|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-541 |
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: 533.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVA-NPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQF-TTSGTVELAGRTIdLGVAADS 107
Cdd:COG4172 7 LSVEDLSVAfGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAaHPSGSILFDGQDL-LGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 108 LRRLRGGGIVWLPQDPFTSLSPLHRCGVQVI----AHRQGPRSERAERALARLAEVGL--PARAARAYPHQLSGGMRQRV 181
Cdd:COG4172 86 LRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAevlrLHRGLSGAAARARALELLERVGIpdPERRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 182 AIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 262 ARPATDYARQLLDAqlrldgpspRPAGAvPATTVADERPIVALRDVVKEF--RSGG-RRAEGHL-ALAGVSLDILPGQSV 337
Cdd:COG4172 246 AAPQHPYTRKLLAA---------EPRGD-PRPVPPDAPPLLEARDLKVWFpiKRGLfRRTVGHVkAVDGVSLTLRRGETL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 338 GIVGESGSGKTTLARITVGLEaPDSGTVHVARAP--GAGRGAPPP----VGIVFQNPYSALNPARTVGQTLAEALAVGGQ 411
Cdd:COG4172 316 GLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldGLSRRALRPlrrrMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 412 GG------AQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAE 485
Cdd:COG4172 395 GLsaaerrARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 486 QGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVP 541
Cdd:COG4172 475 HGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-542 |
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: 527.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDpDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIdlgvaADSLR 109
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDL-----LELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RLRGGGIVWLPQDPFTSLSPLhRCGVQV---IAHRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAA 186
Cdd:COG1123 79 ALRGRRIGMVFQDPMTQLNPV-TVGDQIaeaLENLGLSRAEARARVLELLEAVGLERRLDR-YPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 187 LDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPat 266
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 267 dyarQLLDAQlrldgPSPRPAGAVPATTVADERPIVALRDVVKEFRSGGRRaeGHLALAGVSLDILPGQSVGIVGESGSG 346
Cdd:COG1123 235 ----QALAAV-----PRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKG--GVRAVDDVSLTLRRGETLGLVGESGSG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 347 KTTLARITVGLEAPDSGTVHV------ARAPGAGRGAPPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGG-----AQ 415
Cdd:COG1123 304 KSTLARLLLGLLRPTSGSILFdgkdltKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSraerrER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 416 VPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITH 495
Cdd:COG1123 384 VAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 541492527 496 DLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVPG 542
Cdd:COG1123 464 DLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPS 510
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-537 |
4.85e-113 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 345.92 E-value: 4.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL--APAQFTTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQ 121
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpSPPVVYPSGDIRFHGESL-LHASEQTLRGVRGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSLSPLHRCGVQ---VIAHRQGPRSE--RAErALARLAEVGL--PARAARAYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:PRK15134 100 EPMVSLNPLHTLEKQlyeVLSLHRGMRREaaRGE-ILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLD 274
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 275 AQLRLDgPSPRPAGAVPATTVADERpivalrdVVKEFRSG--GRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLAR 352
Cdd:PRK15134 259 SEPSGD-PVPLPEPASPLLDVEQLQ-------VAFPIRKGilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 353 ITVGLeAPDSGTVHVARAP--GAGRGAPPPV----GIVFQNPYSALNPARTVGQTLAEALAV------GGQGGAQVPDLL 420
Cdd:PRK15134 331 ALLRL-INSQGEIWFDGQPlhNLNRRQLLPVrhriQVVFQDPNSSLNPRLNVLQIIEEGLRVhqptlsAAQREQQVIAVM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 421 GAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVA 500
Cdd:PRK15134 410 EEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV 489
|
490 500 510
....*....|....*....|....*....|....*..
gi 541492527 501 RQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLI 537
Cdd:PRK15134 490 RALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-541 |
4.71e-99 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 312.56 E-value: 4.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAG--------RTIDLGVAADS-LRRLRGGGI 116
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQ---AGGLVQCDKmllrrrsrQVIELSEQSAAqMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 117 VWLPQDPFTSLSPLHRCGVQV---IAHRQGPRSERAERALAR-LAEVGLPARAA--RAYPHQLSGGMRQRVAIAAALDAA 190
Cdd:PRK10261 107 AMIFQEPMTSLNPVFTVGEQIaesIRLHQGASREEAMVEAKRmLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 191 PGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYAR 270
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 271 QLLDAQLRL------DGPS-------PRPAGAVPAT---TVADERPIVALRDVVKEF--RSG--GRRAEGHLALAGVSLD 330
Cdd:PRK10261 267 ALLAAVPQLgamkglDYPRrfplislEHPAKQEPPIeqdTVVDGEPILQVRNLVTRFplRSGllNRVTREVHAVEKVSFD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 331 ILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------ARAPGAGRGAPPPVGIVFQNPYSALNPARTVGQTLAE 404
Cdd:PRK10261 347 LWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqridTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIME 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 405 ALAV-----GGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLL 479
Cdd:PRK10261 427 PLRVhgllpGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 480 RRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVP 541
Cdd:PRK10261 507 LDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
295-541 |
1.14e-98 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 302.04 E-value: 1.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 295 VADERPIVALRDVVKEFRSGG---RRAEGHL-ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH---- 366
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGglfGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 -VARAPGAG-RGAPPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGGAQ-----VPDLLGAVGLPAAHAQRLPAALSG 439
Cdd:COG4608 81 dITGLSGRElRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAerrerVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 440 GQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260
....*....|....*....|..
