVDAAQQVGI-------ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490704625 480 QAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
30-249 |
1.14e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDlseramRGVRGGRIGIIFQEPAtsLNPV 109
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKT----TVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRDICMVFQSYA--LFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVGDQIvetlaahtplrGAAareraidwLRRVGIPEPERRI---------------DDYPFQFSGGQKQRLMIAIALAA 174
Cdd:PRK11432 93 MSLGENV-----------GYG--------LKMLGVPKEERKQrvkealelvdlagfeDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
281-527 |
1.32e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 281 GKAAPEAGAVVLDVQDLLVHYPVRKGVLrrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGR 360
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVP--------VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT--GGQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 361 AMLDGHDLlgaSRRELRRLRQDIQIVFQDPfasldprMRVGDILEEGIAS--LRPELAASARRARAVGLLERVGlpaDTP 438
Cdd:TIGR00958 538 VLLDGVPL---VQYDHHYLHRQVALVGQEP-------VLFSGSVRENIAYglTDTPDEEIMAAAKAANAHDFIM---EFP 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 439 TRYPHE-------FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAqildLLRDLQAELGIAYLFITHNFGVVEYl 511
Cdd:TIGR00958 605 NGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER- 679
|
250
....*....|....*.
gi 490704625 512 ADRIAVMHGGRIVEMG 527
Cdd:TIGR00958 680 ADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-241 |
1.57e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.51 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGrivggQIELGGTDLNDLSERAMRGvrggRIGIIFQEP-- 102
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSG-----EIKIDGITISKENLKEIRK----KIGIIFQNPdn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 -----------ATSL-----NP-VMRvgdQIVETLAAhtplrgaaareraidwlrRVGIpepERRIDDYPFQFSGGQKQR 165
Cdd:PRK13632 95 qfigatveddiAFGLenkkvPPkKMK---DIIDDLAK------------------KVGM---EDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESAD 241
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGK 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-237 |
1.77e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 87.04 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTalalLRLLPDAGRIVGGQIELGGTDLNDLSERA 86
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLLEPDAGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRgvrggRIGIIFQepATSLNPVMRVGDQiVETLAAHTPLRGAAARERaIDWL-RRVGIPE-PERRIDDypfqFSGGQKQ 164
Cdd:cd03266 77 RR-----RLGFVSD--STGLYDRLTAREN-LEYFAGLYGLKGDELTAR-LEELaDRLGMEElLDRRVGG----FSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 165 RLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGiQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
317-536 |
1.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRreLRRLRQDIQIVFQDPFASLdp 396
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK--GKVLVSGIDTGDFSK--LQGIRKLVGIVFQNPETQF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 rmrVGDILEEGIAsLRPE---LAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK13644 91 ---VGRTVEEDLA-FGPEnlcLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 474 ALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVeYLADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
309-537 |
2.10e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.39 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 309 RRVaawveaVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegaRV-QGRAMLDGHDL----------LG------- 370
Cdd:COG1137 16 RTV------VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV---KPdSGRIFLDGEDIthlpmhkrarLGigylpqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRreLRRL--RQDIQIVFQdpFASLDP---RMRVGDILEE-GIASLRpelaasarraravgllervGLPADTptryphe 444
Cdd:COG1137 87 ASI--FRKLtvEDNILAVLE--LRKLSKkerEERLEELLEEfGITHLR-------------------KSKAYS------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALD-VSVqAQILDLLRDLqAELGIAYLfIT-HNfgVVEYLA--DRIAVMHG 520
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHL-KERGIGVL-ITdHN--VRETLGicDRAYIISE 211
|
250
....*....|....*..
gi 490704625 521 GRIVEMGPADTVLHAPR 537
Cdd:COG1137 212 GKVLAEGTPEEILNNPL 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-239 |
2.35e-19 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 91.94 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEpaTSLN 107
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKS----TLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR----QLGVVLQN--GRLM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 108 PvmrvgDQIVETLAAHTPLRGAAARERAidwlRRVGIpepERRIDDYPFQF-----------SGGQKQRLMIAIALAAEP 176
Cdd:TIGR03797 540 S-----GSIFENIAGGAPLTLDEAWEAA----RMAGL---AEDIRAMPMGMhtvisegggtlSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 177 KLLIADEPTTALDVTVQAQVLELLAGIQremgMAVLLITHDLAVVRNvAHHVALMRGGEIVES 239
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQ 665
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
315-531 |
3.13e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.86 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGArVQ---GRAMLDGHDLLGASRRELRRLRqdIQIVFQDPf 391
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKST----LMKILYGL-YQpdsGEILIDGKPVRIRSPRDAIALG--IGMVHQHF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 aSLDPRMRVgdiLE------EGIASLRPELAASARRARAvgLLERVGLPADtPTRYPHEFSGGQRQRIAIARALAVEPKV 465
Cdd:COG3845 90 -MLVPNLTV---AEnivlglEPTKGGRLDRKAARARIRE--LSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV-EMGPADT 531
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVgTVDTAET 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-504 |
3.39e-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: 90.88 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 254 ARELFEAIPtfAKRGRPLSAQGRAADQGkaapeAGAVVLDVQDLLVHYPVRKGVLrrvaawveavNGVTFTLRAGETLAL 333
Cdd:TIGR02868 304 AERIVEVLD--AAGPVAEGSAPAAGAVG-----LGKPTLELRDLSAGYPGAPPVL----------DGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 334 LGESGCGKTTTGKALLRLVEGarVQGRAMLDGHDLLGASRRELRRLrqdIQIVFQDPF---ASLDPRMRVGdileegias 410
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDP--LQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDAHlfdTTVRENLRLA--------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 411 lRPELAASARRAravgLLERVGLpADTPTRYPH-----------EFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSV 479
Cdd:TIGR02868 433 -RPDATDEELWA----ALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
250 260
....*....|....*....|....*
gi 490704625 480 QAQILDLLrdLQAELGIAYLFITHN 504
Cdd:TIGR02868 507 ADELLEDL--LAALSGRTVVLITHH 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
317-525 |
3.68e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASrrelrrlrQDIQIVFQDpfASL 394
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAGfvPYQHGSITLDGKPVEGPG--------AERGVVFQN--EGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIaslrpELAASARRARAV---GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK11248 82 LPWRNVQDNVAFGL-----QLAGVEKMQRLEiahQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMH--GGRIVE 525
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-251 |
6.05e-19 |
|
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: 85.98 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMrgvrggrigIIFQEpaTSL 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 NPVMRVGDQIVETLAAHTPLRGAAARERAID-WLRRVGIPEPErriDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKSERRAIVEeHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 186 TALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRG------GEIVESAdartfFERPRH 251
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVP-----FPRPRD 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-532 |
6.61e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLGASRRElrrlRQDIQIVFQdpFASLDPR 397
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT--HPDAGSISLCGEPVPSRARHA----RQRVGVVPQ--FDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEegIASLRPELAASARRARAVGLLE--RVGLPADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:PRK13537 95 FTVRENLL--VFGRYFGLSAAAARALVPPLLEfaKLENKADAKVG---ELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 476 DVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGR-IVEMGPADTV 532
Cdd:PRK13537 170 DPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRkIAEGAPHALI 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
320-553 |
7.81e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGarvQGRAMLDGHDLLGASRRELRRLR----QDIQIVFQdpfasld 395
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG---QGEILLNGRPLSDWSAAELARHRaylsQQQSPPFA------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 prMRVGDILEegiASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARAL-----AVEP--KVLIC 468
Cdd:COG4138 84 --MPVFQYLA---LHQPAGASSEAVEQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVlhaprheMTQRLLAAV 548
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV-------MTPENLSEV 229
|
....*
gi 490704625 549 PRLRF 553
Cdd:COG4138 230 FGVKF 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
318-527 |
8.01e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 84.52 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDllgasrRELRRLRQDIQIVFQDP--FASLD 395
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRP------LDKRSFRKIIGYVPQDDilHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PR--MRVgdileegIASLRpelaasarraravgllervGLpadtptryphefSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:cd03213 99 VRetLMF-------AAKLR-------------------GL------------SGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 474 ALDVSVQAQILDLLRDLqAELGIAYLFITHN-FGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03213 141 GLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
24-249 |
1.15e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.08 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRIVggqieLGGTDLNDLSERAmRGVRggrigII 98
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIagfetPDSGRIM-----LDGQDITHVPAEN-RHVN-----TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 99 FQEPAtsLNPVMRVGDQIVETL-AAHTPlrGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:PRK09452 92 FQSYA--LFPHMTVFENVAFGLrMQKTP--AAEITPRVMEALRMVQL---EEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
40-239 |
1.17e-18 |
|
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: 84.55 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 40 FALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNdlseRAMRGVRGgRIGIIFQEPATSlnPVMRVGDQiVET 119
Cdd:cd03264 28 YGLLGPNGAGKT----TLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRR-RIGYLPQEFGVY--PNFTVREF-LDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 120 LAAHTPLRGAAARERAIDWLRRVGIPEperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLEL 199
Cdd:cd03264 96 IAWLKGIPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490704625 200 LAGIQREmgMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:cd03264 173 LSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-249 |
1.24e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVggqieLGGTDLNDLSEraMRGVRGgRIGIIFQEP 102
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVL-----VSGIDTGDFSK--LQGIRK-LVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLnpvmrVGDQIVETLA---AHTPLRGAAARERAIDWLRRVGIPEPERRiddYPFQFSGGQKQRLMIAIALAAEPKLL 179
Cdd:PRK13644 87 ETQF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVrNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
317-530 |
1.64e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARVQGRAMLDGHDLLGAS---RRELRRLRQDIQIVFQDPFAS 393
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKST----LLQHLNGLLQPTEGKVTVGDIVVSStskQKEIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDIL----EEGIASLRPELAASARraravglLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:PRK13643 97 LFEETVLKDVAfgpqNFGIPKEKAEKIAAEK-------LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG-PAD 530
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtPSD 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-246 |
2.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 35 AQGETFALVGESGSGKSMTALALLRLLPDA------GRIVGGQIELGGTDLNDLSERAMRGVRGGR--IGIIFQEPATSL 106
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtiqvGDIYIGDKKNNHELITNPYSKKIKNFKELRrrVSMVFQFPEYQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 NPVMRVGDQIVETLAAHTPlrGAAARERAIDWLRRVGIPEPerRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTT 186
Cdd:PRK13631 130 FKDTIEKDIMFGPVALGVK--KSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 187 ALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFF 246
Cdd:PRK13631 206 GLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-238 |
2.65e-18 |
|
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: 84.46 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRL-LPDAGRIVGGQIELGGTDLNDLSERamrgvrggrIGIIFQEpAT 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQ---------VGVVLQE-NV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNpvmrvgDQIVETLAAHTPlrgAAARERAIDWLRRVG-------IPEP-ERRIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:cd03252 87 LFN------RSIRDNIALADP---GMSMERVIEAAKLAGahdfiseLPEGyDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 177 KLLIADEPTTALDVtvqaqvlELLAGIQREM-----GMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:cd03252 158 RILIFDEATSALDY-------ESEHAIMRNMhdicaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-236 |
4.54e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.29 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLSERAMRGVrggrIGIIFQEP- 102
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ----PQGGQVLLDGKPISQYEHKYLHSK----VSLVGQEPv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 --ATSLNPVMRVGDQIVETLAahtpLRGAAARERAIDWLRRVGIpEPERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLI 180
Cdd:cd03248 99 lfARSLQDNIAYGLQSCSFEC----VKEAAQKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 181 ADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNvAHHVALMRGGEI 236
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-293 |
7.39e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.08 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 21 SGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVrggrIGIIFQ 100
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKS----TLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 epatslNPVMRVGDQIVETLAAHTP----LRGAAARERAIDWLRRVGIPEPERRIddyPFQFSGGQKQRLMIAIALAAEP 176
Cdd:PRK13652 86 ------NPDDQIFSPTVEQDIAFGPinlgLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 177 KLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPRhpYARE 256
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD--LLAR 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 490704625 257 LFEAIPTFAKRGRPLSAQGRAADQGKAAPEAGAVVLD 293
Cdd:PRK13652 235 VHLDLPSLPKLIRSLQAQGIAIDMAYTYQEAEDAFLK 271
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
316-526 |
7.64e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDL---LGASRRELRRlrQDIQIVFQdp 390
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKST----LLHLLGGldTPTSGDVIFNGQPMsklSSAAKAELRN--QKLGFIYQ-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FASLDPRMRVgdiLEEG-----IASLRPELAASARRAravgLLERVGLPADTPTRyPHEFSGGQRQRIAIARALAVEPKV 465
Cdd:PRK11629 95 FHHLLPDFTA---LENVampllIGKKKPAEINSRALE----MLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFgvveYLADRIavmhgGRIVEM 526
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM-----SRQLEM 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
319-530 |
7.65e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALL-RLVEGARVQGRAMLDGHdllgasRRELRRLRQDIQIVFQDP--FASLD 395
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVKGSGSVLLNGM------PIDAKEMRAISAYVQQDDlfIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PR--------MRVGDILEEGIASLRPElaasarraravGLLERVGLP--ADTPTRYPHE---FSGGQRQRIAIARALAVE 462
Cdd:TIGR00955 116 VRehlmfqahLRMPRRVTKKEKRERVD-----------EVLQALGLRkcANTRIGVPGRvkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 463 PKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-237 |
1.40e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVagesGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGrivggQIELGGTDLNDLSERA 86
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSG-----TVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MrgvrGGRIGIIFQEPATSLNPVMRvgdQIVE-TLAAHTPLRG--AAARERAIDW-LRRVGIPE-PERRIDDypfqFSGG 161
Cdd:PRK11231 74 L----ARRLALLPQHHLTPEGITVR---ELVAyGRSPWLSLWGrlSAEDNARVNQaMEQTRINHlADRRLTD----LSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-236 |
1.76e-17 |
|
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: 80.55 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDvagesgvtHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSE 84
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQT----ELAEALFGLRPPASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 85 RAMRgvrggRIGIifqepatslnpvmrvgdqivetlaAHTPlrgaaaRERaidwlRRVGIpEPERRIDD---YPFQFSGG 161
Cdd:cd03215 70 RDAI-----RAGI------------------------AYVP------EDR-----KREGL-VLDLSVAEniaLSSLLSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-246 |
2.30e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESGVTHaVKRLQLAVAQGETFALVGESGSGKSMTAlallRLLPDAGRIVGGQIELGGTDLNDLSERA 86
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTA----RLIDGLFEEFEGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 MRGvrggRIGIIFQEPATSLnpvmrVGDQIVETLAAHTPLRGAAARE---RAIDWLRRVGIPEPERRiddYPFQFSGGQK 163
Cdd:PRK13642 79 LRR----KIGMVFQNPDNQF-----VGATVEDDVAFGMENQGIPREEmikRVDEALLAVNMLDFKTR---EPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 164 QRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESADAR 243
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
...
gi 490704625 244 TFF 246
Cdd:PRK13642 226 ELF 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-243 |
2.47e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 37 GETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEPATSLNpvmrvgDQI 116
Cdd:PRK10908 28 GEMAFLTGHSGAGKS----TLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMD------RTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 117 VETLAAHTPLRGAAA---RERAIDWLRRVGIPEPERridDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQ 193
Cdd:PRK10908 97 YDNVAIPLIIAGASGddiRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490704625 194 AQVLELLAGIQReMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADAR 243
Cdd:PRK10908 174 EGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
320-504 |
3.59e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRRELRRLR-QDIQIVFQDPFasLDPRM 398
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFM--LIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 399 rvgDILE--EGIASLRPElAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:PRK10584 104 ---NALEnvELPALLRGE-SSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*...
gi 490704625 477 VSVQAQILDLLRDLQAELGIAYLFITHN 504
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
318-528 |
4.33e-17 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 84.61 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRR----LRQDIQIvFQ----D 389
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWS--GEILFDGIPREEIPREVLANsvamVDQDIFL-FEgtvrD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 PFASLDPRMRVGDIL--------EEGIASLrpelaasarraravgllervglpadtPTRYPHE-------FSGGQRQRIA 454
Cdd:TIGR03796 572 NLTLWDPTIPDADLVrackdaaiHDVITSR--------------------------PGGYDAElaegganLSGGQRQRLE 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 455 IARALAVEPKVLICDEPTSALDVSVQAQILDLLRdlqaELGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGP 528
Cdd:TIGR03796 626 IARALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGT 694
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-238 |
4.66e-17 |
|
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: 80.74 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEpaTSLn 107
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR----AIGVVPQD--TVL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 108 pvmrVGDQIVETLAAHTPlrgAAARERAIDWLRRVGIpepERRIDDYPFQF-----------SGGQKQRLMIAIALAAEP 176
Cdd:cd03253 87 ----FNDTIGYNIRYGRP---DATDEEVIEAAKAAQI---HDKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 177 KLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
316-523 |
6.81e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQG-RAMLDGHDLLGASR--RELRRLRQDIQIVFQDpfA 392
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGsHIELLGRTVQREGRlaRDIRKSRANTGYIFQQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDILEEGIASLRP------ELAASARRARAVGLLERVGLpadtpTRYPHE----FSGGQRQRIAIARALAVE 462
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGM-----VHFAHQrvstLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 463 PKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
328-537 |
9.72e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 9.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 328 GETLALLGESGCGKTTtgkaLLRLVEGARvqgraMLDGHDLLGASRR--ELRRLRQDIQIVFQDpfASLDPRMRVGDILE 405
Cdd:PRK11000 29 GEFVVFVGPSGCGKST----LLRMIAGLE-----DITSGDLFIGEKRmnDVPPAERGVGMVFQS--YALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 406 EGI-------ASLRPELAASARRARAVGLLERvglpadtptrYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVS 478
Cdd:PRK11000 98 FGLklagakkEEINQRVNQVAEVLQLAHLLDR----------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 479 VQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPR 537
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-237 |
1.17e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 2 TASAPLLRIEGLdvdvagesGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLND 81
Cdd:COG1129 251 APGEVVLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 82 LSER-AMRgvRGgrIGIIfqeP----ATSLNPVMRVGDQIV----ETLAAHTPLRGAAARERAIDWLRRVGI--PEPERR 150
Cdd:COG1129 319 RSPRdAIR--AG--IAYV---PedrkGEGLVLDLSIRENITlaslDRLSRGGLLDRRRERALAEEYIKRLRIktPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 151 IDdypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:COG1129 392 VG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILV 466
|
....*..