gi 541492527 520 ATEALLAAPSHPYTASLIDAVP 541
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVP 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
302-546 |
4.00e-95 |
|
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: 289.78 E-value: 4.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA------RAPGAGR 375
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVP---VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvtrRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GApppVGIVFQNPYSALNPARTVGQTLAEALAVGGQG--GAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAA 453
Cdd:COG1124 79 RR---VQMVFQDPYASLHPRHTVDRILAEPLRIHGLPdrEERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYT 533
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
250
....*....|...
gi 541492527 534 ASLIDAVPGRGAP 546
Cdd:COG1124 236 RELLAASLAFERA 248
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
301-546 |
2.59e-92 |
|
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: 285.41 E-value: 2.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAP---DSGTVH-----VARAPG 372
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK---AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgedLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 373 A------GRGapppVGIVFQNPYSALNPARTVGQTLAEALAVGGQGG-----AQVPDLLGAVGLPAA--HAQRLPAALSG 439
Cdd:COG0444 78 KelrkirGRE----IQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSkaearERAIELLERVGLPDPerRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 440 GQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|....*..
gi 541492527 520 ATEALLAAPSHPYTASLIDAVPGRGAP 546
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDPD 260
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
301-519 |
5.03e-91 |
|
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: 278.62 E-value: 5.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRRaegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAGR 375
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS---VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GAP-PPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGGAQ------VPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIA 448
Cdd:cd03257 78 KIRrKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKearkeaVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 449 RALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
48-291 |
2.24e-79 |
|
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: 251.90 E-value: 2.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQDPFTSL 127
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDL-LKLSEKELRKIRGREIQMIFQDPMTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGVQV----IAHRQGPRSERAERALARLAEVGL--PARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:COG0444 100 NPVMTVGDQIaeplRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLDG 281
Cdd:COG0444 180 ALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPRHPYTRALLSSIPRLDP 259
|
250
....*....|...
gi 541492527 282 PSPRPA---GAVP 291
Cdd:COG0444 260 DGRRLIpipGEPP 272
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
300-547 |
9.79e-74 |
|
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: 243.82 E-value: 9.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGL----EAPDSGTVH-----VARA 370
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVE---AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILfdgqdLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 371 PGAG----RGAPppVGIVFQNPYSALNPARTVGQTLAEALAV-GGQGGAQ----VPDLLGAVGLPAAhAQRL---PAALS 438
Cdd:COG4172 82 SERElrriRGNR--IAMIFQEPMTSLNPLHTIGKQIAEVLRLhRGLSGAAararALELLERVGIPDP-ERRLdayPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 439 GGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEE 518
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260
....*....|....*....|....*....
gi 541492527 519 GATEALLAAPSHPYTASLIDAVPGRGAPA 547
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAAEPRGDPRP 267
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-255 |
2.32e-71 |
|
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: 227.77 E-value: 2.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPD-RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtiDLGVAADSL 108
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP---TSGSIIFDGK--DLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRGGGIVWLPQDPFTSLSPLHRCGVQV----IAHRQGPRSERAERALARLAE-VGLPARAARAYPHQLSGGMRQRVAI 183
Cdd:cd03257 77 RKIRRKEIQMVFQDPMSSLNPRMTIGEQIaeplRIHGKLSKKEARKEAVLLLLVgVGLPEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-287 |
1.96e-68 |
|
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: 229.40 E-value: 1.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPDRPIVA--DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADS 107
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAvdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP---TSGSILFDGKDLT-KLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 108 LRRLRGG-GIVwlPQDPFTSLSPLHRCGVQV----IAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVA 182
Cdd:COG1123 337 LRELRRRvQMV--FQDPYSSLNPRMTVGDIIaeplRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 183 IAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
250 260
....*....|....*....|....*
gi 541492527 263 RPATDYARQLLDAQlrldgPSPRPA 287
Cdd:COG1123 495 NPQHPYTRALLAAV-----PSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
300-542 |
4.74e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 222.53 E-value: 4.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVK--EFRSGGRRAEGHL-ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGT-----VHVARAP 371
Cdd:PRK11308 4 PLLQAIDLKKhyPVKRGLFKPERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyyqgQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 372 GAGRGA-PPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGGA-----QVPDLLGAVGLPAAHAQRLPAALSGGQRQRV 445
Cdd:PRK11308 84 PEAQKLlRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAaerreKALAMMAKVGLRPEHYDRYPHMFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
250
....*....|....*..
gi 541492527 526 AAPSHPYTASLIDAVPG 542
Cdd:PRK11308 244 NNPRHPYTQALLSATPR 260
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
296-540 |
1.34e-64 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 211.21 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 296 ADERPIVALRDVVKEFrsgGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGR 375
Cdd:COG4107 3 NEEQPLLSVRGLSKRY---GPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDGGPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 ---GAPPP---------VGIVFQNPYSALNPARTVGQTLAEAL-AVG----GQGGAQVPDLLGAVGLPAAHAQRLPAALS 438
Cdd:COG4107 80 dlfALSEAerrrlrrtdWGMVYQNPRDGLRMDVSAGGNIAERLmAAGerhyGDIRARALEWLERVEIPLERIDDLPRTFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 439 GGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEE 518
Cdd:COG4107 160 GGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVES 239
|
250 260
....*....|....*....|..
gi 541492527 519 GATEALLAAPSHPYTASLIDAV 540
Cdd:COG4107 240 GLTDQVLEDPQHPYTQLLVSSV 261
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
301-529 |
1.00e-62 |
|
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: 205.51 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA------RAPGAG 374
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVT---ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltlLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RGAPPPVGIVFQNpYSALNpARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:cd03258 78 RKARRRIGMIFQH-FNLLS-SRTVFENVALPLEIAGVPKAEieerVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPS 529
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-282 |
4.58e-62 |
|
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: 204.27 E-value: 4.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPDR-PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSL 108
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP---WSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRgggIVWlpQDPFTSLSPLHRCGvQVIA-----HRQGPRSERAERALArlaEVGLPARAARAYPHQLSGGMRQRVAI 183
Cdd:COG1124 79 RRVQ---MVF--QDPYASLHPRHTVD-RILAeplriHGLPDREERIAELLE---QVGLPPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
250
....*....|....*....
gi 541492527 264 PATDYARQLLDAQLRLDGP 282
Cdd:COG1124 230 PKHPYTRELLAASLAFERA 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
301-547 |
1.96e-61 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 205.70 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAPGAG- 374
Cdd:COG1135 1 MIELENLSKTFPTKGG---PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdgvdlTALSEREl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RGAPPPVGIVFQNpySALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:COG1135 78 RAARRKIGMIFQH--FNLLSSRTVAENVALPLEIAGVPKAEirkrVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSH 530
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
250
....*....|....*..
gi 541492527 531 PYTASLIDAVPGRGAPA 547
Cdd:COG1135 235 ELTRRFLPTVLNDELPE 251
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
323-541 |
6.81e-61 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 204.17 E-value: 6.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH------VARAPGAGRGAPPPVGIVFQNPYSALNPAR 396
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdlLGMKDDEWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 TVGQTLAEALAV------GGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVS 470
Cdd:PRK15079 116 TIGEIIAEPLRTyhpklsRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 471 VQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVP 541
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
299-547 |
8.67e-61 |
|
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: 208.99 E-value: 8.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 299 RPIVALRDVVKEFRSGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPD---SGTVHVA-----RA 370
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPA-----VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgrdllEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 371 PGAGRGAPppVGIVFQNPYSALNPArTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVA 446
Cdd:COG1123 77 SEALRGRR--IGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAEararVLELLEAVGL-ERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 447 IARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|.
gi 541492527 527 APSHPYTASLIDAVPGRGAPA 547
Cdd:COG1123 233 APQALAAVPRLGAARGRAAPA 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
48-280 |
1.10e-60 |
|
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: 209.16 E-value: 1.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttsGTVELAGRTIDlGVAADSLRRLRGG-GIVWlpQDPFTS 126
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE----GEIRFDGQDLD-GLSRRALRPLRRRmQVVF--QDPFGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LSPLHRCGvQVIA-----HRQGP-RSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:COG4172 375 LSPRMTVG-QIIAeglrvHGPGLsAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 201 TALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLD 280
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
305-537 |
2.05e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 197.75 E-value: 2.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 305 RDVVKEF--RSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagRGAPPPVG 382
Cdd:COG4167 8 RNLSKTFkyRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILI-------NGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 383 ----------IVFQNPYSALNPARTVGQTLAEALAV-----GGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAI 447
Cdd:COG4167 81 dykyrckhirMIFQDPNTSLNPRLNIGQILEEPLRLntdltAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 448 ARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|
gi 541492527 528 PSHPYTASLI 537
Cdd:COG4167 241 PQHEVTKRLI 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
300-540 |
1.52e-57 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 192.98 E-value: 1.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGG-RRAEGHLA-LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP-----G 372
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGlSGKHQHQTvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklnR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 373 AGRGA-PPPVGIVFQNPYSALNPARTVGQTLAE------ALAVGGQGgAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRV 445
Cdd:PRK10419 82 AQRKAfRRDIQMVFQDSISAVNPRKTVREIIREplrhllSLDKAERL-ARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250
....*....|....*
gi 541492527 526 AApSHPYTASLIDAV 540
Cdd:PRK10419 241 TF-SSPAGRVLQNAV 254
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
300-518 |
1.23e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 186.40 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAPGAG 374
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVT---ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdiSSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RGApp--pVGIVFQNPYsaLNPARTVGQTLAEALAVGGQGGAQVP----DLLGAVGLpAAHAQRLPAALSGGQRQRVAIA 448
Cdd:COG1136 80 LARlrrrhIGFVFQFFN--LLPELTALENVALPLLLAGVSRKERRerarELLERVGL-GDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 449 RALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARqMSDRIIVMKDGAIVEE 518
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
296-518 |
1.29e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 187.60 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 296 ADERPIVALRDVVKEFRSGGrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGR 375
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGG---GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GapPPVGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARAL 451
Cdd:COG1116 79 G--PDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAErrerARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 452 AARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDL--AVArqMSDRIIVMKD--GAIVEE 518
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAVF--LADRVVVLSArpGRIVEE 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
300-537 |
3.96e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 189.54 E-value: 3.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGR---G 376
Cdd:COG3842 4 PALELENVSKRY-------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-----GRdvtG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APP---PVGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIAR 449
Cdd:COG3842 72 LPPekrNVGMVFQDY--ALFPHLTVAENVAFGLRMRGVPKAEirarVAELLELVGL-EGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 450 ALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPS 529
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
....*...