gi 490704625 231 MRGGEIV 237
Cdd:COG1129 467 MREGRIV 473
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-247 |
1.28e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.18 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 10 IEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVGGQIELGGTDLNDLSERamr 88
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLRKH--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 89 gvrggrIGIIFQEPAtslnpvmrvgDQIVETLAAHTPLRG--------AAARERAIDWLRRVGIPEperRIDDYPFQFSG 160
Cdd:PRK13648 85 ------IGIVFQNPD----------NQFVGSIVKYDVAFGlenhavpyDEMHRRVSEALKQVDMLE---RADYEPNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESA 240
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
....*..
gi 490704625 241 DARTFFE 247
Cdd:PRK13648 225 TPTEIFD 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-236 |
1.49e-16 |
|
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: 78.75 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDL--SERAmrgvrggrIGIIFQEp 102
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKS----TLLNLIAGFIEPASGSIKVNDQSHTGLapYQRP--------VSMLFQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 aTSLNPVMRVGDQIveTLAAHTPLR-GAAARERAIDWLRRVGIPEPERRIddyPFQFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:TIGR01277 79 -NNLFAHLTVRQNI--GLGLHPGLKlNAEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-218 |
1.82e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 82.41 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVDVAGESGVthaVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDagriVGGQIELGGTDLNDLSE 84
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPPV---LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP----LQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 85 RAMRGvrggRIGIIFQEP---ATSLNPVMRVGdqivetlaahtplRGAAARERAIDWLRRVGIPEPERRIDD-------- 153
Cdd:TIGR02868 405 DEVRR----RVSVCAQDAhlfDTTVRENLRLA-------------RPDATDEELWAALERVGLADWLRALPDgldtvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 154 YPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAgiQREMGMAVLLITHDL 218
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL--AALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
30-248 |
2.03e-16 |
|
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: 82.48 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVrggrIGIIFQEPatslnpV 109
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKS----TLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQEP------Y 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVGdQIVETLaahtpLRGAAARERAIDWLRRVGIPEPERRIDDYP-----------FQFSGGQKQRLMIAIALAAEPKL 178
Cdd:TIGR01193 559 IFSG-SILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREmgmAVLLITHDLAVVRNVaHHVALMRGGEIVESADARTFFER 248
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-532 |
2.98e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRL---------VEGARVQGRAmldghdllgasrrelRRLRQDIQIVFQ 388
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMtspdagkitVLGVPVPARA---------------RLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 389 dpFASLDPRMRVGDILEegIASLRPELAASARRARAVGLLE--RVGLPADTPTRyphEFSGGQRQRIAIARALAVEPKVL 466
Cdd:PRK13536 122 --FDNLDLEFTVRENLL--VFGRYFGMSTREIEAVIPSLLEfaRLESKADARVS---DLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 467 ICDEPTSALDVSVQAQILDLLRDLQAeLGIAYLFITHNFGVVEYLADRIAVMHGGR-IVEMGPADTV 532
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEGRPHALI 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-230 |
3.17e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.89 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRIvggqielggtdlndlseramRGVRGGRIGIIFQEPA 103
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKS-TLLKVLAgvLRPTSGTV--------------------RRAGGARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRVGDQIVETLAAHT-PLR--GAAARERAIDWLRRVGIPEPERRiddyPFQ-FSGGQKQRLMIAIALAAEPKLL 179
Cdd:NF040873 66 VPDSLPLTVRDLVAMGRWARRgLWRrlTRDDRAAVDDALERVGLADLAGR----QLGeLSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-218 |
3.43e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTALALL--RLLPDAGRIvggqiELGGTDLNDLSERAmrgvRGGRIGIIFQEP 102
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIagSLPPDSGSI-----LIDGKDVTKLPEYK----RAKYIGRVFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 ATSLNPVMrvgdQIVETLA-AHtpLRG----------AAARERAIDWLRRVGIpEPERRIDDYPFQFSGGQKQRLMIAIA 171
Cdd:COG1101 90 MMGTAPSM----TIEENLAlAY--RRGkrrglrrgltKKRRELFRELLATLGL-GLENRLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490704625 172 LAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDL 218
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-255 |
3.58e-16 |
|
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: 81.69 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEpats 105
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR----QVALVSQD---- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 lnpVMRVGDQIVETLAAHTP-------LRGAAARERAIDWLRRV--GIPEPerrIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:TIGR02203 415 ---VVLFNDTIANNIAYGRTeqadraeIERALAAAYAQDFVDKLplGLDTP---IGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 177 KLLIADEPTTALDVTVQAQVlelLAGIQREM-GMAVLLITHDLAVVRNvAHHVALMRGGEIVESADARTFFERPRHpYAR 255
Cdd:TIGR02203 489 PILILDEATSALDNESERLV---QAALERLMqGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGL-YAQ 563
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
3.61e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 78.23 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmTALALL--RLLPDAGRIVggqieLGGTD 78
Cdd:COG4674 4 DTMHGPILYVEDLTVSFDG----FKALNDLSLYVDPGELRVIIGPNGAGKT-TLMDVItgKTRPDSGSVL-----FGGTD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 79 LNDLSERAMrgVRGGrIGIIFQEPatSLNPVMRVGDQIVETLAAHTPL-------RGAAARERAIDWLRRVGIpepERRI 151
Cdd:COG4674 74 LTGLDEHEI--ARLG-IGRKFQKP--TVFEELTVFENLELALKGDRGVfaslfarLTAEERDRIEEVLETIGL---TDKA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 152 DDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVAHHV 228
Cdd:COG4674 146 DRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK--HSVVVVEHDMEFVRQIARKV 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-236 |
4.05e-16 |
|
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: 76.10 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVThaVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrivgGQIELGGTDLNDLSERAm 87
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS----GRVRLDGADISQWDPNE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 rgvRGGRIGIIFQEpatslnpVMRVGDQIVETLaahtplrgaaareraidwlrrvgipeperriddypfqFSGGQKQRLM 167
Cdd:cd03246 74 ---LGDHVGYLPQD-------DELFSGSIAENI-------------------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 168 IAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRnVAHHVALMRGGEI 236
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
318-548 |
4.20e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLL----RLVEgaRVQGRAMLDGHDLLGASRRELRR----LRQDIQIVfqd 389
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKST----LLsmisRLLP--PDSGEVLVDGLDVATTPSRELAKrlaiLRQENHIN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 390 pfasldPRMRVGD--------------------ILEEGIASLrpELaasarraravgllervglpADTPTRYPHEFSGGQ 449
Cdd:COG4604 88 ------SRLTVRElvafgrfpyskgrltaedreIIDEAIAYL--DL-------------------EDLADRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 450 RQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITH--NFGVVeYlADRIAVMHGGRIVEMG 527
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHdiNFASC-Y-ADHIVAMKDGRVVAQG 218
|
250 260
....*....|....*....|.
gi 490704625 528 PADTVlhaprheMTQRLLAAV 548
Cdd:COG4604 219 TPEEI-------ITPEVLSDI 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-238 |
4.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKS-MTALALLRLLPDAGRIVGGQIELGGtDLNDLSEraMRGVRGgRIGIIFQEPAT 104
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKStMIQLTNGLIISETGQTIVGDYAIPA-NLKKIKE--VKRLRK-EIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNpvmrvgDQIVETLAAHTPLRGAAARERAIDwlrrvGIPE-------PERRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:PRK13645 102 QLF------QETIEKDIAFGPVNLGENKQEAYK-----KVPEllklvqlPEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-241 |
4.29e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEglDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDL 82
Cdd:PRK11160 334 ADQVSLTLN--NVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAMRGvrggRIGIIFQEP---ATSLNPVMRvgdqivetLAAHTplrgaAARERAIDWLRRVGIP---EPERRID---- 152
Cdd:PRK11160 408 SEAALRQ----AISVVSQRVhlfSATLRDNLL--------LAAPN-----ASDEALIEVLQQVGLEkllEDDKGLNawlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 153 DYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAgiQREMGMAVLLITHDLavvRNVAH--HVAL 230
Cdd:PRK11160 471 EGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA--EHAQNKTVLMITHRL---TGLEQfdRICV 545
|
250
....*....|.
gi 490704625 231 MRGGEIVESAD 241
Cdd:PRK11160 546 MDNGQIIEQGT 556
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-253 |
4.64e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.13 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGRIVGGQIELGGTDLNDlSERAMRGVRGGR--IGIIFQEpa 103
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKS-TLLRHLSGLITGDKSAGSHIELLGRTVQR-EGRLARDIRKSRanTGYIFQQ-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 tsLNPVMR--VGDQIVETLAAHTPLRGAAAR-------ERAIDWLRRVGIPE-PERRIDdypfQFSGGQKQRLMIAIALA 173
Cdd:PRK09984 95 --FNLVNRlsVLENVLIGALGSTPFWRTCFSwftreqkQRALQALTRVGMVHfAHQRVS----TLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 174 AEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTF-FERPRHP 252
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFdNERFDHL 248
|
.
gi 490704625 253 Y 253
Cdd:PRK09984 249 Y 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-256 |
6.06e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVdvagESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLR-------LLPDAGriVGGQIE 73
Cdd:PRK14243 4 LNGTETVLRTENLNV----YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFR--VEGKVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 74 LGGTDLNDlSERAMRGVRGgRIGIIFQEPatslNPV-----------MRVG------DQIVETlaahtPLRGAAARERAI 136
Cdd:PRK14243 74 FHGKNLYA-PDVDPVEVRR-RIGMVFQKP----NPFpksiydniaygARINgykgdmDELVER-----SLRQAALWDEVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 137 DWLRRVGIpeperriddypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITH 216
Cdd:PRK14243 143 DKLKQSGL------------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTH 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490704625 217 DLAVVRNVAHHVALM---------RGGEIVESADARTFFERPRHPYARE 256
Cdd:PRK14243 209 NMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
292-527 |
7.07e-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: 76.80 E-value: 7.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVRKGVLRRV-----------AAWVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG------ 354
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAGiyppds 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 355 --ARVQGR------------AMLDGHD-------LLGASRRELRRLRQDIqIVFQDpfasldprmrvgdiLEEGIaslrp 413
Cdd:cd03220 77 gtVTVRGRvssllglgggfnPELTGREniylngrLLGLSRKEIDEKIDEI-IEFSE--------------LGDFI----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 414 elaasarraravgllervglpaDTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAE 493
Cdd:cd03220 137 ----------------------DLPVK---TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ 191
|
250 260 270
....*....|....*....|....*....|....
gi 490704625 494 LGIAyLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:cd03220 192 GKTV-ILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-256 |
7.26e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.77 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRI-VGGQIELGGtdlNDLSERAMRGVRGGR-IGIIFQEPat 104
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrVEGRVEFFN---QNIYERRVNLNRLRRqVSMVHPKP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 SLNPvMRVGDQI---VETLAAHTPLRGAAARERAID----WlrrvgiPEPERRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:PRK14258 98 NLFP-MSVYDNVaygVKIVGWRPKLEIDDIVESALKdadlW------DEIKHKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRG-----GEIVESADARTFFERPRHP 252
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDS 250
|
....
gi 490704625 253 YARE 256
Cdd:PRK14258 251 RTRE 254
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-239 |
8.24e-16 |
|
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: 75.43 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGrivggQIELGGTDLNDLsERAMRGVrggrIGIIFQE 101
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKS-TLLQLLTgdLKPQQG-----EITLDGVPVSDL-EKALSSL----ISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 P---ATSLnpvmrvgdqivetlaahtplrgaaareraidwLRRVGIpeperriddypfQFSGGQKQRLMIAIALAAEPKL 178
Cdd:cd03247 84 PylfDTTL--------------------------------RNNLGR------------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNVaHHVALMRGGEIVES 239
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
318-531 |
1.10e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGR-AMLDGHDLLgasrrelrrlrqdiqivfqdpFASL 394
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKST----LLRAIAGlwPYGSGRiARPAGARVL---------------------FLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEegiASLRPELAASARRARAVGLLERVGLPA-----DTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:COG4178 434 RPYLPLGTLRE---ALLYPATAEAFSDAELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 470 EPTSALDVSVQAQILDLLRDlqaEL-GIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPADT 531
Cdd:COG4178 511 EATSALDEENEAALYQLLRE---ELpGTTVISVGHRSTLAAF-HDRVLELTGDGSWQLLPAEA 569
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
316-527 |
1.21e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTT---TGKALLRLVEGARV-QGRAmldghdlLGASRRELRRLRQDIQIVFQDPf 391
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTlfmNLSGLLRPQKGAVLwQGKP-------LDYSKRGLLALRQQVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 aslDPRMRVGDILEEGIASLR----PELAASARRARAVGLLErvglpadtPTRYPHE----FSGGQRQRIAIARALAVEP 463
Cdd:PRK13638 87 ---EQQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTLVD--------AQHFRHQpiqcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 464 KVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-242 |
1.27e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMrgvrGGRIGIIFQE-PATSlnp 108
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKS----TLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQlPAAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 109 vmrvGDQIVETLAA-----HTPLR--GAAARERAIDWLRRVGI-PEPERRIDdypfQFSGGQKQRLMIAIALAAEPKLLI 180
Cdd:PRK10575 99 ----GMTVRELVAIgrypwHGALGrfGAADREKVEEAISLVGLkPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 181 ADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADA 242
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
318-533 |
2.18e-15 |
|
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: 75.66 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegaRV-QGRAMLDGHDLlgaSRREL-RRLRQDIQIVFQDpfASLD 395
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV---KPdSGKILLDGQDI---TKLPMhKRARLGIGYLPQE--ASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGD----ILEEgiaslrPELAASARRARAVGLLERVGLP--ADTPTRYpheFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:cd03218 88 RKLTVEEnilaVLEI------RGLSKKEREEKLEELLEEFHIThlRKSKASS---LSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 470 EPTSALD-VSVQaQILDLLRDLqAELGIAYLFITHNfgVVEYLA--DRIAVMHGGRIVEMGPADTVL 533
Cdd:cd03218 159 EPFAGVDpIAVQ-DIQKIIKIL-KDRGIGVLITDHN--VRETLSitDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
317-527 |
2.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGK---ALLRLVEGA------------RVQGRAMLDGHDLLGASRRE----LR 377
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnALLLPDTGTiewifkdeknkkKTKEKEKVLEKLVIQKTRFKkikkIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 378 RLRQDIQIVFQdpFASLDprmrvgdILEEGI------ASLRPELAASARRARAVGLLERVGLPADTPTRYPHEFSGGQRQ 451
Cdd:PRK13651 102 EIRRRVGVVFQ--FAEYQ-------LFEQTIekdiifGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 452 RIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNF-GVVEYlADRIAVMHGGRIVEMG 527
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLdNVLEW-TKRTIFFKDGKIIKDG 247
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-237 |
2.73e-15 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 74.93 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGRivgGQIELGGTDLNDLSERAMRGvrggRIGIIFQEP- 102
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKS-TLLKLLAGLYKPTS---GSVLLDGTDIRQLDPADLRR----NIGYVPQDVt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 --ATSLNPVMRVGDQIVETlaahtplrgaaarERAIDWLRRVGIPE-----P---ERRIDDYPFQFSGGQKQRLMIAIAL 172
Cdd:cd03245 89 lfYGTLRDNITLGAPLADD-------------ERILRAAELAGVTDfvnkhPnglDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 173 AAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVrNVAHHVALMRGGEIV 237
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
317-539 |
2.88e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGASRREL-RRLRQDIQIVFQDPFASLD 395
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTRQALQKNLvAYVPQSEEVDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRM--RVGDILEEGIASLRPELAASARraravglLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK15056 100 VVMmgRYGHMGWLRRAKKRDRQIVTAA-------LARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 474 ALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADrIAVMHGGRIVEMGPADTVLHAPRHE 539
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAENLE 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
291-527 |
3.44e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 291 VLDVQDLlvHYPVRKGVlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDL 368
Cdd:PRK13647 4 IIEVEDL--HFRYKDGT--------KALKGLSLSIPEGSKTALLGPNGAGKST----LLLHLNGIYLpqRGRVKVMGREV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 369 LGASRRELRrlrQDIQIVFQDPfaslDPRMRVGDILEE-GIASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSG 447
Cdd:PRK13647 70 NAENEKWVR---SKVGLVFQDP----DDQVFSSTVWDDvAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 448 GQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-217 |
3.72e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDvAGESGVTHAVkrlQLAVAQGETFALVGESGSGKSmTALALLRLL--PDAGRIVggqieLGGTD 78
Cdd:PRK10247 1 MQENSPLLQLQNVGYL-AGDAKILNNI---SFSLRAGEFKLITGPSGCGKS-TLLKIVASLisPTSGTLL-----FEGED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 79 LNDLSERAMRGvrggRIGIIFQEPATslnpvmrVGDQIVETLAAHTPLRGAAARERAI-DWLRRVGIPEP--ERRIDDyp 155
Cdd:PRK10247 71 ISTLKPEIYRQ----QVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPDPAIFlDDLERFALPDTilTKNIAE-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 156 fqFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHD 217
Cdd:PRK10247 138 --LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-236 |
4.88e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.99 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLsERAMRGVrggriGIIFQE 101
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGDLFIGEKRMNDV-PPAERGV-----GMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 PAtsLNPVMRVGDQIVETLAahtpLRGAAARERAidwlRRVG----IPEPERRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:PRK11000 84 YA--LYPHLSVAENMSFGLK----LAGAKKEEIN----QRVNqvaeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-238 |
5.14e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.49 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 18 AGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRI-VGGQI----ELGGTDLNDLSeram 87
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLagiypPDSGTVtVRGRVssllGLGGGFNPELT---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 rgvrgGRIGIIFqepatslnpVMRV----GDQIvetlaahtplrgaAARERAIdwlrrVGIPEPERRIDdYPF-QFSGGQ 162
Cdd:cd03220 101 -----GRENIYL---------NGRLlglsRKEI-------------DEKIDEI-----IEFSELGDFID-LPVkTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 163 KQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGiQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVE 238
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
306-525 |
6.25e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 306 GVLRRVAAWVeAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDghdllgasrrelrrlrqdiQI 385
Cdd:COG2401 35 GVELRVVERY-VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVP-------------------DN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 386 VFQDPFASLDPRMRVGDILEegiaslrpelaasarrarAVGLLERVGLpADTPT--RYPHEFSGGQRQRIAIARALAVEP 463
Cdd:COG2401 95 QFGREASLIDAIGRKGDFKD------------------AVELLNAVGL-SDAVLwlRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 464 KVLICDEPTSALDVSVqAQILDL-LRDLQAELGIAYLFITHNFGVVEYLA-DRIAVMH-GGRIVE 525
Cdd:COG2401 156 KLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGyGGVPEE 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
315-529 |
8.31e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGA----RVQGR--AMLDGhDLLGASRRElrrlrqDIQIVFQ 388
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTsgtyRVAGQdvATLDA-DALAQLRRE------HFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 389 DpfASLDPRMRVGDILEegIASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:PRK10535 94 R--YHLLSHLTAAQNVE--VPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPA 529
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
318-533 |
9.28e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALL------RLVEGARVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPF 391
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltggGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 A-SLDPRMRVGDILEegiaSLRPELAASARRARAVGLLERVGLPAdTPTRYPHEFSGGQRQRIAIARALA---------V 461
Cdd:PRK13547 97 AfSAREIVLLGRYPH----ARRAGALTHRDGEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 462 EPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-236 |
9.96e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDLNDLsERAMRGvrggrIGIIF 99
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMV--AGleRITSGEIWIGGRVVNEL-EPADRD-----IAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEPAtsLNPVMRVgdqiVETLAAHTPLRGAAARERAidwlRRV----GIPEPERRIDDYPFQFSGGQKQRLMIAIALAAE 175
Cdd:PRK11650 83 QNYA--LYPHMSV----RENMAYGLKIRGMPKAEIE----ERVaeaaRILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 176 PKLLIADEPTTALDVTVQAQV-LELLAgIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMrLEIQR-LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-236 |
1.04e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 5 APLLRIEGLDVdvagESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLR-----LLPDAGrivggQIELGGTDL 79
Cdd:PRK09536 1 MPMIDVSDLSV----EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKT----TLLRaingtLTPTAG-----TVLVAGDDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 80 NDLSERAMrgvrGGRIGIIFQEPATSLNPVMRvgdQIVET--------LAAHTPlRGAAARERAIDwlrRVGIPeperRI 151
Cdd:PRK09536 68 EALSARAA----SRRVASVPQDTSLSFEFDVR---QVVEMgrtphrsrFDTWTE-TDRAAVERAME---RTGVA----QF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 152 DDYPF-QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:PRK09536 133 ADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVL 211
|
....*.