gi 541492527 530 HPYTASLI 537
Cdd:COG3842 229 TRFVADFI 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
302-518 |
5.64e-54 |
|
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: 181.90 E-value: 5.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSGGRRaegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGapPPV 381
Cdd:cd03293 1 LEVRNVSKTYGGGGGA---VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG--PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 GIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPEL 457
Cdd:cd03293 76 GYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEarerAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVM--KDGAIVEE 518
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
302-515 |
4.01e-53 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 179.61 E-value: 4.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSGGRRaegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA-----RAPGAGRG 376
Cdd:cd03255 1 IELKNLSKTYGGGGEK---VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 A--PPPVGIVFQNPYsaLNPARTVGQTLAEALAVGGQGGAQVPD----LLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:cd03255 78 AfrRRHIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKERREraeeLLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARqMSDRIIVMKDGAI 515
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
304-540 |
6.59e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 183.42 E-value: 6.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRGAP---PP 380
Cdd:COG1118 5 VRNISKRF--GSFTL-----LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN-----GRDLFtnlPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 ----VGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALA 452
Cdd:COG1118 73 rerrVGFVFQHY--ALFPHMTVAENIAFGLRVRPPSKAEirarVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPY 532
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
....*...
gi 541492527 533 TASLIDAV 540
Cdd:COG1118 230 VARFLGCV 237
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
42-281 |
7.89e-53 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 182.62 E-value: 7.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQ 121
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREI-LNLPEKELNKLRAEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSLSPLHRCGVQVIA----HRQGPRSERAERALARLAEVGLP-ARA-ARAYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:PRK09473 105 DPMTSLNPYMRVGEQLMEvlmlHKGMSKAEAFEESVRMLDAVKMPeARKrMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDA 275
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
....*.
gi 541492527 276 QLRLDG 281
Cdd:PRK09473 265 VPRLDA 270
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
304-547 |
9.87e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 182.69 E-value: 9.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------ARAPGAGRGA 377
Cdd:PRK11153 4 LKNISKVFPQGGRTIH---ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 378 PPPVGIVFQNPYsaLNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAA 453
Cdd:PRK11153 81 RRQIGMIFQHFN--LLSSRTVFDNVALPLELAGTPKAEikarVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYT 533
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
250
....*....|....
gi 541492527 534 ASLIDAVPGRGAPA 547
Cdd:PRK11153 238 REFIQSTLHLDLPE 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
296-540 |
3.05e-52 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 178.58 E-value: 3.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 296 ADERPIVALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH--------- 366
Cdd:PRK11701 1 MMDQPLLSVRGLTKLY--GPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 -VARAPGAGRG--APPPVGIVFQNPYSALNPARTVGQTLAEAL-AVG----GQGGAQVPDLLGAVGLPAAHAQRLPAALS 438
Cdd:PRK11701 74 dLYALSEAERRrlLRTEWGFVHQHPRDGLRMQVSAGGNIGERLmAVGarhyGDIRATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 439 GGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEE 518
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|..
gi 541492527 519 GATEALLAAPSHPYTASLIDAV 540
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSSV 255
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
48-288 |
7.20e-52 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 179.93 E-value: 7.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLRGG-GIVWlpQDPFTS 126
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP---TSGEILFDGQDI-TGLSGRELRPLRRRmQMVF--QDPYAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LSPLHRCGvQVIA-----HRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:COG4608 108 LNPRMTVG-DIIAeplriHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQlrldg 281
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLSAV----- 261
|
....*..
gi 541492527 282 PSPRPAG 288
Cdd:COG4608 262 PVPDPER 268
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
301-540 |
9.17e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 176.72 E-value: 9.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPP 380
Cdd:COG1126 1 MIEIENLHKSF-------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 -----VGIVFQNPysALNPARTVGQTLAEAL-AVGGQGGAQVP----DLLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:COG1126 74 klrrkVGMVFQQF--NLFPHLTVLENVTLAPiKVKKMSKAEAEeramELLERVGL-ADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 451 LAARPELLICDEAVSALD---VS-VQATIIDLlrrlqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDpelVGeVLDVMRDL-----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|....
gi 541492527 527 APSHPYTASLIDAV 540
Cdd:COG1126 226 NPQHERTRAFLSKV 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
316-528 |
6.63e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 174.06 E-value: 6.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA---RAPGAGRGAPPPVGIVFQNPYSAL 392
Cdd:COG1122 9 SYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdITKKNLRELRRKVGLVFQNPDDQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 npartVGQTLAEALAVG----GQGGAQVP----DLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAV 464
Cdd:COG1122 89 -----FAPTVEEDVAFGpenlGLPREEIRerveEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 465 SALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:COG1122 163 AGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
304-519 |
5.33e-50 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 171.16 E-value: 5.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSggrraegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRgaPP---P 380
Cdd:cd03259 3 LKGLSKTYGS-------VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPerrN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 VGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLPAaHAQRLPAALSGGQRQRVAIARALAARPE 456
Cdd:cd03259 74 IGMVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEirarVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 457 LLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
300-532 |
1.49e-49 |
|
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: 170.93 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAPGAG 374
Cdd:COG1127 4 PMIEVRNLTKSF-------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqdiTGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RGAPPP-VGIVFQNpySALNPARTVGQ----------TLAEALAVggqggAQVPDLLGAVGLPAAhAQRLPAALSGGQRQ 443
Cdd:COG1127 77 LYELRRrIGMLFQG--GALFDSLTVFEnvafplrehtDLSEAEIR-----ELVLEKLELVGLPGA-ADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 444 RVAIARALAARPELLICDEAVSALD-VSVqATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATE 522
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|
gi 541492527 523 ALLAAPsHPY 532
Cdd:COG1127 228 ELLASD-DPW 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
304-532 |
8.01e-49 |
|
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: 168.83 E-value: 8.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG------RGA 377
Cdd:cd03261 3 LRGLTKSF--GGRTV-----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 378 PPPVGIVFQNpySALNPARTVGQTLAEALAVGGQG-----GAQVPDLLGAVGLPAAhAQRLPAALSGGQRQRVAIARALA 452
Cdd:cd03261 76 RRRMGMLFQS--GALFDSLTVFENVAFPLREHTRLseeeiREIVLEKLEAVGLRGA-EDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPsHPY 532
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPL 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
302-537 |
6.45e-48 |
|
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: 166.26 E-value: 6.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGrgAPP-- 379
Cdd:cd03300 1 IELENVSKFY-------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPhk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 380 -PVGIVFQNpYsALNPARTVGQTLAEALAVGGQGGA----QVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAAR 454
Cdd:cd03300 72 rPVNTVFQN-Y-ALFPHLTVFENIAFGLRLKKLPKAeikeRVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 455 PELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTA 534
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
...
gi 541492527 535 SLI 537
Cdd:cd03300 229 DFI 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
48-275 |
9.59e-48 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 168.77 E-value: 9.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLA--PAQfTTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQDPFT 125
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGR-VMAEKLEFNGQDL-QRISEKERRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVI----AHRQGPRSERAERALARLAEVGLPARAAR--AYPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:PRK11022 101 SLNPCYTVGFQIMeaikVHQGGNKKTRRQRAIDLLNQVGIPDPASRldVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 200 TTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDA 275
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
327-541 |
1.21e-46 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 166.07 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 327 VSLDILPGQSVGIVGESGSGKTTLARITVGL-EAPdsGTVHVARAPGAGR--------------GAPppVGIVFQNPYSA 391
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVMAEKLEFNGQdlqrisekerrnlvGAE--VAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 392 LNPARTVGQTLAEALAVGgQGGAQ------VPDLLGAVGLPAAhAQRL---PAALSGGQRQRVAIARALAARPELLICDE 462
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVH-QGGNKktrrqrAIDLLNQVGIPDP-ASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVP 541
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP 258
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
304-513 |
1.40e-46 |
|
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: 160.82 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRsggrraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAGRGAP 378
Cdd:cd03229 3 LKNVSKRYG-------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgeDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 PPVGIVFQNPysALNPARTVGQTLAEalavggqggaqvpdllgavglpaahaqrlpaALSGGQRQRVAIARALAARPELL 458
Cdd:cd03229 76 RRIGMVFQDF--ALFPHLTVLENIAL-------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 459 ICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
323-513 |
1.76e-46 |
|
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: 161.87 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG---RGAPPPVGIVFQNPYSALnpartVG 399
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslKELRRKVGLVFQNPDDQF-----FG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVG----GQGGAQVP----DLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:cd03225 91 PTVEEEVAFGlenlGLPEEEIEerveEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 541492527 472 QATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:cd03225 170 RRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
327-540 |
6.49e-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: 161.54 E-value: 6.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 327 VSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG------------RGAPPPVGIVFQNPYSALNP 394
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyqlseaerrRLMRTEWGFVHQNPRDGLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 ARTVGQTLAEAL-AVG----GQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:TIGR02323 102 RVSAGANIGERLmAIGarhyGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDV 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 470 SVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAV 540
Cdd:TIGR02323 182 SVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