gi 490704625 231 MRGGEI 236
Cdd:PRK09536 212 LADGRV 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
259-536 |
1.15e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 259 EAIPTFakrgrpLSAQGRAADQG-KAAPEAGAVVLDVQDLLVHYPVRKgvlrrvaawvEAVNGVTFTLRAGETLALLGES 337
Cdd:PRK11174 322 ESLVTF------LETPLAHPQQGeKELASNDPVTIEAEDLEILSPDGK----------TLAGPLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 338 GCGKTTTGKALLrlveG-ARVQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPF---ASLDPRMRVG--DILEEGIASl 411
Cdd:PRK11174 386 GAGKTSLLNALL----GfLPYQGSLKINGIEL---RELDPESWRKHLSWVGQNPQlphGTLRDNVLLGnpDASDEQLQQ- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 412 rpelaasarraravgLLERVGLpadtptrypHEF-------------------SGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PRK11174 458 ---------------ALENAWV---------SEFlpllpqgldtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPT 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 473 SALDVSVQAQILDLLRdlQAELGIAYLFITHNfgvVEYLA--DRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:PRK11174 514 ASLDAHSEQLVMQALN--AASRRQTTLMVTHQ---LEDLAqwDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-237 |
1.53e-14 |
|
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: 76.33 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVThaVKRLQLAVAQGETFALVGESGSGKSMtalaLLRLLPDAGRIVGGQIELGGTDLNDLSeram 87
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKST----LARLLVGVWPPTAGSVRLDGADLSQWD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 RGVRGGRIGIIFQE----PATslnpvmrvgdqIVETLAahtplR-GAAARERAIDWLRRVGIPE-----PER---RIDDY 154
Cdd:COG4618 401 REELGRHIGYLPQDvelfDGT-----------IAENIA-----RfGDADPEKVVAAAKLAGVHEmilrlPDGydtRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 155 PFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVrNVAHHVALMRGG 234
Cdd:COG4618 465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDG 542
|
...
gi 490704625 235 EIV 237
Cdd:COG4618 543 RVQ 545
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
322-503 |
1.61e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 322 TFTLRAGETLALLGESGCGKTTtgkaLLRLVEG------ARVQgraMLDGHDLLGASRRelrrlrqdiqivfqdpfasld 395
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSS----LFRALAGlwpwgsGRIG---MPEGEDLLFLPQR--------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGdileegiaSLRPELaasarraravgllervglpadtptRYP--HEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:cd03223 73 PYLPLG--------TLREQL------------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190
....*....|....*....|....*....|
gi 490704625 474 ALDVSVQAQILDLLRdlqaELGIAYLFITH 503
Cdd:cd03223 121 ALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-237 |
1.75e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.08 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRIVggqieLGGTDLNDLSErAMRGVrggriGIIFQEp 102
Cdd:PRK10771 13 HLPMRFDLTVERGERVAILGPSGAGKS-TLLNLIAgfLTPASGSLT-----LNGQDHTTTPP-SRRPV-----SMLFQE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 aTSLNPVMRVGDQIveTLAAHTPLR-GAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIA 181
Cdd:PRK10771 80 -NNLFSHLTVAQNI--GLGLNPGLKlNAAQREKLHAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-237 |
2.31e-14 |
|
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: 72.75 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRI-VGGQIElggtdlndlSERAMRGVRggRIGIIF-QE 101
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKT-TTLKILSglLQPTSGEVrVAGLVP---------WKRRKKFLR--RIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 PATSLN-PVMrvgdqivETLAAH------TPLRGAAARERAIDWLrrvgipEPERRIDDYPFQFSGGQKQRLMIAIALAA 174
Cdd:cd03267 104 TQLWWDlPVI-------DSFYLLaaiydlPPARFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-238 |
2.49e-14 |
|
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: 72.14 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLSERAMRgvrgGRIGIIFQEpats 105
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDLR----SRISIIPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 lnPVMRVGdqiveTLAAHTPLRGAAARERAIDWLRRVGIPE-----PER---RIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:cd03244 87 --PVLFSG-----TIRSNLDPFGEYSDEELWQALERVGLKEfveslPGGldtVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 178 LLIADEPTTALDVTVQAQVLELlagIQREM-GMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-234 |
2.53e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEGLDVDVAGesgvTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDL 82
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKT----TVFNCLTGFYKPTGGTILLRGQHIEGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SeramrGVRGGRIGII--FQEpaTSLNPVMRVgdqiVETL--AAHTPLRG----------------AAARERAIDWLRRV 142
Cdd:PRK11300 73 P-----GHQIARMGVVrtFQH--VRLFREMTV----IENLlvAQHQQLKTglfsgllktpafrraeSEALDRAATWLERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 143 GIPEPERRIDDypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVR 222
Cdd:PRK11300 142 GLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVM 218
|
250
....*....|..
gi 490704625 223 NVAHHVALMRGG 234
Cdd:PRK11300 219 GISDRIYVVNQG 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
328-552 |
2.84e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 328 GETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLGASRRELRR----LRQDI----QIVFQD-------PFA 392
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLM--TPAHGHVWLDGEHIQHYASKEVARriglLAQNAttpgDITVQElvargryPHQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDPRMRVGDilEEGIASlrpelaasarRARAVGLLERVGLPADTptrypheFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PRK10253 111 PLFTRWRKED--EEAVTK----------AMQATGITHLADQSVDT-------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 473 SALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGpadtvlhAPRHEMTQRLLAAVPRLR 552
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERIYGLR 244
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
320-533 |
2.96e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.32 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDP--FA----- 392
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER--GRILIDGCDI---SKFGLMDLRKVLGIIPQAPvlFSgtvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDP--RMRVGDILEEgiaslrpelaasarraravglLERVGLpADTPTRYP-----------HEFSGGQRQRIAIARAL 459
Cdd:PLN03130 1332 NLDPfnEHNDADLWES---------------------LERAHL-KDVIRRNSlgldaevseagENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 460 AVEPKVLICDEPTSALDVSVQAQILDLLRDlqaEL-GIAYLFITHNFGVVeYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIRE---EFkSCTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
157-235 |
3.26e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.78 E-value: 3.26e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemgmAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:cd03221 70 QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
321-544 |
3.50e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDP--FASLDP 396
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTT----LLRLIGGqiAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGalFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEEGiASLRPELAASARRARavglLERVGLPAdTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:PRK11831 102 FDNVAYPLREH-TQLPAPLLHSTVMMK----LEAVGLRG-AAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 477 VSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVLHAPRHEMTQRL 544
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFL 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-219 |
5.14e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTALALLR--LLPDAGRI-VGGQIElggtdlndlSERAMRGVRggRIGIIF-Q 100
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgiLVPTSGEVrVLGYVP---------FKRRKEFAR--RIGVVFgQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EpaTSLN---PVMrvgdqivETLaahtplrgaaareraiDWLRRV-GIPEPE--RRIDDY-------PF------QFSGG 161
Cdd:COG4586 104 R--SQLWwdlPAI-------DSF----------------RLLKAIyRIPDAEykKRLDELvelldlgELldtpvrQLSLG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 162 QKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLA 219
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-236 |
6.42e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 3 ASAPLLRIEgldvDVAGEsgvthAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDL 82
Cdd:PRK15439 264 AGAPVLTVE----DLTGE-----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP----ARGGRIMLNGKEINAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 SERAM-----------RGVRGgrigiIFQEPATSLNpvmrvgdqiVETLAAHTP---LRGAaaRERAI--DWLRRVGIP- 145
Cdd:PRK15439 331 STAQRlarglvylpedRQSSG-----LYLDAPLAWN---------VCALTHNRRgfwIKPA--RENAVleRYRRALNIKf 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 146 ----EPERRIddypfqfSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAVV 221
Cdd:PRK15439 395 nhaeQAARTL-------SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEI 466
|
250
....*....|....*
gi 490704625 222 RNVAHHVALMRGGEI 236
Cdd:PRK15439 467 EQMADRVLVMHQGEI 481
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
317-537 |
6.76e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.56 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGHDLLGAS-----RRELRRLRQDIQI------ 385
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPT--GGTILLRGQHIEGLPghqiaRMGVVRTFQHVRLfremtv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 386 ---------------VFQDPFASLDPRMRVGDILEEGIASLRpelaasarrarAVGLLERVGLPADTptrypheFSGGQR 450
Cdd:PRK11300 98 ienllvaqhqqlktgLFSGLLKTPAFRRAESEALDRAATWLE-----------RVGLLEHANRQAGN-------LAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 451 QRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
....*..
gi 490704625 531 TVLHAPR 537
Cdd:PRK11300 240 EIRNNPD 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-244 |
7.53e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 25 HAVKRLQLAVAQGETFALVGESGSGKSmTalaLLRLL-----PDAGRIvggqielggtdlndlseramrgVRGGRIGIIF 99
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKS-T---LLKLIagilePTSGRV----------------------EVNGRVSALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 qEPATSLNPVMRVGDQIVetlaahtpLRGAAAreraidwlrrvGIP--EPERRID------------DYPFQ-FSGGQKQ 164
Cdd:COG1134 94 -ELGAGFHPELTGRENIY--------LNGRLL-----------GLSrkEIDEKFDeivefaelgdfiDQPVKtYSSGMRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 165 RLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADART 244
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-216 |
7.65e-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: 70.27 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAGR----IVGGQIELGGTDLNDLSERAmrgvrggRIGIIFQEp 102
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKS----TLLNAL--AGRrtglGVSGEVLINGRPLDKRSFRK-------IIGYVPQD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 atslnpvmrvgDQIVETLAAHTPLRGAAAreraidwLRRVgipeperriddypfqfSGGQKQRLMIAIALAAEPKLLIAD 182
Cdd:cd03213 91 -----------DILHPTLTVRETLMFAAK-------LRGL----------------SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190
....*....|....*....|....*....|....