299-523 |
6.74e-46 |
|
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: 161.06 E-value: 6.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 299 RPIVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV----------- 367
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELT---ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfalded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 368 ARAPGAGRGapppVGIVFQNpySALNPARTVGQTLAEALAVGGQGGAQVP--DLLGAVGLpAAHAQRLPAALSGGQRQRV 445
Cdd:COG4181 83 ARARLRARH----VGFVFQS--FQLLPTLTALENVMLPLELAGRRDARARarALLERVGL-GHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEA 523
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
302-527 |
8.43e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 8.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRsggrraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAPGAGRG 376
Cdd:COG1131 1 IEVRGLTKRYG-------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvARDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 ApppVGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALA 452
Cdd:COG1131 74 R---IGYVPQEP--ALYPDLTVRENLRFFARLYGLPRKEarerIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
47-277 |
2.36e-45 |
|
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: 159.46 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPAQFTTSGTVELAGRTidlgVAADSLRRLRGGGIVwlpQDPFT 125
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGlLPPGLTQTSGEILLDGRP----LLPLSIRGRHIATIM---QNPRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQV---IAHRQGPRSERAERALARLAEVGL--PARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:TIGR02770 74 AFNPLFTMGNHAietLRSLGKLSKQARALILEALEAVGLpdPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 201 TALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQL 277
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAHL 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
48-285 |
3.84e-45 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 162.06 E-value: 3.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRLRGGGIVWLPQDPFTSL 127
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP---TGGELYYQG--QDLLKADPEAQKLLRQKIQIVFQNPYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGVQV----IAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:PRK11308 106 NPRKKVGQILeeplLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLDgPS 283
Cdd:PRK11308 186 DVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLN-PD 264
|
..
gi 541492527 284 PR 285
Cdd:PRK11308 265 DR 266
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
322-519 |
7.93e-45 |
|
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: 159.13 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRGAPPP---------VGIVFQNPYSAL 392
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTLDEenlweirkkVGMVFQNPDNQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 npartVGQTLAEALAVG--GQG------GAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAV 464
Cdd:TIGR04520 91 -----VGATVEDDVAFGleNLGvpreemRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 465 SALDVSVQATIIDLLRRLQAEQGFALAFITHDL--AVarqMSDRIIVMKDGAIVEEG 519
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMeeAV---LADRVIVMNKGKIVAEG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
300-546 |
9.89e-45 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 165.65 E-value: 9.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGGrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLA-RITVGLEAP------------DSGTVH 366
Cdd:PRK15134 4 PLLAIENLSVAFRQQQ---TVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvypsgdirfhGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 VARAPGAG-RGAPppVGIVFQNPYSALNPARTVGQTLAEALAVG-GQGG----AQVPDLLGAVGLPAAhAQRL---PAAL 437
Cdd:PRK15134 81 ASEQTLRGvRGNK--IAMIFQEPMVSLNPLHTLEKQLYEVLSLHrGMRReaarGEILNCLDRVGIRQA-AKRLtdyPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 438 SGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVE 517
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|....*....
gi 541492527 518 EGATEALLAAPSHPYTASLIDAVPgRGAP 546
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNSEP-SGDP 265
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
302-537 |
1.17e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 161.39 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRG 376
Cdd:COG3839 4 LELENVSKSY-------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdVTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 apppVGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALA 452
Cdd:COG3839 77 ----IAMVFQSY--ALYPHMTVYENIAFPLKLRKVPKAEidrrVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPY 532
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
....*
gi 541492527 533 TASLI 537
Cdd:COG3839 230 VAGFI 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
44-526 |
1.37e-44 |
|
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: 164.98 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfTTSGTV----------------------------ELA 95
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYE-PTSGRIiyhvalcekcgyverpskvgepcpvcggTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 96 GRTIDLGVAADSLRRLRGGGIVWLPQDPFtSLSPLHRCGVQVIA--HRQGPRSERA-ERALARLAEVGLPAR---AARay 169
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEalEEIGYEGKEAvGRAVDLIEMVQLSHRithIAR-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 170 phQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:TIGR03269 168 --DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 250 AIVEAGQARRVLARpatdYARQLLDAQlrldgpsprpagavPATTVADERPIVALRDVVKEFRSGGRraeGHL-ALAGVS 328
Cdd:TIGR03269 246 EIKEEGTPDEVVAV----FMEGVSEVE--------------KECEVEVGEPIIKVRNVSKRYISVDR---GVVkAVDNVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 329 LDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV--------ARAPGA-GRG-APPPVGIVFQNpYSaLNPARTV 398
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdMTKPGPdGRGrAKRYIGILHQE-YD-LYPHRTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLAEALavggqgGAQVPDLLG---------AVGLPAAHAQ----RLPAALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:TIGR03269 383 LDNLTEAI------GLELPDELArmkavitlkMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 466 ALD----VSVQATIidLLRRLQAEQGFALafITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:TIGR03269 457 TMDpitkVDVTHSI--LKAREEMEQTFII--VSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
50-527 |
1.74e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 164.42 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQDPftSLSP 129
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQP---DSGEILLDGEPVRFRSPRDAQAA----GIAIIHQEL--NLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 ---------LHRcgvqvIAHRQGPRSERAERALAR--LAEVGL---PARAARayphQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:COG1129 93 nlsvaenifLGR-----EPRRGGLIDWRAMRRRARelLARLGLdidPDTPVG----DLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 196 ADEPTTALdvtTQKEILTLLASLRD--ARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVlarPATDYARQLL 273