gi 490704625 183 EPTTALDVTVQAQVLELLAGIqREMGMAVLLITH 216
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-248 |
8.63e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLnDLSERAMRGVRGgRIGIIFQEPatsl 106
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGKPL-DYSKRGLLALRQ-QVATVFQDP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 npvmrvgDQIVetlaAHTPLRGAAAREraidwLRRVGIPEPE--RRIDD------------YPFQ-FSGGQKQRLMIAIA 171
Cdd:PRK13638 87 -------EQQI----FYTDIDSDIAFS-----LRNLGVPEAEitRRVDEaltlvdaqhfrhQPIQcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 172 LAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFER 248
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
34-238 |
9.68e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 74.09 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 34 VAQGETFALVGESGSGKSmtalALLRLL-----PDAGRIVggqieLGGTDLNDLSERAMRGVrggrIGIIFQEpaTSL-N 107
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKS----TLARLLfrfydVTSGRIL-----IDGQDIRDVTQASLRAA----IGIVPQD--TVLfN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 108 pvmrvgDQIVETLAAHTPlrGA-------AARERAID---------WLRRVGipepERriddyPFQFSGGQKQRLMIAIA 171
Cdd:COG5265 446 ------DTIAYNIAYGRP--DAseeeveaAARAAQIHdfieslpdgYDTRVG----ER-----GLKLSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 172 LAAEPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
321-548 |
1.33e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTTGKALLRLVEGarvQGRAMLDGHDLLGASRRELRRLR----QDIQIVFQdpfasldp 396
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQPLEAWSAAELARHRaylsQQQTPPFA-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 rMRVGDILeegiASLRPELAASARRARAVGLL-ERVGLpADTPTRYPHEFSGGQRQRIAIARA-LAVEP------KVLIC 468
Cdd:PRK03695 84 -MPVFQYL----TLHQPDKTRTEAVASALNEVaEALGL-DDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 469 DEPTSALDVSVQAqILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVlhaprheMTQRLLAAV 548
Cdd:PRK03695 158 DEPMNSLDVAQQA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV-------LTPENLAQV 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
279-518 |
1.37e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 279 DQGKAAPEAGAVvlDVQDLLVHYPVRKGVlrrvaawvEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQ 358
Cdd:PTZ00265 372 DDGKKLKDIKKI--QFKNVRFHYDTRKDV--------EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--PTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 359 GRAML-DGHDLLGASrreLRRLRQDIQIVFQDPFA--------------SLDPRMRVGDILEE-GIASLRPELAASARRA 422
Cdd:PTZ00265 440 GDIIInDSHNLKDIN---LKWWRSKIGVVSQDPLLfsnsiknnikyslySLKDLEALSNYYNEdGNDSQENKNKRNSCRA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 423 RAVGLLERVGLPADT----------------------------------PTRY-------PHEFSGGQRQRIAIARALAV 461
Cdd:PTZ00265 517 KCAGDLNDMSNTTDSneliemrknyqtikdsevvdvskkvlihdfvsalPDKYetlvgsnASKLSGGQKQRISIARAIIR 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 462 EPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYlADRIAVM 518
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVL 652
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
315-527 |
1.81e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLLGASRRELRRLrqDIQIVFQDPFA 392
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKST----LMKVLSGIHepTKGTITINNINYNKLDHKLAAQL--GIGIIYQELSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 ----SLDPRMRVGDILEEGIASLrPELAASARRARAVGLLERVGLPADtPTRYPHEFSGGQRQRIAIARALAVEPKVLIC 468
Cdd:PRK09700 92 idelTVLENLYIGRHLTKKVCGV-NIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMG 527
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
148-520 |
1.87e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 148 ERRIDdypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVlellAGIQREM--GMAVLLITHDLAVVRNVA 225
Cdd:PRK13409 207 DRDIS----ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV----ARLIRELaeGKYVLVVEHDLAVLDYLA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 226 HHVALMRGgeiVESAdartfFERPRHPY-ARElfeAIPTFAK----------RGRPLSAQGRAADQGKAAPeagaVVLDV 294
Cdd:PRK13409 279 DNVHIAYG---EPGA-----YGVVSKPKgVRV---GINEYLKgylpeenmriRPEPIEFEERPPRDESERE----TLVEY 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 295 QDLLVHYP-----VRKGvlrrvaawveavngvtfTLRAGETLALLGESGCGKTTTGKAL---LRLVEGArvqgramldgh 366
Cdd:PRK13409 344 PDLTKKLGdfsleVEGG-----------------EIYEGEVIGIVGPNGIGKTTFAKLLagvLKPDEGE----------- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 367 dllgasrrelrrLRQDIQIVFQDPFASLDPRMRVGDILEEgIAS------LRPELaasarraravglLERVGLPaDTPTR 440
Cdd:PRK13409 396 ------------VDPELKISYKPQYIKPDYDGTVEDLLRS-ITDdlgssyYKSEI------------IKPLQLE-RLLDK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 441 YPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHG 520
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-249 |
2.62e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 69.49 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMT---ALALLRllPDAGRIvggqiELGGTDLNDL--SERAMRGvrggrIG 96
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVK--PDSGKI-----LLDGQDITKLpmHKRARLG-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 97 IIFQEPatSLNPVMRVGDQIVETLAAHTPLRgAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:cd03218 79 YLPQEA--SIFRKLTVEENILAVLEIRGLSK-KEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 177 KLLIADEPTTALD-VTV---QAQVLELlagiqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERP 249
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVqdiQKIIKIL-----KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
318-533 |
3.50e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDLLGASRRElrRLRQDIQIVFQDpfASLDPR 397
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIV--PRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQE--ASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEeGIASLRPELAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALD- 476
Cdd:PRK10895 93 LSVYDNLM-AVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDp 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 477 VSVQ--AQILDLLRDlqaeLGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:PRK10895 171 ISVIdiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
318-525 |
3.60e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARvqGRAMLDGHDLLGASRRELRRLrqdIQIVFQDP-FASLDP 396
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK--GRIMIDDCDVAKFGLTDLRRV---LSIIPQSPvLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEEGIASLRPELaasarraravgllERVGLpADTPTRYP-----------HEFSGGQRQRIAIARALAVEPKV 465
Cdd:PLN03232 1327 RFNIDPFSEHNDADLWEAL-------------ERAHI-KDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 466 LICDEPTSALDVSVQAQILDLLRDlqaEL-GIAYLFITHNFGVVeYLADRIAVMHGGRIVE 525
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE---EFkSCTMLVIAHRLNTI-IDCDKILVLSSGQVLE 1449
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
315-531 |
4.69e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARVQ--GRAMLDGHDLLGASRRELRRLrqDIQIVFQDP-- 390
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKST----LMKIIAGIVPPdsGTLEIGGNPCARLTPAKAHQL--GIYLVPQEPll 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 FASLDP------RMRVGDILEEGIASLRPELAASARRARAVGLLErvglPADtptryphefsggqRQRIAIARALAVEPK 464
Cdd:PRK15439 98 FPNLSVkenilfGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLE----VAD-------------RQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 465 VLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADT 531
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-243 |
5.12e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.10 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 29 RLQ---LAVAQGETFALVGESGSGKSmTALALLrllpdAGRIVG-GQIELGGTDLNDLSERAMRGVRGgrigiiF----Q 100
Cdd:COG4138 11 RLGpisAQVNAGELIHLIGPNGAGKS-TLLARM-----AGLLPGqGEILLNGRPLSDWSAAELARHRA------YlsqqQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EPAtslnPVMRVGdqivETLAAHTPLRG-AAARERAIDWL-RRVGI-PEPERRIDdypfQFSGGQKQRLMIAIALA---- 173
Cdd:COG4138 79 SPP----FAMPVF----QYLALHQPAGAsSEAVEQLLAQLaEALGLeDKLSRPLT----QLSGGEWQRVRLAAVLLqvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 174 ---AEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADAR 243
Cdd:COG4138 147 tinPEGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
319-522 |
7.31e-13 |
|
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: 67.49 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTTGKALLRlvEGARVQGRAMLDGHD--------LLGASRRElrrlrqdiQIVFQDP 390
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEKLSGSVSVPGSIayvsqepwIQNGTIRE--------NILFGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 F-----------ASLDPRMrvgDILEEGIASlrpelaasarrarAVGllER-VGLpadtptryphefSGGQRQRIAIARA 458
Cdd:cd03250 92 FdeeryekvikaCALEPDL---EILPDGDLT-------------EIG--EKgINL------------SGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 459 LAVEPKVLICDEPTSALDVSVQAQILD--LLRDLQaeLGIAYLFITHNFGVVEYlADRIAVMHGGR 522
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLL--NNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
267-536 |
7.38e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 267 RGRPLSAQGRAADQGKAAPEAGAVVLDVQDLLVHYPvrkgvlrrvAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGK 346
Cdd:PRK10789 289 RIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQFTYP---------QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 347 ALLRLVEGArvQGRAMLDGHDLlgaSRRELRRLRQDIQIVFQDPFAsldprmrVGDILEEGIASLRPELAASArraravg 426
Cdd:PRK10789 360 LIQRHFDVS--EGDIRFHDIPL---TKLQLDSWRSRLAVVSQTPFL-------FSDTVANNIALGRPDATQQE------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 427 lLERVGLPADT-------PTRYPHE-------FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRdlQA 492
Cdd:PRK10789 421 -IEHVARLASVhddilrlPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR--QW 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490704625 493 ELGIAYLFITHNFGVVEYlADRIAVMHGGRIVEMGPADTVLHAP 536
Cdd:PRK10789 498 GEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-237 |
8.46e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLRLLP-DAGRIVggqIELGGTDLNDLSERAMRGvrggrIGIIFQEPatS 105
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNII---IDDEDISLLPLHARARRG-----IGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490704625 186 TALDvtvQAQVLELLAGIQ--REMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK10895 166 AGVD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-237 |
9.08e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAV-----AQGETfALVGESGSGKSmtalALLRLL-----PDAGRIVggqieLGGTDLNDLSERAMRGVRGGRIGIIF 99
Cdd:PRK11144 13 LCLTVnltlpAQGIT-AIFGRSGAGKT----SLINAIsgltrPQKGRIV-----LNGRVLFDAEKGICLPPEKRRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 100 QEpaTSLNPVMRV-GDqivetlaahtpLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRLMIAIALAAEPKL 178
Cdd:PRK11144 83 QD--ARLFPHYKVrGN-----------LRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 179 LIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
319-526 |
1.08e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--------ARVQGRA--------------------MLDGHDLLG 370
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKST----LLKILAGelepdsgeVSIPKGLrigylpqeppldddltvldtVLDGDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 ASRRELRRLRQDIQIVFQDPfasldprMRVGDILEEGIA----SLRPELAAsarraravgLLERVGLPADTPTRYPHEFS 446
Cdd:COG0488 91 ALEAELEELEAKLAEPDEDL-------ERLAELQEEFEAlggwEAEARAEE---------ILSGLGFPEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 447 GGQRQRIAIARALAVEPKVLICDEPTSALDV-SVQaqildLLRDLQAELGIAYLFITHNfgvvEYLADRIAvmhgGRIVE 525
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD----RYFLDRVA----TRILE 221
|
.
gi 490704625 526 M 526
Cdd:COG0488 222 L 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
314-509 |
1.08e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.00 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 314 WVEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGAR--VQGRAMLDGHDLlgasrRELRRLRQDiQIVFQDPF 391
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTT----LLRILAGLLrpDSGEVRWNGTPL-----AEQRDEPHE-NILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLDPRMRVGDILEEGIASLRPELAASARRARAVGLLERVGLPAdtptrypHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPA-------AQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVE 509
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-504 |
1.32e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRElrrlrqdiQIVFQDPFASLDPR 397
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTT----LLRLIAGllPPAAGTIKLDGGDIDDPDVAE--------ACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEEGIASLRPELAASARRaravglLERVGLP--ADTPTRYpheFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEELDIAAA------LEAVGLAplAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*....
gi 490704625 476 DVSVQAQILDLLRDLQAELGIAyLFITHN 504
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIV-IAATHI 186
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-238 |
1.64e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.05 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEpa 103
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD----IDEGEILLDGHDLRDYTLASLRN----QVALVSQN-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 tslnpVMRVGDQIVETLA-------AHTPLRGAAARERAIDWLRRV--GIpepERRIDDYPFQFSGGQKQRLMIAIALAA 174
Cdd:PRK11176 426 -----VHLFNDTIANNIAyarteqySREQIEEAARMAYAMDFINKMdnGL---DTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREmgMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-238 |
2.30e-12 |
|
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: 66.28 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESgvTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIVGGQIELGGTDLNDLSEra 86
Cdd:cd03369 7 IEVENLSVRYAPDL--PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDLRS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 87 mrgvrggRIGIIFQEPA-------TSLNPVMRVGD-QIVETLaahtplrgaaareraidwlrrvgipeperRIDDYPFQF 158
Cdd:cd03369 83 -------SLTIIPQDPTlfsgtirSNLDPFDEYSDeEIYGAL-----------------------------RVSEGGLNL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELlagIQREM-GMAVLLITHDLAVVRNVAhHVALMRGGEIV 237
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT---IREEFtNSTILTIAHRLRTIIDYD-KILVMDAGEVK 202
|
.
gi 490704625 238 E 238
Cdd:cd03369 203 E 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
148-520 |
2.55e-12 |
|
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: 69.43 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 148 ERRIDDypfqFSGGQKQRLMIAIALAAEPKLLIADEPTTALDV----TVqAQVLELLAgiqrEMGMAVLLITHDLAVVRN 223
Cdd:COG1245 207 DRDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrlNV-ARLIRELA----EEGKYVLVVEHDLAILDY 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 224 VAHHVALMRGgeiVESAdartfFERPRHPY-ARElfeAIPTFAK----------RGRPLSAQGRAADQGKAAPeagaVVL 292
Cdd:COG1245 278 LADYVHILYG---EPGV-----YGVVSKPKsVRV---GINQYLDgylpeenvriRDEPIEFEVHAPRREKEEE----TLV 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 293 DVQDLLVHYP-----VRKGVLRRvaawveavngvtftlraGETLALLGESGCGKTTTGKAL---LRLVEGArvqgramld 364
Cdd:COG1245 343 EYPDLTKSYGgfsleVEGGEIRE-----------------GEVLGIVGPNGIGKTTFAKILagvLKPDEGE--------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 365 ghdllgasrrelrrLRQDIQIVFQDPFASLDPRMRVGDILEEGIAS------LRPELaasarraravglLERVGLPA--D 436
Cdd:COG1245 397 --------------VDEDLKISYKPQYISPDYDGTVEEFLRSANTDdfgssyYKTEI------------IKPLGLEKllD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 437 tptRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIA 516
Cdd:COG1245 451 ---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
....
gi 490704625 517 VMHG 520
Cdd:COG1245 528 VFEG 531
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-234 |
2.81e-12 |
|
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: 70.04 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESgvTHAVKRLQLAVAQGETFALVGESGSGKSMTalalLRLLPDAGRIVGGQIELGGTD-LNDLSEr 85
Cdd:TIGR01257 1937 ILRLNELTKVYSGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKSiLTNISD- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 amrgvrggrigiIFQEpaTSLNPVMRVGDQIV---ETLAAHTPLRGAAARE--RAIDW-LRRVGIPEPERRIDDypfQFS 159
Cdd:TIGR01257 2010 ------------VHQN--MGYCPQFDAIDDLLtgrEHLYLYARLRGVPAEEieKVANWsIQSLGLSLYADRLAG---TYS 2072
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 160 GGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGG 234
Cdd:TIGR01257 2073 GGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-508 |
3.40e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGarvqgramldghdLLGASRRELRRLRQ-DIQIVFQ----DP-- 390
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKST----LVRVVLG-------------LVAPDEGVIKRNGKlRIGYVPQklylDTtl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 ------FASLDPRMRVGDILEEgiaslrpelaasarraravglLERV--GLPADTPTRyphEFSGGQRQRIAIARALAVE 462
Cdd:PRK09544 83 pltvnrFLRLRPGTKKEDILPA---------------------LKRVqaGHLIDAPMQ---KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490704625 463 PKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVV 508
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-241 |
3.93e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSMTALALLRLLPdagriVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPatslnpv 109
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----YQGSLKINGIELRELDPESWRK----HLSWVGQNP------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 mrvgdQIVE-TLAAHTPLRGAAARERAIDW-LRRVGIPEPERRID---DYPFQ-----FSGGQKQRLMIAIALAAEPKLL 179
Cdd:PRK11174 433 -----QLPHgTLRDNVLLGNPDASDEQLQQaLENAWVSEFLPLLPqglDTPIGdqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 180 IADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVRNVaHHVALMRGGEIVESAD 241
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-522 |
4.29e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.01 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 319 NGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGarvqgramldghdllgasrrelrRLRQDIQIVfqdpfaSLDPRM 398
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKST----LLKLIAG-----------------------ELEPDEGIV------TWGSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 399 RVGdileegiaslrpelaasarraravgllervglpadtptrYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVS 478
Cdd:cd03221 64 KIG---------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490704625 479 VQAQILDLLRDLQAelgiAYLFITHNFGVVEYLADRIAVMHGGR 522
Cdd:cd03221 105 SIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
318-533 |
4.77e-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: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLrlVEGARVQGRAMLDGHDLLGASRRELRRLRQDIQIVFQDPfasLDPR 397
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALL--AEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKA---LNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 mRVGDILEEgiASLRPELAAsarraravgllervgLPADTPTRYPHE---FSGGQRQRIAIARALAVEPKVLICDEPTSA 474
Cdd:TIGR00957 729 -YYQQVLEA--CALLPDLEI---------------LPSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 475 LDVSVQAQILDLLRDLQAEL-GIAYLFITHNfgvVEYL--ADRIAVMHGGRIVEMGPADTVL 533
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVLkNKTRILVTHG---ISYLpqVDVIIVMSGGKISEMGSYQELL 849
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
316-527 |
5.22e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDLLGASRRElrRLRQDIQIVFQDPF---- 391
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 --------------------ASLDpRMRVGDILEEGIASLRpelaasarraravgllervgLPADTPTRYPHE-FSGGQR 450
Cdd:PRK09580 93 vsnqfflqtalnavrsyrgqEPLD-RFDFQDLMEEKIALLK--------------------MPEDLLTRSVNVgFSGGEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 451 QRIAIARALAVEPKVLICDEPTSALDV---SVQAQILDLLRDLQAelgiAYLFITHNFGVVEYLA-DRIAVMHGGRIVEM 526
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKS 227
|
.
gi 490704625 527 G 527
Cdd:PRK09580 228 G 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
32-221 |
9.13e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 32 LAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqielggtdlndlsERAmrgvRGGRIGIIFQEpaTSLNPVM 110
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVI----------------KRN----GKLRIGYVPQK--LYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 111 RVgdqiveTLAAHTPLRGAAARERAIDWLRRVgipePERRIDDYPFQ-FSGGQKQRLMIAIALAAEPKLLIADEPTTALD 189
Cdd:PRK09544 83 PL------TVNRFLRLRPGTKKEDILPALKRV----QAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|..
gi 490704625 190 VTVQAQVLELLAGIQREMGMAVLLITHDLAVV 221
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-246 |
1.11e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 14 DVDVAGESGVThAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLNdlseramRGVRGG 93
Cdd:PRK15056 11 DVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPTR-------QALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 94 RIGIIFQEPATSLNPVMRVGDQIVETLAAHTP-LRGAAARERAI--DWLRRVGIPE-PERRIDdypfQFSGGQKQRLMIA 169
Cdd:PRK15056 79 LVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGwLRRAKKRDRQIvtAALARVDMVEfRHRQIG----ELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 170 IALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRgGEIVESADARTFF 246
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTF 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-239 |
1.11e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSmTALALLrllpdAGRIVG-GQIELGGTDLNDLSERAMRGVRGGrigIIFQEPATSLNP 108
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARM-----AGLLPGsGSIQFAGQPLEAWSAAELARHRAY---LSQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 109 VMrvgdqivETLAAHTP-LRGAAARERAIDWL-RRVGI-PEPERRIDdypfQFSGGQKQR-------LMIAIALAAEPKL 178
Cdd:PRK03695 86 VF-------QYLTLHQPdKTRTEAVASALNEVaEALGLdDKLGRSVN----QLSGGEWQRvrlaavvLQVWPDINPAGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 179 LIADEPTTALDVTVQA---QVLELLAgiqrEMGMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAaldRLLSELC----QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-238 |
1.18e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVAGEsgvtHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRIVGGQielggtdln 80
Cdd:COG0488 314 KVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLagelePDSGTVKLGE--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 81 dlseramrGVRggrIGIIFQEPATsLNPVMRVgdqiVETLAAHTPlrgAAARERAIDWLRRVGIP--EPERRIDDypfqF 158
Cdd:COG0488 377 --------TVK---IGYFDQHQEE-LDPDKTV----LDELRDGAP---GGTEQEVRGYLGRFLFSgdDAFKPVGV----L 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDV-TVQAqVLELLAGIQremGmAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
.
gi 490704625 238 E 238
Cdd:COG0488 509 E 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
27-258 |
1.31e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMT---ALALLRllPDAGRIvggqiELGGTDLNDLS--ERAMRGvrggrIGIIFQE 101
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTfymIVGLVK--PDSGRI-----FLDGEDITHLPmhKRARLG-----IGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 PAtslnpVMR---VGDQIvetLAA--HTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEP 176
Cdd:COG1137 87 AS-----IFRkltVEDNI---LAVleLRKLSKKEREERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 177 KLLIADEPTTALD-VTV---QAQVLELlagiqREMGMAVlLIT-HDlavVR---NVAHHVALMRGGEIVESADARTFFEr 248
Cdd:COG1137 156 KFILLDEPFAGVDpIAVadiQKIIRHL-----KERGIGV-LITdHN---VRetlGICDRAYIISEGKVLAEGTPEEILN- 225
|
250
....*....|
gi 490704625 249 prHPYARELF 258
Cdd:COG1137 226 --NPLVRKVY 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-216 |
1.65e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 15 VDVAGES---GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLL-PDAGRIvggqielggTDLNDLSERAMRGV 90
Cdd:PRK13536 42 IDLAGVSksyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKI---------TVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 91 RGgRIGIIFQEPATSLNPVMRvgdqivETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRLMIAI 170
Cdd:PRK13536 113 RA-RIGVVPQFDNLDLEFTVR------ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490704625 171 ALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITH 216
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTH 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
316-530 |
1.67e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDLLGASRRElrRLRQDIQIVFQDPFASld 395
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEE--RAHLGIFLAFQYPIEI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDILEEGIASLR-----PELAASARRARAVGLLERVGLPADTPTRYPHE-FSGGQRQRIAIARALAVEPKVLICD 469
Cdd:CHL00131 97 PGVSNADFLRLAYNSKRkfqglPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 470 EPTSALDVSVQAQI---LDLLRDLQAelgiAYLFITHNFGVVEYLA-DRIAVMHGGRIVEMGPAD 530
Cdd:CHL00131 177 ETDSGLDIDALKIIaegINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
317-527 |
1.82e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGET--------------LALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLLGASRRELRrlr 380
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKST----LASLLMGYYPltEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 381 QDIQIVFQDPF---ASLDPRMRVG-DILEEGIaslrpelaasARRARAVGLLERV-GLPADTPTRYPHE---FSGGQRQR 452
Cdd:PRK10790 415 QGVAMVQQDPVvlaDTFLANVTLGrDISEEQV----------WQALETVQLAELArSLPDGLYTPLGEQgnnLSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 453 IAIARALAVEPKVLICDEPTSALDVSV-QA--QILDLLRDLQAELGIAYLFIThnfgVVEylADRIAVMHGGRIVEMG 527
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTeQAiqQALAAVREHTTLVVIAHRLST----IVE--ADTILVLHRGQAVEQG 556
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-261 |
2.41e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVRGgRIGIIFQEPA--TSLN 107
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGAlfTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 108 pvmrVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIPEPERRIddyPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTA 187
Cdd:PRK11831 101 ----VFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490704625 188 LDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPrHPYARELFEAI 261
Cdd:PRK11831 174 QDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
159-493 |
2.65e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTvqaqVLELLAGIQREMGMAVLLITHDLAVVRNVAHH-VALMRGGEI- 236
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRiVDLDRGKLVs 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 237 -----------------VEsADARTFFERP---RHPYARELFEAIPTFAK-RGRPLSA-----------QGRAADQGKAA 284
Cdd:PRK11147 234 ypgnydqyllekeealrVE-ELQNAEFDRKlaqEEVWIRQGIKARRTRNEgRVRALKAlrrerserrevMGTAKMQVEEA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 285 PEAGAVVLDVQDllVHYPVRKGVLrrvaawveaVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLvegarvqgramld 364
Cdd:PRK11147 313 SRSGKIVFEMEN--VNYQIDGKQL---------VKDFSAQVQRGDKIALIGPNGCGKTT----LLKL------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 365 ghdLLGASRRELRRLR--QDIQIVFQDPF-ASLDPRMRVGDILEEGiaslRPELAASARRARAVGLLERVGLP---ADTP 438
Cdd:PRK11147 365 ---MLGQLQADSGRIHcgTKLEVAYFDQHrAELDPEKTVMDNLAEG----KQEVMVNGRPRHVLGYLQDFLFHpkrAMTP 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 439 TRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVsvqaQILDLLRDLQAE 493
Cdd:PRK11147 438 VK---ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDS 485
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-240 |
3.75e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLRL-LPDAGrivggQIELGGTDLNDLSERAMRgvrggRIGIIFQepATS 105
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAG-----SISLCGEPVPSRARHARQ-----RVGVVPQ--FDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVGDQIVeTLAAHTPLRGAAARERAIDWLRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:PRK13537 91 LDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 186 TALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGG-EIVESA 240
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGA 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-237 |
4.68e-11 |
|
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: 62.67 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIvGGQIELGGTDLN-DLSERamrgvrggRIGIIFQEpatslnp 108
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTT-SGQILFNGQPRKpDQFQK--------CVAYVRQD------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 109 vmrvgDQIVETL--------AAHTPLR----GAAARERAIDW-LRRVGIpepeRRIDDYPFQ-FSGGQKQRLMIAIALAA 174
Cdd:cd03234 90 -----DILLPGLtvretltyTAILRLPrkssDAIRKKRVEDVlLRDLAL----TRIGGNLVKgISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITH----DLAvvrNVAHHVALMRGGEIV 237
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHqprsDLF---RLFDRILLLSSGEIV 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
159-525 |
5.08e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALdvtVQAQVLELLAGIQ--REMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:PRK10982 136 SVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQW 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 237 VESADAR--TFFERPRHPYARELFEAIPTfaKRGRPlsaqgraadqgkaapeaGAVVLDVQDLlvhypvrkgvlrrVAAW 314
Cdd:PRK10982 213 IATQPLAglTMDKIIAMMVGRSLTQRFPD--KENKP-----------------GEVILEVRNL-------------TSLR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLLGASRRElrrlrqdiqiVFQDPFASL 394
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE--KSAGTITLHGKKINNHNANE----------AINHGFALV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDI---LEEGIASLrpeLAASARRARAVGLLERVGLPAD-----------TPTRYPH--EFSGGQRQRIAIARA 458
Cdd:PRK10982 329 TEERRSTGIyayLDIGFNSL---ISNIRNYKNKVGLLDNSRMKSDtqwvidsmrvkTPGHRTQigSLSGGNQQKVIIGRW 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 459 LAVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHGGR---IVE 525
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVD 474
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
318-524 |
5.24e-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: 62.28 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKAL-LRLVEGARVQGRAMLDGHDLLGASRRELRrlrqdiQIVFQDPFASLDP 396
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSVEGDIHYNGIPYKEFAEKYPG------EIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEegiASLRpelaasarraravgllervgLPADtptRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:cd03233 97 TLTVRETLD---FALR--------------------CKGN---EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490704625 477 VSVQAQILDLLRDLQAELGIAYLFITHNFGVVEY-LADRIAVMHGGRIV 524
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGRQI 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
315-524 |
5.36e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRlvEGARVQGRAMLDGHDLlgASRRELRRLRQDIQIVFQDpfASL 394
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDI--TDWQTAKIMREAVAIVPEG--RRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEG-IASLRPELAASARRARAV--GLLERVGLPADTptrypheFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK11614 92 FSRMTVEENLAMGgFFAERDQFQERIKWVYELfpRLHERRIQRAGT-------MSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 472 TSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIV 524
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
446-536 |
5.45e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRIVE 525
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
90
....*....|.
gi 490704625 526 MGPADTVLHAP 536
Cdd:PRK10575 229 QGTPAELMRGE 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-252 |
5.65e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 37 GETFALVGESGSGKS--MTALALLRLlpdAGRIVGGQIELGGTDLNDLSERAMRG-VRGGRIGI---------IFQ---- 100
Cdd:TIGR00955 51 GELLAVMGSSGAGKTtlMNALAFRSP---KGVKGSGSVLLNGMPIDAKEMRAISAyVQQDDLFIptltvrehlMFQahlr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 --EPATSLNPVMRVgDQIVETL----AAHTplrgaaareraidwlrRVGIPEPERRIddypfqfSGGQKQRLMIAIALAA 174
Cdd:TIGR00955 128 mpRRVTKKEKRERV-DEVLQALglrkCANT----------------RIGVPGRVKGL-------SGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGI-QRemGMAVLLITHD-LAVVRNVAHHVALMRGGEIV------ESADartFF 246
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQpSSELFELFDKIILMAEGRVAylgspdQAVP---FF 258
|
....*.
gi 490704625 247 ERPRHP 252
Cdd:TIGR00955 259 SDLGHP 264
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-236 |
6.97e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 64.68 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 8 LRIEGLDVDVAGESGVThaVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAM 87
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKS----TLARLIVGIWPPTSGSVRLDGADLKQWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 88 rgvrGGRIGIIFQE----PATSLNPVMRVGD-----QIVEtlAAhtplRGAAARERAIdwlrrvGIPEP-ERRIDDYPFQ 157
Cdd:TIGR01842 391 ----GKHIGYLPQDvelfPGTVAENIARFGEnadpeKIIE--AA----KLAGVHELIL------RLPDGyDTVIGPGGAT 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 158 FSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVrNVAHHVALMRGGEI 236
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGRI 531
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-237 |
7.02e-11 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 64.89 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 24 THAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPa 103
Cdd:TIGR03375 478 TPALDNVSLTIRPGEKVAIIGRIGSGKS----TLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR----NIGYVPQDP- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 104 TSLNPVMRvgdqivETLAahtpLRGAAARERAI-DWLRRVGIPE-----P---ERRIDDYPFQFSGGQKQRLMIAIALAA 174
Cdd:TIGR03375 549 RLFYGTLR------DNIA----LGAPYADDEEIlRAAELAGVTEfvrrhPdglDMQIGERGRSLSGGQRQAVALARALLR 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQRemGMAVLLITHDLAVVrNVAHHVALMRGGEIV 237
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-230 |
7.18e-11 |
|
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: 61.74 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 15 VDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggr 94
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 95 igIIFQEPATSLNPVMRVgdqiVETLAAHTPLRGAAARERAIDwlrRVGIpepeRRIDDYPF-QFSGGQKQRLMIAIALA 173
Cdd:cd03231 75 --LLYLGHAPGIKTTLSV----LENLRFWHADHSDEQVEEALA---RVGL----NGFEDRPVaQLSAGQQRRVALARLLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 174 AEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVAL 230
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
154-216 |
1.16e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 60.25 E-value: 1.16e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 154 YPFQ--FSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLagiqREMGMAVLLITH 216
Cdd:cd03223 86 YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
321-519 |
1.19e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTTGKALLRLV--------------------------------------------EGAR 356
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkEGGS 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 357 VQ--------GRAMLDGHDLLGASRRELRRLrqdIQIVFQDPF---ASLDPRMRVGDilEEgiaSLRPELAASARRARAV 425
Cdd:PTZ00265 1267 GEdstvfknsGKILLDGVDICDYNLKDLRNL---FSIVSQEPMlfnMSIYENIKFGK--ED---ATREDVKRACKFAAID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 426 GLLERVGLPADTPT-RYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHN 504
Cdd:PTZ00265 1339 EFIESLPNKYDTNVgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1418
|
250
....*....|....*
gi 490704625 505 FGVVEYlADRIAVMH 519
Cdd:PTZ00265 1419 IASIKR-SDKIVVFN 1432
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
41-239 |
1.51e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 61.64 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 41 ALVGESGSGKSmTALALL-RLLP-DAGRI-VGGQiELGGTDLNDLSERamrgvrggrIGIIFQEPATslnpVMRVgdqIV 117
Cdd:COG4604 31 ALIGPNGAGKS-TLLSMIsRLLPpDSGEVlVDGL-DVATTPSRELAKR---------LAILRQENHI----NSRL---TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 118 ETLAA-----HTplRGA------AARERAIDWLRRVGIPEpeRRIDdypfQFSGGQKQRLMIAIALAAEPKLLIADEPTT 186
Cdd:COG4604 93 RELVAfgrfpYS--KGRltaedrEIIDEAIAYLDLEDLAD--RYLD----ELSGGQRQRAFIAMVLAQDTDYVLLDEPLN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 187 ALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIVES 239
Cdd:COG4604 165 NLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
317-518 |
1.70e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 60.33 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKAL---LRLVEGARVQGRAmldghdllgasrrelRRLRQDIQIVfqdpfaS 393
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagvLRPTSGTVRRAGG---------------ARVAYVPQRS------E 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRM--RVGDILEEGIASLRPELAASARRARAV--GLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICD 469
Cdd:NF040873 66 VPDSLplTVRDLVAMGRWARRGLWRRLTRDDRAAvdDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490704625 470 EPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEyLADRIAVM 518
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-216 |
1.74e-10 |
|
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: 60.45 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 15 VDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggr 94
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 95 igIIFQEPATSLNPVMRVgdqiVETLAAHTPLRGAAARErAIDWLRRVGIpepeRRIDDYPF-QFSGGQKQRLMIAIALA 173
Cdd:TIGR01189 75 --ILYLGHLPGLKPELSA----LENLHFWAAIHGGAQRT-IEDALAAVGL----TGFEDLPAaQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490704625 174 AEPKLLIADEPTTALDVTVQAQVLELLAG-IQRemGMAVLLITH 216
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAhLAR--GGIVLLTTH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-235 |
2.07e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSmtalALLRL---LPDAGRivgGQIEL-GGTDLNDLSERamrgvrggrigiifqep 102
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKS----TLLRAiagLWPYGS---GRIARpAGARVLFLPQR----------------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 103 atslnPVMRVGdqiveTLAA-----HTPlrGAAARERAIDWLRRVGIPEPERRID---DYPFQFSGGQKQRLMIAIALAA 174
Cdd:COG4178 435 -----PYLPLG-----TLREallypATA--EAFSDAELREALEAVGLGHLAERLDeeaDWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLagIQREMGMAVLLITHDLAVVRNVAHHVALMRGGE 235
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDGS 561
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
321-530 |
2.25e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 321 VTFTLRAGETLALLGESGCGKTTTGKALLRLVEGArvQGRAMLDGhdlLGASRRELRRLRQDIQIVFQDPF-------AS 393
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA--EGEIIIDG---LNIAKIGLHDLRFKITIIPQDPVlfsgslrMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 394 LDPRMRVGDilEEGIASLRpelaasarraravgLLERVGLPADTPTRYPHE-------FSGGQRQRIAIARALAVEPKVL 466
Cdd:TIGR00957 1380 LDPFSQYSD--EEVWWALE--------------LAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 467 ICDEPTSALDVS----VQAQILDLLRDLQAeLGIAYLFIThnfgVVEYlaDRIAVMHGGRIVEMG-PAD 530
Cdd:TIGR00957 1444 VLDEATAAVDLEtdnlIQSTIRTQFEDCTV-LTIAHRLNT----IMDY--TRVIVLDKGEVAEFGaPSN 1505
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-476 |
4.00e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 31 QLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLS-ERAMRgvrggRIGIIFQEPATSLnpv 109
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP----LLSGERQSQFSHITRLSfEQLQK-----LVSDEWQRNNTDM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVGDQIVETLAAHTPLRGAAARERAIDWLRRVGIpepeRRIDDYPF-QFSGGQKQRLMIAIALAAEPKLLIADEPTTAL 188
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGI----TALLDRRFkYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 189 DVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADartfferprhpyaRELFEAIPTFAKrg 268
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE-------------REEILQQALVAQ-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 269 rpLSAQGRAADQGKAAPEAGAVVLDVQDLLVHYPVRKGVL----RRVaawveaVNGVTFTLRAGETLALLGESGCGKTTt 344
Cdd:PRK10938 231 --LAHSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVsyndRPI------LHNLSWQVNPGEHWQIVGPNGAGKST- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 345 gkaLLRLVEGARVQGRAmldgHDLLGASRRE-----LRRLRQDIQIVfqdpFASLDPRMRVGDILEEGIASlrpelaasa 419
Cdd:PRK10938 302 ---LLSLITGDHPQGYS----NDLTLFGRRRgsgetIWDIKKHIGYV----SSSLHLDYRVSTSVRNVILS--------- 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 420 RRARAVGL---------------LERVGLPADTPTRYPHEFSGGQrQRIA-IARALAVEPKVLICDEPTSALD 476
Cdd:PRK10938 362 GFFDSIGIyqavsdrqqklaqqwLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
315-530 |
4.13e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.67 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgKALLRLVEGARVQGRAMLdgHDLLGASRRELRR---LRQDIQIVFQDPF 391
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**R--GALPAHV*GPDAGRRPWR--F*TWCANRRALRRtig*HRPVR*GRRESF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 ASLDPRMRVGDILEegiaslrpeLAASARRARAVGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:NF000106 102 SGRENLYMIGR*LD---------LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 472 TSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPAD 530
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-216 |
4.94e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 17 VAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAGRIVGGQIElGGTDLNDLSeramrgvrggrig 96
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL--AGALKGTPVA-GCVDVPDNQ------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 97 iiFQEPATSLNPVMRVGD--QIVETLAAhtplrgaAARERAIDWLRRVGipeperriddypfQFSGGQKQRLMIAIALAA 174
Cdd:COG2401 96 --FGREASLIDAIGRKGDfkDAVELLNA-------VGLSDAVLWLRRFK-------------ELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490704625 175 EPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITH 216
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
318-490 |
9.51e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEGARVQGRAMLDGHDLlgaSRRELRRlrqdIQIVFQDPFasLDPR 397
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKP---TKQILKR----TGFVTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDILEE-GIASLRPELAASARRARAVGLLERVGLPADTPTRYPHEF----SGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PLN03211 155 LTVRETLVFcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPT 234
|
170
....*....|....*...