Cdd:COG1129 164 LDEPTASL---TEREVERLFRIIRRlkAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL---TEDELVRLMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 274 DAQLrldgpsprpAGAVPATTVADERPIVALRDVvkefrSGGRRaeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARI 353
Cdd:COG1129 238 GREL---------EDLFPKRAAAPGEVVLEVEGL-----SVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 354 TVGLEAPDSGTVHVarapgagRGAPppvgIVFQNPYSA----------------LNPARTVGQ--TLAeALAVGGQGG-- 413
Cdd:COG1129 298 LFGADPADSGEIRL-------DGKP----VRIRSPRDAiragiayvpedrkgegLVLDLSIREniTLA-SLDRLSRGGll 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 414 ------AQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQG 487
Cdd:COG1129 366 drrrerALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEG 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 541492527 488 FALAFITHDLAVARQMSDRIIVMKDGAIVEE----GAT-EALLAA 527
Cdd:COG1129 445 KAVIVISSELPELLGLSDRILVMREGRIVGEldreEATeEAIMAA 489
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
300-524 |
2.10e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.53 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGgrraegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA-RAPGAGRGAP 378
Cdd:COG3638 1 PMLELRNLSKRYPGG------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDgQDVTALRGRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 -----PPVGIVFQNPysALNPARTVGQT-LAEALA--------VGGQGGAQVP---DLLGAVGLpAAHAQRLPAALSGGQ 441
Cdd:COG3638 75 lrrlrRRIGMIFQQF--NLVPRLSVLTNvLAGRLGrtstwrslLGLFPPEDREralEALERVGL-ADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 442 RQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGAT 521
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
...
gi 541492527 522 EAL 524
Cdd:COG3638 232 AEL 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
334-541 |
3.49e-44 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 159.50 E-value: 3.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 334 GQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGA----------GRGAPPPVGIVFQNPYSALNPARTVGQTLA 403
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGReilnlpekelNKLRAEQISMIFQDPMTSLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 404 EALAV-GGQGGAQVPD----LLGAVGLPAAHaQRL---PAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATI 475
Cdd:PRK09473 122 EVLMLhKGMSKAEAFEesvrMLDAVKMPEAR-KRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 476 IDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVP 541
Cdd:PRK09473 201 MTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
305-537 |
2.20e-43 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 155.33 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 305 RDVVKEFR--SGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP---GAGRGAPP 379
Cdd:PRK15112 8 RNLSKTFRyrTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfGDYSYRSQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 380 PVGIVFQNPYSALNPARTVGQTLAEALAVGGQGGA-----QVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAAR 454
Cdd:PRK15112 88 RIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPeqrekQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 455 PELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTA 534
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTK 247
|
...
gi 541492527 535 SLI 537
Cdd:PRK15112 248 RLI 250
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
300-537 |
2.35e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 158.19 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAG 374
Cdd:PRK09452 13 PLVELRGISKSF-------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqdITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RgappPVGIVFQNpYsALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:PRK09452 86 R----HVNTVFQS-Y-ALFPHMTVFENVAFGLRMQKTPAAEitprVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSH 530
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
....*..
gi 541492527 531 PYTASLI 537
Cdd:PRK09452 239 LFVARFI 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
302-537 |
3.78e-42 |
|
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: 150.95 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAGRG 376
Cdd:cd03296 3 IEVRNVSKRF-------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggeDATDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 apppVGIVFQNpYsALNPARTVGQTLAEALAV--------GGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIA 448
Cdd:cd03296 76 ----VGFVFQH-Y-ALFRHMTVFDNVAFGLRVkprserppEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 449 RALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....*....
gi 541492527 529 SHPYTASLI 537
Cdd:cd03296 229 ASPFVYSFL 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
302-539 |
3.84e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 151.30 E-value: 3.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKefrsggRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapGAGRGAPPPV 381
Cdd:cd03295 1 IEFENVTK------RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID---GEDIREQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 ------GIVFQNpySALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLPAAH-AQRLPAALSGGQRQRVAIARA 450
Cdd:cd03295 72 elrrkiGYVIQQ--IGLFPHMTVEENIALVPKLLKWPKEKirerADELLALVGLDPAEfADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSH 530
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*....
gi 541492527 531 PYTASLIDA 539
Cdd:cd03295 230 DFVAEFVGA 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
302-515 |
1.09e-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: 148.83 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPP- 380
Cdd:cd03262 1 IEIKNLHKSF-------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 ----VGIVFQNpySALNPARTVGQTLAEAL-AVGGQGGAQVP----DLLGAVGLpAAHAQRLPAALSGGQRQRVAIARAL 451
Cdd:cd03262 74 lrqkVGMVFQQ--FNLFPHLTVLENITLAPiKVKGMSKAEAEeralELLEKVGL-ADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 452 AARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
305-541 |
1.31e-41 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 150.49 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 305 RDVVKEFRSGGRRAEGH------LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG--RG 376
Cdd:cd03294 15 QKAFKLLAKGKSKEEILkktgqtVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPPV-----GIVFQNpySALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAI 447
Cdd:cd03294 95 ELRELrrkkiSMVFQS--FALLPHRTVLENVAFGLEVQGVPRAEreerAAEALELVGL-EGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 448 ARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
250
....*....|....