gi 490704625 473 SALDVSVQAQILDLLRDL 490
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL 252
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
292-480 |
1.28e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 59.15 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYPVR-KGVLRRVAAWVeavngvtftlRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLlg 370
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYI----------KPGQKVGICGRTGSGKSSLSLAFFRMVD--IFDGKIVIDGIDI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 371 aSRRELRRLRQDIQIVFQDPFA-------SLDPRMRVGD-----ILEegIASLRPELAASARraravgllervGLPAdTP 438
Cdd:cd03288 86 -SKLPLHTLRSRLSIILQDPILfsgsirfNLDPECKCTDdrlweALE--IAQLKNMVKSLPG-----------GLDA-VV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490704625 439 TRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQ 480
Cdd:cd03288 151 TEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
317-523 |
1.39e-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: 61.18 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVegARVQGRAMLDGHDL---LGASRRELRRLRQDiQIVFQDP--- 390
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL--PPTSGTVLVGGKDIetnLDAVRQSLGMCPQH-NILFHHLtva 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 391 -----FASLDPRMRvgdilEEgiASLRPElaasarraravGLLERVGLpADTPTRYPHEFSGGQRQRIAIARALAVEPKV 465
Cdd:TIGR01257 1022 ehilfYAQLKGRSW-----EE--AQLEME-----------AMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 466 LICDEPTSALDVSVQAQILDLLrdLQAELGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
1.45e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 1 MTASAPLLRIEGLDVDVagesGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALlrllpdAG----RIVGGQIELGG 76
Cdd:CHL00131 1 MNKNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI------AGhpayKILEGDILFKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 77 TDLNDLS--ERAMRGvrggrIGIIFQEPAT----SLNPVMRVG---DQIVETLAAHTPLrgaAARERAIDWLRRVGIPEP 147
Cdd:CHL00131 71 ESILDLEpeERAHLG-----IFLAFQYPIEipgvSNADFLRLAynsKRKFQGLPELDPL---EFLEIINEKLKLVGMDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 148 --ERRIDDypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLEllaGIQREMGM--AVLLITH-----DL 218
Cdd:CHL00131 143 flSRNVNE---GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAE---GINKLMTSenSIILITHyqrllDY 216
|
250 260
....*....|....*....|....
gi 490704625 219 AVVRNVahHValMRGGEIVESADA 242
Cdd:CHL00131 217 IKPDYV--HV--MQNGKIIKTGDA 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
428-524 |
2.01e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 428 LERVGLPADTPTRyphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelgiAYLFITHNFGV 507
Cdd:PRK11147 143 LAQLGLDPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSF 215
|
90
....*....|....*..
gi 490704625 508 VEYLADRIAVMHGGRIV 524
Cdd:PRK11147 216 IRNMATRIVDLDRGKLV 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-241 |
2.46e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 7 LLRIEGLDVDVAGESgvthAVKRLQLAVAQGETFALVGESGSGKSMTALALlrllpdAGR----IVGGQIELGGTDLNDL 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL------AGRedyeVTGGTVEFKGKDLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 83 S--ERAMRGvrggrIGIIFQEPA------------TSLNPVMRVGDQivetlaahTPLRGAAARERAIDWLRRVGIPEP- 147
Cdd:PRK09580 71 SpeDRAGEG-----IFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--------EPLDRFDFQDLMEEKIALLKMPEDl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 148 -ERRIDdypFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVA- 225
Cdd:PRK09580 138 lTRSVN---VGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKp 213
|
250
....*....|....*.
gi 490704625 226 HHVALMRGGEIVESAD 241
Cdd:PRK09580 214 DYVHVLYQGRIVKSGD 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-216 |
3.28e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.87 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 14 DVDVAGES-----GVTHAVKRLQLAvaqgetfALVGESGSGKSmtalALLRLLpdAGR----IVGGQIELGGTDLNDLSE 84
Cdd:cd03232 12 TVPVKGGKrqllnNISGYVKPGTLT-------ALMGESGAGKT----TLLDVL--AGRktagVITGEILINGRPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 85 RamrgvrggRIGIIFQEPAtsLNPVMRVgdqiVETLAAHTPLRGaaareraidwlrrvgipeperriddypfqFSGGQKQ 164
Cdd:cd03232 79 R--------STGYVEQQDV--HSPNLTV----REALRFSALLRG-----------------------------LSVEQRK 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490704625 165 RLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITH 216
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-216 |
3.55e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSmtalALLRLLpdAG--RIVGGQIELGGTDLNDLSERAMrgvrggrigIIFQEPATS 105
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKT----TLLRLI--AGllPPAAGTIKLDGGDIDDPDVAEA---------CHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPVMRVgdqiVETLAAHTPLRGAAaRERAIDWLRRVGIPeperRIDDYPFQF-SGGQKQRLMIAIALAAEPKLLIADEP 184
Cdd:PRK13539 84 MKPALTV----AENLEFWAAFLGGE-ELDIAAALEAVGLA----PLAHLPFGYlSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 490704625 185 TTALDVTVQAQVLELLAGiQREMGMAVLLITH 216
Cdd:PRK13539 155 TAALDAAAVALFAELIRA-HLAQGGIVIAATH 185
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-268 |
4.03e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 22 GVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRivgGQIELGGTDLNDLSERAM----RGVRGGRigi 97
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR---RPWRF*TWCANRRALRRTig*hRPVR*GR--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 98 ifQEPATSLNPVMRVGDQIvetlaahtPLRGAAARERAIDWLRRVGIPEPERRIddyPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:NF000106 98 --RESFSGRENLYMIGR*L--------DLSRKDARARADELLERFSLTEAAGRA---AAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESAD---------ARTFFER 248
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKvdelktkvgGRTLQIR 243
|
250 260
....*....|....*....|
gi 490704625 249 PRHpyARELFEAIPTFAKRG 268
Cdd:NF000106 244 PAH--AAELDRMVGAIAQAG 261
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-237 |
1.45e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGRIVGGQIElGGTDLNDLSERAMRGVRGGRIGIIFQEPATSLNPV 109
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVT-GDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MrvGDQIVeTLAAHTPLRGAAA---RERAIDW--LRRVGIPEPERRidDYPfQFSGGQKQRLMIAIALA---------AE 175
Cdd:PRK13547 99 S--AREIV-LLGRYPHARRAGAlthRDGEIAWqaLALAGATALVGR--DVT-TLSGGELARVQFARVLAqlwpphdaaQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 176 PKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV 237
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-243 |
1.73e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSMTALALLrllpDAGRIVGGQIELGGTDLNDLSEraMRGVRGGrIGIIFQE----- 101
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLF----GVDKRAGGEIRLNGKDISPRSP--LDAVKKG-MAYITESrrdng 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 102 --PATSLNPVMRVGDQIVET-------LAAHTPLRGAAARERAIDWLRRVGIpepERRIDdypfQFSGGQKQRLMIAIAL 172
Cdd:PRK09700 352 ffPNFSIAQNMAISRSLKDGgykgamgLFHEVDEQRTAENQRELLALKCHSV---NQNIT----ELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 173 AAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGEIVESADAR 243
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
445-521 |
1.86e-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: 55.03 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSV-----QAQILDLLRDLQAELgiayLFITHNfgvVEYL--ADRIAV 517
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHK---LQYLphADWIIA 213
|
....
gi 490704625 518 MHGG 521
Cdd:cd03290 214 MKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
40-222 |
2.28e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 40 FALVGESGSGKSMTalallrLLPDAGRIVggqieLGGTDLNDLSERAMRGVrggrIGIIFQEPA---TSLNPVMRVG--D 114
Cdd:PTZ00265 1258 FSLTKEGGSGEDST------VFKNSGKIL-----LDGVDICDYNLKDLRNL----FSIVSQEPMlfnMSIYENIKFGkeD 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 115 QIVETLAAhtplrgaAARERAIDWLRRVGIPEPERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQA 194
Cdd:PTZ00265 1323 ATREDVKR-------ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
170 180
....*....|....*....|....*...
gi 490704625 195 QVLELLAGIQREMGMAVLLITHDLAVVR 222
Cdd:PTZ00265 1396 LIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-515 |
3.29e-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: 54.04 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLlGASRRELRRlrqdiQIVFQDPFASLDPR 397
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTT----LLRILAGlsPPLAGRVLLNGGPL-DFQRDSIAR-----GLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVgdilEEGIASLRPELAASARRARavglLERVGLPA--DTPTrypHEFSGGQRQRIAIARALAVEPKVLICDEPTSAL 475
Cdd:cd03231 88 LSV----LENLRFWHADHSDEQVEEA----LARVGLNGfeDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490704625 476 DVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRI 515
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
444-520 |
3.53e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 3.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 444 EFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYLADRIAVMHG 520
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
235-272 |
4.60e-08 |
|
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: 50.82 E-value: 4.60e-08
10 20 30
....*....|....*....|....*....|....*...
gi 490704625 235 EIVESADARTFFERPRHPYARELFEAIPTFAKRGRPLS 272
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLI 38
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
429-520 |
4.61e-08 |
|
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: 52.96 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 429 ERVGLPADTPTRYPH--EFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFG 506
Cdd:cd03222 54 DNDEWDGITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLA 133
|
90
....*....|....
gi 490704625 507 VVEYLADRIAVMHG 520
Cdd:cd03222 134 VLDYLSDRIHVFEG 147
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-220 |
4.91e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.27 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 29 RLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDLSERAMRGVR--GGRIGIifqepATSL 106
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKT----SLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylGHQPGI-----KTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 NPVmrvgdqivETLAAHTPLRGAAARERAIDWLRRVGIpepeRRIDDYPF-QFSGGQKQRlmiaIALA----AEPKLLIA 181
Cdd:PRK13538 90 TAL--------ENLRFYQRLHGPGDDEALWEALAQVGL----AGFEDVPVrQLSAGQQRR----VALArlwlTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 490704625 182 DEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAV 220
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
323-533 |
5.37e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 323 FTLRAGETLALLGESGCGKTTTGKAL---LRLVEGARVqgramldgHDLLGASRRELRRLRQDIQIVFQDPFASL----- 394
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALageLPLLSGERQ--------SQFSHITRLSFEQLQKLVSDEWQRNNTDMlspge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 -DPRMRVGDILEEGIASlrPELAASARRARAVG-LLERvglpadtPTRYpheFSGGQRQRIAIARALAVEPKVLICDEPT 472
Cdd:PRK10938 96 dDTGRTTAEIIQDEVKD--PARCEQLAQQFGITaLLDR-------RFKY---LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490704625 473 SALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPADTVL 533
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
313-527 |
7.09e-08 |
|
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: 52.33 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 313 AWVEAVNGVTFTLRAGETLALLGESGCGKTTTgkallrLVEGARVQGRamldghdllgasrrelRRLRQDIQIVFQDPFA 392
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL------VNEGLYASGK----------------ARLISFLPKFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLDprmRVGDILEEGIASLRPelaasarraravgllervGLPADTptrypheFSGGQRQRIAIARALAVEPK--VLICDE 470
Cdd:cd03238 64 FID---QLQFLIDVGLGYLTL------------------GQKLST-------LSGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 471 PTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEYlADRIAVM------HGGRIVEMG 527
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
318-544 |
9.24e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVE---GA-RVQGRAmldghdlLGASrrELRRLRQDIQIVFQDPF-- 391
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEvcgGEiRVNGRE-------IGAY--GLRELRRQFSMIPQDPVlf 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 392 -----ASLDPRMRVGDilEEGIASLrpELaasarraraVGLLERVGLPADTPTRYPHE----FSGGQRQRIAIARALAVE 462
Cdd:PTZ00243 1397 dgtvrQNVDPFLEASS--AEVWAAL--EL---------VGLRERVASESEGIDSRVLEggsnYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 463 PKVLIC-DEPTS----ALDVSVQAQILDLLRdlqaelgiAYLFIT--HNF-GVVEYlaDRIAVMHGGRIVEMG-PADTVL 533
Cdd:PTZ00243 1464 GSGFILmDEATAnidpALDRQIQATVMSAFS--------AYTVITiaHRLhTVAQY--DKIIVMDHGAVAEMGsPRELVM 1533
|
250
....*....|...
gi 490704625 534 HAPR--HEMTQRL 544
Cdd:PTZ00243 1534 NRQSifHSMVEAL 1546
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
316-477 |
1.07e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 316 EAVNGVTFTLRAGETLALLGESGCGKTTTGKAL-LRLVEG-----------ARVQGRAMLDGHDLLGASRRELRRLRQDI 383
Cdd:PLN03073 191 DLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMaMHAIDGipkncqilhveQEVVGDDTTALQCVLNTDIERTQLLEEEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 384 QIVFQD-----PFASLDPRMRVGDILEEGIASLRPE--------LAASARRARAVGLLERVGLPADTPTRYPHEFSGGQR 450
Cdd:PLN03073 271 QLVAQQrelefETETGKGKGANKDGVDKDAVSQRLEeiykrlelIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWR 350
|
170 180
....*....|....*....|....*..
gi 490704625 451 QRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:PLN03073 351 MRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-236 |
1.29e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAGrivgGQIELGGTDLndlsERAMRGVRGGrIGIIFQepats 105
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS----GTVLVGGKDI----ETNLDAVRQS-LGMCPQ----- 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 lNPVMRVGDQIVETLAAHTPLRGAAARERAIDW---LRRVGIpepERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIAD 182
Cdd:TIGR01257 1011 -HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMeamLEDTGL---HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490704625 183 EPTTALDVTVQAQVLELLagIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEI 236
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
324-520 |
1.47e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.80 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 324 TLRAGETLALLGESGCGKTTTGKALlrlvegarvQGRAMLDGHDLlGASRRELRRLRQDIQIVFQdpfasldprMRVGDI 403
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML---------AGVLKPDEGDI-EIELDTVSYKPQYIKADYE---------GTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 404 LEEGIASL------RPELAASARRAravGLLERVgLPadtptryphEFSGGQRQRIAIARALAVEPKVLICDEPTSALDV 477
Cdd:cd03237 82 LSSITKDFythpyfKTEIAKPLQIE---QILDRE-VP---------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490704625 478 SVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAVMHG 520
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
17-253 |
1.79e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 17 VAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGGTDLNDL-SERAMRG----VR 91
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREavaiVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 92 GGRIgiIFQEPATSLNPVMrvgdqivetlaahtplrGA--AARERAIDWLRRVGIPEP---ERRIDDYPfQFSGGQKQRL 166
Cdd:PRK11614 87 EGRR--VFSRMTVEENLAM-----------------GGffAERDQFQERIKWVYELFPrlhERRIQRAG-TMSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 167 MIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV--ESADART 244
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDALL 225
|
....*....
gi 490704625 245 FFERPRHPY 253
Cdd:PRK11614 226 ANEAVRSAY 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-222 |
2.30e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 28 KRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDAGRivGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPAT--- 104
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPTE--GDIIINDSHNLKDINLKWWRS----KIGVVSQDPLLfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 105 -----------SLNPVMRVGDQIVETLAAHTPLRGAAARERA---------------------------------IDWLR 140
Cdd:PTZ00265 475 siknnikyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAkcagdlndmsnttdsneliemrknyqtikdsevVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 141 RV-------GIPEP-ERRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVL 212
Cdd:PTZ00265 555 KVlihdfvsALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250
....*....|
gi 490704625 213 LITHDLAVVR 222
Cdd:PTZ00265 635 IIAHRLSTIR 644
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-247 |
2.84e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 37 GETFALVGESGSGKSMTALALlrllpdAGRIVGGQieLGGTDL-ND--LSERAMRgvrggRIGIIFQEPAtsLNPVMRVG 113
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL------AGRIQGNN--FTGTILaNNrkPTKQILK-----RTGFVTQDDI--LYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 114 DQIV--------ETLAAHTPLRGAaarERAIDWLrrvGIPEPERRIDDYPF--QFSGGQKQRLMIAIALAAEPKLLIADE 183
Cdd:PLN03211 159 ETLVfcsllrlpKSLTKQEKILVA---ESVISEL---GLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 184 PTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRGGEIV---ESADARTFFE 247
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLffgKGSDAMAYFE 299
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
328-530 |
3.08e-07 |
|
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: 50.06 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 328 GETLALLGESGCGKTTTGKALLRLVEgarvqgramldghdllgasrrelrrlRQDIQIVFQDPfasldprmrvGDILEEG 407
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELG--------------------------PPGGGVIYIDG----------EDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 408 IASLRPELAasarraravgllervglpadtpTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLL 487
Cdd:smart00382 46 LDQLLLIIV----------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490704625 488 RD-----LQAELGIAYLFITHNFGVveyLADRIAVMHGGRIVEMGPAD 530
Cdd:smart00382 104 ELrllllLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIVLLLIL 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
325-533 |
3.35e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 325 LRAGETLALLGESGCGKTTTGKALLRLVEGAR--VQGRAMLDGHDLlgasrREL-RRLRQDIqiVFQdpfASLD---PRM 398
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigVEGVITYDGITP-----EEIkKHYRGDV--VYN---AETDvhfPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 399 RVGDILEEGIA----SLRPELAASARRARAVG--LLERVGLPADTPTRYPHEF----SGGQRQRIAIARALAVEPKVLIC 468
Cdd:TIGR00956 154 TVGETLDFAARcktpQNRPDGVSREEYAKHIAdvYMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 469 DEPTSALDVSVQAQILDLLRDLQAELGIAYLFITHNFGVVEY-LADRIAVMHGGRIVEMGPADTVL 533
Cdd:TIGR00956 234 DNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQIYFGPADKAK 299
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
446-527 |
3.57e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDllRDLQAEL-GIAYLFITHNFGVVEYLaDRIAVMHGGRIV 524
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
...
gi 490704625 525 EMG 527
Cdd:PLN03130 819 EEG 821
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
237-283 |
4.85e-07 |
|
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: 47.01 E-value: 4.85e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490704625 237 VESADARTFFERPRHPYARELFEAIPTFAKRGRPL-SAQGRAADQGKA 283
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLyTIPGNVPSLLEL 48
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
133-516 |
5.03e-07 |
|
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: 52.63 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 133 ERAIDWLRrvgIPEPERRIDDypfqFSGGQKQRLMIAIALAAEPKLLIADEPTTALDvtvqAQVLELLAGIQREMGMAVL 212
Cdd:TIGR03719 144 EIAMDALR---CPPWDADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 213 LITHDLAVVRNVAHHVA-LMRGGEI---------VESADARTFFE-----RPRHPYARELfEAIPTFAKrGRPLSAQGR- 276
Cdd:TIGR03719 213 AVTHDRYFLDNVAGWILeLDRGRGIpwegnysswLEQKQKRLEQEekeesARQKTLKREL-EWVRQSPK-GRQAKSKARl 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 277 --------AADQGKA---------APEAGAVVLDVQDllvhypVRKGVLRRVaawveAVNGVTFTLRAGETLALLGESGC 339
Cdd:TIGR03719 291 aryeellsQEFQKRNetaeiyippGPRLGDKVIEAEN------LTKAFGDKL-----LIDDLSFKLPPGGIVGVIGPNGA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 340 GKTTtgkaLLRLvegarVQGRAMLDGHDLlgasrrelrRLRQDIQIVFQDPF-ASLDPRMRVGDILEEGIASLRpelaas 418
Cdd:TIGR03719 360 GKST----LFRM-----ITGQEQPDSGTI---------EIGETVKLAYVDQSrDALDPNKTVWEEISGGLDIIK------ 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 419 arraraVGllervglPADTPTR-YPHEF--------------SGGQRQRIAIARALAVEPKVLICDEPTSALDVsvqaqi 483
Cdd:TIGR03719 416 ------LG-------KREIPSRaYVGRFnfkgsdqqkkvgqlSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV------ 476
|
410 420 430
....*....|....*....|....*....|....*..
gi 490704625 484 lDLLRDLQAEL----GIAyLFITHNfgvvEYLADRIA 516
Cdd:TIGR03719 477 -ETLRALEEALlnfaGCA-VVISHD----RWFLDRIA 507
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-193 |
5.60e-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: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSMTALALLRLLPdagriVGGQIELGGTDLNDLSERAMR---GVRGGRIGIIFQEPATSL 106
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-----TEGEIQIDGVSWNSVTLQTWRkafGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 107 NPVMRVGDQIVETLAAHTPLRGAAarERAIDWLRRVgipeperrIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTT 186
Cdd:TIGR01271 1313 DPYEQWSDEEIWKVAEEVGLKSVI--EQFPDKLDFV--------LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
....*...
gi 490704625 187 ALD-VTVQ 193
Cdd:TIGR01271 1383 HLDpVTLQ 1390
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
41-238 |
5.72e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.41 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 41 ALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLSERAMRgvRGgrIGIIFQEPATslnpvmrvgdqIVETL 120
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVLR--QG--VAMVQQDPVV-----------LADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 121 AAHTPLRGAAARERAIDWLRRVGIPEPER--------RIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTV 192
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARslpdglytPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490704625 193 QAQVLELLAGIQREMGMAVllITHDLAVVRNVAHHVALMRgGEIVE 238
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVV--IAHRLSTIVEADTILVLHR-GQAVE 554
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
317-534 |
6.74e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTTGKALL---RLVEG-ARVQGRAML----DGHDLLGASRR-----ELRRLRQDI 383
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTgdtTVTSGdATVAGKSILtnisDVHQNMGYCPQfdaidDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 384 QIvfqdpFASLD--PRMRVGDILEEGIASLrpelaasarraravGLlervGLPADtptRYPHEFSGGQRQRIAIARALAV 461
Cdd:TIGR01257 2034 YL-----YARLRgvPAEEIEKVANWSIQSL--------------GL----SLYAD---RLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490704625 462 EPKVLICDEPTSALDVSVQAQILDLLRDLQAElGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGpadTVLH 534
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG---TIQH 2156
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-220 |
8.10e-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: 50.44 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 34 VAQGETFALVGESGSGKSmTALALL--RLLPDAGRIVGGQ------IELGGTDLNDLSERamrgVRGGRIGIIFQEPATS 105
Cdd:cd03236 23 PREGQVLGLVGPNGIGKS-TALKILagKLKPNLGKFDDPPdwdeilDEFRGSELQNYFTK----LLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 LNPvmRVGDQIVETLAAHTPLRGAaaRERAIDWLRRVGIPEpeRRIDdypfQFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:cd03236 98 LIP--KAVKGKVGELLKKKDERGK--LDELVDQLELRHVLD--RNID----QLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|....*
gi 490704625 186 TALDVTVQAQVLELLAGIQREmGMAVLLITHDLAV 220
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAV 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
159-235 |
1.05e-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: 49.39 E-value: 1.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLagIQREM--GMAVLLITHDLAVVRNvAHHVALMRGGE 235
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLlnNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
286-528 |
1.11e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 286 EAGAVVLDVQDLLVHYPVRKGVLRrvaawveAVNGVTFTLRAGETLALLGESGCGKTTTGKALL-RLVEGARVQGRAMLD 364
Cdd:TIGR00956 754 ESGEDIFHWRNLTYEVKIKKEKRV-------ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVTTGVITGGDRLVN 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 365 GHDL-----------------LGAS--RRELR---RLRQDIQIvfqdpfaSLDPRMR----VGDILEegIASLRPELaas 418
Cdd:TIGR00956 827 GRPLdssfqrsigyvqqqdlhLPTStvRESLRfsaYLRQPKSV-------SKSEKMEyveeVIKLLE--MESYADAV--- 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 419 arraravgllerVGLPADTptrypheFSGGQRQRIAIARALAVEPKVLI-CDEPTSALDVSVQAQILDLLRDLqAELGIA 497
Cdd:TIGR00956 895 ------------VGVPGEG-------LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQA 954
|
250 260 270
....*....|....*....|....*....|...
gi 490704625 498 YLFITHNFGVVEYLA-DRIAVMH-GGRIVEMGP 528
Cdd:TIGR00956 955 ILCTIHQPSAILFEEfDRLLLLQkGGQTVYFGD 987
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
444-539 |
1.12e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 444 EFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:PRK13546 143 KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
90
....*....|....*.
gi 490704625 524 VEMGPADTVLhaPRHE 539
Cdd:PRK13546 222 KDYGELDDVL--PKYE 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
318-503 |
1.87e-06 |
|
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: 50.90 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 318 VNGVTFTLRAGETLALLGESGCGKTTTGKALLRL--VEGARV------------QGRAMldghdllgaSRRELRRlrqdi 383
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpVYGGRLtkpakgklfyvpQRPYM---------TLGTLRD----- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 384 QIVFqdPFASLDPRMR-VGDileegiaslrPELAASARRARAVGLLER-VGLpaDTPTRYPHEFSGGQRQRIAIARALAV 461
Cdd:TIGR00954 534 QIIY--PDSSEDMKRRgLSD----------KDLEQILDNVQLTHILEReGGW--SAVQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490704625 462 EPKVLICDEPTSALDVSVQAQILDLLRdlqaELGIAYLFITH 503
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-249 |
2.04e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSmTALALLRLLPDagrIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEPats 105
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKS-TLLSLIQRHFD---VSEGDIRFHDIPLTKLQLDSWRS----RLAVVSQTP--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 lnpvMRVGDQIVETLAAHTPLRGAAARERAI-------DWLRrvgIPEP-ERRIDDYPFQFSGGQKQRLMIAIALAAEPK 177
Cdd:PRK10789 399 ----FLFSDTVANNIALGRPDATQQEIEHVArlasvhdDILR---LPQGyDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490704625 178 LLIADEPTTALDVTVQAQVLELLAgiQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVESADARTFFERP 249
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
292-484 |
2.32e-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: 50.68 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 292 LDVQDLLVHYpvrkgvlrrVAAWVEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLvegARVQGRAMLDGhdlLGA 371
Cdd:TIGR01271 1218 MDVQGLTAKY---------TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL---LSTEGEIQIDG---VSW 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 372 SRRELRRLRQDIQIVFQDPF-------ASLDPRMRVGDileEGIASLRPELAASARRARAVGLLERVGLPADtptrypHE 444
Cdd:TIGR01271 1283 NSVTLQTWRKAFGVIPQKVFifsgtfrKNLDPYEQWSD---EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG------YV 1353
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDvSVQAQIL 484
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQII 1392
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
320-503 |
2.39e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.65 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGhdllgasrRELRRLRQDiqivFQDPFASLDPR 397
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTS----LLRILAGlaRPDAGEVLWQG--------EPIRRQRDE----YHQDLLYLGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 398 MRVGDIL--EEGIASLRPeLAASARRARAVGLLERVGLP--ADTPTRYpheFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK13538 83 PGIKTELtaLENLRFYQR-LHGPGDDEALWEALAQVGLAgfEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|
gi 490704625 474 ALDVSVQAQILDLLRDLQAELGIAyLFITH 503
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-222 |
4.98e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 4.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 159 SGGQKQRLMIAIALAAEPK--LLIADEPTTALDVTVQAQVLELLAGIqREMGMAVLLITHDLAVVR 222
Cdd:cd03238 89 SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLS 153
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-236 |
7.80e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 6 PLLRIEGLDVDVaGESGVTHAVKrlqLAVAQGETFALVGESGSGKSmtalALLRLLPDAGRIVGGQIELGgtdlndlser 85
Cdd:PRK10636 311 PLLKMEKVSAGY-GDRIILDSIK---LNLVPGSRIGLLGRNGAGKS----TLIKLLAGELAPVSGEIGLA---------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 86 amRGVRGGrigiifqepatslnpvmrvgdqiveTLAAHTpLRGAAARERAIDWLRRVGIPEPERRIDDY----PFQ---- 157
Cdd:PRK10636 373 --KGIKLG-------------------------YFAQHQ-LEFLRADESPLQHLARLAPQELEQKLRDYlggfGFQgdkv 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 158 ------FSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAgiqrEMGMAVLLITHDLAVVRNVAHHVALM 231
Cdd:PRK10636 425 teetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLLRSTTDDLYLV 500
|
....*
gi 490704625 232 RGGEI 236
Cdd:PRK10636 501 HDGKV 505
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-222 |
8.22e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 36 QGETFALVGESGSGKSMTALALLRLLPDAGRIVggqIELGGTDLNDLSERAMRGVrggrigiifqepatslnpvmrvgdq 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDILEEVLDQLLLI------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 116 ivetlaahtplrgaaareraidwlrrvgipeperRIDDYPFQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQ 195
Cdd:smart00382 53 ----------------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|..
gi 490704625 196 VLEL-----LAGIQREMGMAVLLITHDLAVVR 222
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
110-354 |
9.72e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRVGDqiVETLAAHtpLRGAAARERAIDWLRRVGIPEperridDYPF----QFSGGQKQRLMIAIALAAEPKLLIADEPT 185
Cdd:PRK15064 114 MKVAD--LEVKFAE--MDGYTAEARAGELLLGVGIPE------EQHYglmsEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 186 TALDV-TVQ--AQVLEllagiQREMGMavLLITHDLAVVRNVAHHVALMRGGEI-----------VESADARtffERPRH 251
Cdd:PRK15064 184 NNLDInTIRwlEDVLN-----ERNSTM--IIISHDRHFLNSVCTHMADLDYGELrvypgnydeymTAATQAR---ERLLA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 252 PYAR------EL------FEAIPTFAKRgrplsAQGRAADQGKAAPEagavvlDVQDLLVHYP-VR---KGVLRRVAAWV 315
Cdd:PRK15064 254 DNAKkkaqiaELqsfvsrFSANASKAKQ-----ATSRAKQIDKIKLE------EVKPSSRQNPfIRfeqDKKLHRNALEV 322
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490704625 316 EAV----------NGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG 354
Cdd:PRK15064 323 ENLtkgfdngplfKNLNLLLEAGERLAIIGENGVGKTT----LLRTLVG 367
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-238 |
1.08e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 9 RIEGLDVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPDAgrivGGQIELGGTDLNDLSERAMR 88
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA----EGEIIIDGLNIAKIGLHDLR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 89 gvrgGRIGIIFQEPA-------TSLNPVMRVGDQIVETLAAHTPLRG-AAARERAIDWLRRVGIPeperriddypfQFSG 160
Cdd:TIGR00957 1360 ----FKITIIPQDPVlfsgslrMNLDPFSQYSDEEVWWALELAHLKTfVSALPDKLDHECAEGGE-----------NLSV 1424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 161 GQKQRLMIAIALAAEPKLLIADEPTTALDVTVQaQVLELLAGIQREmGMAVLLITHDLAVVRNVAhHVALMRGGEIVE 238
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETD-NLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAE 1499
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
524-556 |
1.13e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 43.16 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|...
gi 490704625 524 VEMGPADTVLHAPRHEMTQRLLAAVPRLRFGAE 556
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKR 33
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
446-527 |
1.29e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLrdLQAEL-GIAYLFITHNFGVVEyLADRIAVMHGGRIV 524
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC--MKDELkGKTRVLVTNQLHFLP-LMDRIILVSEGMIK 818
|
...
gi 490704625 525 EMG 527
Cdd:PLN03232 819 EEG 821
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
315-529 |
1.30e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTTGKALLRLVEgaRVQGRAMLDGHDLLGASRRElrRLRQDIQIVFQDpfASL 394
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ--KDSGSILFQGKEIDFKSSKE--ALENGISMVHQE--LNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 395 DPRMRVGDILEEGIASLR-PELAASARRARAVGLLERVGLPADtPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTS 473
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKgMFVDQDKMYRDTKAIFDELDIDID-PRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 474 ALDVSVQAQILDLLRDLQaELGIAYLFITHNFGVVEYLADRIAVMHGGRIVEMGPA 529
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
159-225 |
1.42e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVtvqaQVLELLAGIQREMGMAVLLITHDLAVVRNVA 225
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFVDNTV 504
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
522-556 |
1.42e-05 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 43.50 E-value: 1.42e-05
10 20 30
....*....|....*....|....*....|....*
gi 490704625 522 RIVEMGPADTVLHAPRHEMTQRLLAAVPRLRFGAE 556
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDR 35
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
159-239 |
1.57e-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: 48.09 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAE---PKLLIADEPTTALDVtvqAQVLELLAGIQR--EMGMAVLLITHDLAVVRNVAHHVAL--- 230
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRlvDKGNTVVVIEHNLDVIKTADYIIDLgpe 907
|
90
....*....|.
gi 490704625 231 --MRGGEIVES 239
Cdd:TIGR00630 908 ggDGGGTVVAS 918
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
317-526 |
1.97e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.27 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 317 AVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLrqdIQIVFQD--PFA 392
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKST----LAMLLTGlyQPQSGEILLDGKPVTAEQPEDYRKL---FSAVFTDfhLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 393 SLdprmrVGDileEGIASLrPELAASarraravgLLERVGLpADTPTRYPHE-----FSGGQRQRIAIARALAVEPKVLI 467
Cdd:PRK10522 411 QL-----LGP---EGKPAN-PALVEK--------WLERLKM-AHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 468 CDEptSALDVSVQ------AQILDLLRdlqaELGIAYLFITHNFGVVEyLADRIAVMHGGRIVEM 526
Cdd:PRK10522 473 LDE--WAADQDPHfrrefyQVLLPLLQ----EMGKTIFAISHDDHYFI-HADRLLEMRNGQLSEL 530
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-254 |
2.15e-05 |
|
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: 46.44 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 14 DVDVAGESGVTHAVKRLQLAVAQGETFALVGESGSGKSMTALALLRLLPdagrIVGGQIELGGTDLNDLSERAMRgvrgG 93
Cdd:cd03288 24 DLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTLR----S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 94 RIGIIFQEPAT-------SLNPVMRVGD-QIVETLAAHTPLRGAAARERAIDWLrrvgipeperrIDDYPFQFSGGQKQR 165
Cdd:cd03288 96 RLSIILQDPILfsgsirfNLDPECKCTDdRLWEALEIAQLKNMVKSLPGGLDAV-----------VTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 166 LMIAIALAAEPKLLIADEPTTALDVTVQ--AQVLELLAGIQRemgmAVLLITHDLAVVRNvAHHVALMRGGEIVESADAR 243
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATEniLQKVVMTAFADR----TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPE 239
|
250
....*....|.
gi 490704625 244 TFFERPRHPYA 254
Cdd:cd03288 240 NLLAQEDGVFA 250
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-238 |
2.80e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 26 AVKRLQLAVAQGETFALVGESGSGKSMTAlallRLLPDAGRIVGGQIELGGTDLNDLSERAMRGvrggRIGIIFQEpats 105
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLA----MLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----LFSAVFTD---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 106 lnpvMRVGDQIVEtlaahtPLRGAAARERAIDWLRRVGIPEpERRIDDYPF---QFSGGQKQRLMIAIALAAEPKLLIAD 182
Cdd:PRK10522 406 ----FHLFDQLLG------PEGKPANPALVEKWLERLKMAH-KLELEDGRIsnlKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 183 EPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNvAHHVALMRGGEIVE 238
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-218 |
4.63e-05 |
|
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: 45.01 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 30 LQLAVAQGETFALVGESGSGKSMTALALLRLLpdagRIVGGQIELGGTDLNDLSERAMRGVRGGRIGIIFQEPATsLNPV 109
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 110 MRvgdqivETLAAHTPLR--------GAAARERAIDWLrrvgiPEPER-RIDDYPFQFSGGQKQRLMIAIALAAEPKLLI 180
Cdd:cd03290 95 VE------ENITFGSPFNkqrykavtDACSLQPDIDLL-----PFGDQtEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490704625 181 ADEPTTALDV-----TVQAQVLELLAGIQRemgmAVLLITHDL 218
Cdd:cd03290 164 LDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
158-313 |
5.59e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.09 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 158 FSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGiqrEMGM----AVLLITHDLAVVRNVaHHVALMRG 233
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG---PEGVlknkTRILVTHGISYLPQV-DVIIVMSG 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 234 GEIVESADARTFFERPrhpyarelfEAIPTFAKRGRPLSAQGRAADQGKAAPEA-GAVVLDVQD-LLVHYPVRKGVLRRV 311
Cdd:TIGR00957 837 GKISEMGSYQELLQRD---------GAFAEFLRTYAPDEQQGHLEDSWTALVSGeGKEAKLIENgMLVTDVVGKQLQRQL 907
|
..
gi 490704625 312 AA 313
Cdd:TIGR00957 908 SA 909
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
159-228 |
5.78e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 5.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490704625 159 SGGQKQRLMIAIALAA---EPKLLIADEPTTAL---DVTVQAQVLELLAgiqrEMGMAVLLITHDLAVVRnVAHHV 228
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLT----HQGHTVVIIEHNMHVVK-VADYV 881
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
37-237 |
6.33e-05 |
|
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: 44.18 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 37 GETFALVGESGSGKSmtalALLRLLpdAGRIVG-----GQIELGGTDLNDLSERAMRGvrggrigIIFQEPATSLNPVMR 111
Cdd:cd03233 33 GEMVLVLGRPGSGCS----TLLKAL--ANRTEGnvsveGDIHYNGIPYKEFAEKYPGE-------IIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 112 VGdqivETLAAhtplrgaAARERAIDWLRrvGIpeperriddypfqfSGGQKQRLMIAIALAAEPKLLIADEPTTALDvt 191
Cdd:cd03233 100 VR----ETLDF-------ALRCKGNEFVR--GI--------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490704625 192 vQAQVLELLAGIQ---REMGMAVLLITHDLAV-VRNVAHHVALMRGGEIV 237
Cdd:cd03233 151 -SSTALEILKCIRtmaDVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
159-237 |
7.12e-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: 44.53 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIAL---AAEPKLLIADEPTTALDVtvqAQVLELLAGIQR--EMGMAVLLITHDLAVVRNVAHHVAL--- 230
Cdd:cd03271 171 SGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHF---HDVKKLLEVLQRlvDKGNTVVVIEHNLDVIKCADWIIDLgpe 247
|
....*....
gi 490704625 231 --MRGGEIV 237
Cdd:cd03271 248 ggDGGGQVV 256
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
315-533 |
8.25e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 315 VEAVNGVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARV--QGRAMLDGHDLlgASRRELRRLRQDI----Q---- 384
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAGARKiqQGRVEVLGGDM--ADARHRRAVCPRIaympQglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 385 ------IVFQ--DPFASL---DPRMRVGDILEegiaslrpelaasarraravgLLERVGLpADTPTRYPHEFSGGQRQRI 453
Cdd:NF033858 88 nlyptlSVFEnlDFFGRLfgqDAAERRRRIDE---------------------LLRATGL-APFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 454 AIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAE-------LGIAYLFITHNFgvveylaDRIAVMHGGRIVEM 526
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgmsvlVATAYMEEAERF-------DWLVAMDAGRVLAT 218
|
....*..
gi 490704625 527 GPADTVL 533
Cdd:NF033858 219 GTPAELL 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
446-536 |
1.12e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQIL-DLLrdLQAELGIAYLFITHNFGVVEyLADRIAVMHGGRIV 524
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeECF--LGALAGKTRVLATHQVHVVP-RADYVVALGDGRVE 860
|
90
....*....|..
gi 490704625 525 EMGPADTVLHAP 536
Cdd:PTZ00243 861 FSGSSADFMRTS 872
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-216 |
1.55e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 34 VAQGETFALVGESGSGKSmTALALLRLLPDAGRIVGGQIELGGTDLNDLSERamrgvrggRIGIIFQEpatslnpvmrvg 113
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKT-TLLNVLAERVTTGVITGGDRLVNGRPLDSSFQR--------SIGYVQQQ------------ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 114 DQIVETLAAHTPLRGAAAreraidwLRR---VGIPEPERRID---------DYPFQFSG--------GQKQRLMIAIALA 173
Cdd:TIGR00956 845 DLHLPTSTVRESLRFSAY-------LRQpksVSKSEKMEYVEevikllemeSYADAVVGvpgeglnvEQRKRLTIGVELV 917
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490704625 174 AEPKLLI-ADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITH 216
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
132-523 |
1.57e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 132 RERAIDWLRRVGIPEP--ERRIDDypfqFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVqaqVLELLAGIQREMGm 209
Cdd:PRK10636 126 RSRAASLLHGLGFSNEqlERPVSD----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 210 AVLLITHDLAVVRNVAHHVALMRGGEIVESADARTFFERPR------------HPYAR--ELFEAIPTF-AKRGRPLSAQ 274
Cdd:PRK10636 198 TLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRatrlaqqqamyeSQQERvaHLQSYIDRFrAKATKAKQAQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 275 GRAADQGKAAPEAGAVVldvqDLLVHYPVRKG--------VLRRVAAWVE---AVNGVTFTLRAGETLALLGESGCGKTT 343
Cdd:PRK10636 278 SRIKMLERMELIAPAHV----DNPFHFSFRAPeslpnpllKMEKVSAGYGdriILDSIKLNLVPGSRIGLLGRNGAGKST 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 344 tgkaLLRLVEG--ARVQGRAMLDGHDLLGA-SRRELRRLRQDiqivfQDPF---ASLDPRmrvgdILEEgiaSLRPELAA 417
Cdd:PRK10636 354 ----LIKLLAGelAPVSGEIGLAKGIKLGYfAQHQLEFLRAD-----ESPLqhlARLAPQ-----ELEQ---KLRDYLGG 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 418 sarraravgllerVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILDLLRDLQAelgiA 497
Cdd:PRK10636 417 -------------FGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----A 479
|
410 420
....*....|....*....|....*.
gi 490704625 498 YLFITHNFGVVEYLADRIAVMHGGRI 523
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
425-527 |
2.30e-04 |
|
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: 42.63 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 425 VGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVE-PKVL-ICDEPTSALDVSVQAQILDLLRDLQAeLGIAYLFIT 502
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVE 196
|
90 100 110
....*....|....*....|....*....|.
gi 490704625 503 HNFGVVEyLADRI------AVMHGGRIVEMG 527
Cdd:cd03270 197 HDEDTIR-AADHVidigpgAGVHGGEIVAQG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
159-249 |
4.12e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLE-----LLAGIQRemgmavLLITHDLAVVrNVAHHVALMRG 233
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecflgALAGKTR------VLATHQVHVV-PRADYVVALGD 856
|
90
....*....|....*.
gi 490704625 234 GEIVESADARTFFERP 249
Cdd:PTZ00243 857 GRVEFSGSSADFMRTS 872
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
322-515 |
6.54e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 322 TFTLRAGETLALLGESGCGKTTtgkaLLRLVEG--ARVQGRAMLDGHDLLGASRRELRRLRQ---DIQIVFQDPFASLDP 396
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKST----LLALLKNeiSADGGSYTFPGNWQLAWVNQETPALPQpalEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 397 RMRVGDILEEG--IASLRPELAASAR---RARAVGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPKVLICDEP 471
Cdd:PRK10636 97 QLHDANERNDGhaIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490704625 472 TSALDVSVQAQILDLLRDLQAELgiayLFITHNFGVVEYLADRI 515
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVDKI 216
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
430-532 |
8.51e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 430 RVGLPADTptrypheFSGGQRQRIAIARAL---AVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFG 506
Cdd:TIGR00630 822 RLGQPATT-------LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLD 893
|
90 100 110
....*....|....*....|....*....|..
gi 490704625 507 VVEyLADRIAVM------HGGRIVEMGPADTV 532
Cdd:TIGR00630 894 VIK-TADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
320-489 |
1.14e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 320 GVTFTLRAGETLALLGESGCGKTTtgkaLLRLVEGARVQGraMLDGhdllgasrrelrrlrqDIQIV----FQDPFASLD 395
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTT----LMDVLAGRKTGG--YIEG----------------DIRISgfpkKQETFARIS 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 396 PRMRVGDI------LEEGI---ASLR-PELAASARRARAVG----LLER-------VGLPADTptryphEFSGGQRQRIA 454
Cdd:PLN03140 956 GYCEQNDIhspqvtVRESLiysAFLRlPKEVSKEEKMMFVDevmeLVELdnlkdaiVGLPGVT------GLSTEQRKRLT 1029
|
170 180 190
....*....|....*....|....*....|....*
gi 490704625 455 IARALAVEPKVLICDEPTSALDVSVQAQILDLLRD 489
Cdd:PLN03140 1030 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-266 |
1.24e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 20 ESGVTHavKRLQL------AVAQGETFALVGESGSGKSmtalALLRLLpdAGRIVGGQIE------------------LG 75
Cdd:PLN03140 885 EQGVTE--DRLQLlrevtgAFRPGVLTALMGVSGAGKT----TLMDVL--AGRKTGGYIEgdirisgfpkkqetfariSG 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 76 GTDLNDLSERAMRgVRGGRIGIIF-QEPA-TSLNPVMRVGDQIVEtLAAHTPLRGAAareraidwlrrVGIPEPErridd 153
Cdd:PLN03140 957 YCEQNDIHSPQVT-VRESLIYSAFlRLPKeVSKEEKMMFVDEVME-LVELDNLKDAI-----------VGLPGVT----- 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 154 ypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQrEMGMAVLLITHDLAV-VRNVAHHVALM- 231
Cdd:PLN03140 1019 ---GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSIdIFEAFDELLLMk 1094
|
250 260 270
....*....|....*....|....*....|....*
gi 490704625 232 RGGEIVESADartfFERPRHPYArELFEAIPTFAK 266
Cdd:PLN03140 1095 RGGQVIYSGP----LGRNSHKII-EYFEAIPGVPK 1124
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
159-238 |
1.26e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLEllAGIQREM-GMAVLLITHDLAVVRNVaHHVALMRGGEIV 237
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
.
gi 490704625 238 E 238
Cdd:PLN03130 819 E 819
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-228 |
1.28e-03 |
|
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: 41.46 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 27 VKRLQLAVAQGETFALVGESGSGKSmtalALLRLL-----PDAGRI-VGGQIELGGTDLndlSERAMRGVRGgrigiIFQ 100
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKS----TLFRMItgqeqPDSGTIeIGETVKLAYVDQ---SRDALDPNKT-----VWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 101 EPATSLNpVMRVGDQIVETLA--AHTPLRGAaareraiDWLRRVGipeperriddypfQFSGGQKQRLMIAIALAAEPKL 178
Cdd:TIGR03719 406 EISGGLD-IIKLGKREIPSRAyvGRFNFKGS-------DQQKKVG-------------QLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490704625 179 LIADEPTTALDV-TVQA--QVLELLAGiqremgmAVLLITHDLAVVRNVAHHV 228
Cdd:TIGR03719 465 LLLDEPTNDLDVeTLRAleEALLNFAG-------CAVVISHDRWFLDRIATHI 510
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
425-537 |
1.46e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 425 VGLLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVE-PKVL-ICDEPTSALDVSVQAQILDLLRDLQaELGIAYLFIT 502
Cdd:TIGR00630 469 LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVE 547
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490704625 503 HNFGVVEyLADRI------AVMHGGRIVEMGPADTVLHAPR 537
Cdd:TIGR00630 548 HDEDTIR-AADYVidigpgAGEHGGEVVASGTPEEILANPD 587
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
159-216 |
2.04e-03 |
|
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: 40.89 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLagiqREMGMAVLLITH 216
Cdd:TIGR00954 584 SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
25-68 |
2.08e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.16 E-value: 2.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490704625 25 HAVKRLQLAVAQGETFALV-GESGSGKSMTALALLRLLPDAGRIV 68
Cdd:COG3267 30 EALARLEYALAQGGGFVVLtGEVGTGKTTLLRRLLERLPDDVKVA 74
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
445-556 |
2.10e-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: 41.05 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 445 FSGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILD--LLRDLQAELGIaylFITHNfgvVEYL--ADRIAVMHG 520
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNKTRI---LVTSK---LEHLkkADKILLLHE 622
|
90 100 110
....*....|....*....|....*....|....*.
gi 490704625 521 GRIVEMGpADTVLHAPRHEMTQRLLAAVPRLRFGAE 556
Cdd:TIGR01271 623 GVCYFYG-TFSELQAKRPDFSSLLLGLEAFDNFSAE 657
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
446-518 |
2.13e-03 |
|
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: 39.27 E-value: 2.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490704625 446 SGGQRQRIAIARALA---VEPKVLIC-DEPTSALDVSVQAQILDLLRDlQAELGIAYLFITHNFGVVEyLADRIAVM 518
Cdd:cd03227 79 SGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAE-LADKLIHI 153
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
159-233 |
2.40e-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: 39.09 E-value: 2.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREMGMAVLLITHDLAVVRNVAHHVALMRG 233
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
156-226 |
2.41e-03 |
|
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: 38.88 E-value: 2.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490704625 156 FQFSGGQKQRLMIAIALA-AEPK---LLIADEPTTALDVTVQAQVLELLAGiQREMGMAVLLITHDLAVVRNVAH 226
Cdd:cd03227 76 LQLSGGEKELSALALILAlASLKprpLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAELADK 149
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
159-248 |
2.55e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.73 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLEllAGIQREM-GMAVLLITHDLAVVRNVAHHVALMRG---- 233
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD--SCMKDELkGKTRVLVTNQLHFLPLMDRIILVSEGmike 819
|
90
....*....|....*.
gi 490704625 234 -GEIVESADARTFFER 248
Cdd:PLN03232 820 eGTFAELSKSGSLFKK 835
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
427-530 |
2.82e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 427 LLERVGLPADTPTRYPHEFSGGQRQRIAIARALAVEPK--VLICDEPTSAL---DVSVQAQILDLLRDlqaeLGIAYLFI 501
Cdd:PRK00635 459 ILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLhpqDTHKLINVIKKLRD----QGNTVLLV 534
|
90 100 110
....*....|....*....|....*....|....*.
gi 490704625 502 THNFGVVEyLADRI------AVMHGGRIVEMG-PAD 530
Cdd:PRK00635 535 EHDEQMIS-LADRIidigpgAGIFGGEVLFNGsPRE 569
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
133-225 |
2.97e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 133 ERAIDWLRrvgIPEPERRIDdypfQFSGGQKQRLMIAIALAAEPKLLIADEPTTALDV-TVQ--AQVLELLAGiqremgm 209
Cdd:PRK11819 146 EIAMDALR---CPPWDAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVAwlEQFLHDYPG------- 211
|
90
....*....|....*.
gi 490704625 210 AVLLITHDLAVVRNVA 225
Cdd:PRK11819 212 TVVAVTHDRYFLDNVA 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
157-190 |
2.99e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.99e-03
10 20 30
....*....|....*....|....*....|....
gi 490704625 157 QFSGGQKQRLMIAIALAAEPKLLIADEPTTALDV 190
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
446-521 |
3.28e-03 |
|
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: 39.84 E-value: 3.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALDVSVQAQILD-LLRDLQAELgiAYLFITHNfgvVEYL--ADRIAVMHGG 521
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANK--TRILVTSK---MEHLkkADKILILHEG 234
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
284-349 |
4.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 4.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 284 APEAGA---VVLDVQDLLVHYPVRKGVLRRVA--AWVEAVNGVTFT--------LRAGETLALLGESGCGKTTTGKALL 349
Cdd:PRK01889 138 AWESGAepvIVLTKADLCEDAEEKIAEVEALApgVPVLAVSALDGEgldvlaawLSGGKTVALLGSSGVGKSTLVNALL 216
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
446-528 |
6.55e-03 |
|
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: 38.75 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 446 SGGQRQRIAIARAL---AVEPKVLICDEPTSALDVSVQAQILDLLRDLqAELGIAYLFITHNFGVVEyLADRIAVM---- 518
Cdd:cd03271 171 SGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK-CADWIIDLgpeg 248
|
90
....*....|..
gi 490704625 519 --HGGRIVEMGP 528
Cdd:cd03271 249 gdGGGQVVASGT 260
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
159-240 |
8.59e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490704625 159 SGGQKQRLMIAIALAAEPKLLIADEPTTALDVTVQAQVLELLAGIQREmGMAVLLITHDLAVVRNVAHHVALMRGGE--- 235
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvag 471
|
....*
gi 490704625 236 IVESA 240
Cdd:PRK10982 472 IVDTK 476
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
446-476 |
8.96e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 8.96e-03
10 20 30
....*....|....*....|....*....|.
gi 490704625 446 SGGQRQRIAIARALAVEPKVLICDEPTSALD 476
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
446-517 |
9.88e-03 |
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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: 37.59 E-value: 9.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490704625 446 SGGQRQ------RIAIARALAVEPKVLICDEPTSALDV-SVQAQILDLLRDLQAELGIAYLFITHNFGVVEYLADRIAV 517
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
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