gi 541492527 528 PSHPYTASLIDAVP 541
Cdd:cd03294 252 PANDYVREFFRGVD 265
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
297-546 |
2.18e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.17 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 297 DERPIVALRDVVKEFRSGGRraeghLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRG 376
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-----YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-----GMV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPP--------VGIVFQNPYSALnpartVGQTLAEALAVG--GQGGA------QVPDLLGAVGLpAAHAQRLPAALSGG 440
Cdd:PRK13635 71 LSEEtvwdvrrqVGMVFQNPDNQF-----VGATVQDDVAFGleNIGVPreemveRVDQALRQVGM-EDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 441 QRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGA 520
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
250 260 270
....*....|....*....|....*....|....
gi 541492527 521 TEALLAAPSH--------PYTASLIDAVPGRGAP 546
Cdd:PRK13635 224 PEEIFKSGHMlqeigldvPFSVKLKELLKRNGIL 257
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
302-538 |
7.04e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 147.97 E-value: 7.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRsggrraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-------ARAPGAG 374
Cdd:PRK11264 4 IEVKNLVKKFH-------GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RGA----PPPVGIVFQNpySALNPARTVGQTLAEALAV-----GGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRV 445
Cdd:PRK11264 77 KGLirqlRQHVGFVFQN--FNLFPHRTVLENIIEGPVIvkgepKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|...
gi 541492527 526 AAPSHPYTASLID 538
Cdd:PRK11264 233 ADPQQPRTRQFLE 245
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
301-520 |
9.44e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 146.74 E-value: 9.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAPgagR 375
Cdd:COG2884 1 MIRFENVSKRYP------GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlSRLK---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GAPPP----VGIVFQNpySALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAI 447
Cdd:COG2884 72 REIPYlrrrIGVVFQD--FRLLPDRTVYENVALPLRVTGKSRKEirrrVREVLDLVGL-SDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 448 ARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA 520
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
302-532 |
3.39e-40 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 154.99 E-value: 3.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVkeFRSGGRraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-------------HVA 368
Cdd:COG2274 474 IELENVS--FRYPGD---SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaSLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 369 RApgagrgapppVGIVFQNPY--SAlnpartvgqTLAEALAVGGQGgAQVPDLLGAVGLPAAHA--QRLP---------- 434
Cdd:COG2274 549 RQ----------IGVVLQDVFlfSG---------TIRENITLGDPD-ATDEEIIEAARLAGLHDfiEALPmgydtvvgeg 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 435 -AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqaEQGFALAFITHDLAVARqMSDRIIVMKDG 513
Cdd:COG2274 609 gSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVLDKG 685
|
250
....*....|....*....
gi 541492527 514 AIVEEGATEALLAAPSHPY 532
Cdd:COG2274 686 RIVEDGTHEELLARKGLYA 704
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
302-519 |
7.05e-40 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 143.93 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRG 376
Cdd:cd03301 1 VELENVTKRF-------GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 apppVGIVFQNpYsALNPARTVGQTLAEALAVGGQGGA-------QVPDLLGAvglpAAHAQRLPAALSGGQRQRVAIAR 449
Cdd:cd03301 74 ----IAMVFQN-Y-ALYPHMTVYDNIAFGLKLRKVPKDeidervrEVAELLQI----EHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 450 ALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-528 |
1.04e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.46 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGagRGAPPPVGIVFQNPYSALN-PArt 397
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--RRARRRIGYVPQRAEVDWDfPI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 vgqTLAEALAVG--GQGG----------AQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:COG1121 93 ---TVRDVVLMGryGRRGlfrrpsradrEAVDEALERVGL-EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 466 ALDVSVQATIIDLLRRLQAEqGFALAFITHDLAVARQMSDRIIVMKDGaIVEEGATEALLAAP 528
Cdd:COG1121 169 GVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPE 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
48-290 |
1.18e-39 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 147.16 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLRGGgIVWLPQDPFTSL 127
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA---TDGEVAWLGKDL-LGMKDDEWRAVRSD-IQMIFQDPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGvQVIA------HRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK15079 112 NPRMTIG-EIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDA------ 275
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAvpipdp 270
|
250 260
....*....|....*....|....*..
gi 541492527 276 --------QLrLDG--PSP--RPAGAV 290
Cdd:PRK15079 271 dlernktiQL-LEGelPSPinPPSGCV 296
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
301-531 |
1.31e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 144.08 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFrsggrraeGHLA-LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV----ARAPGAG- 374
Cdd:PRK09493 1 MIEFKNVSKHF--------GPTQvLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkVNDPKVDe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 RGAPPPVGIVFQNPY-----SALN-----PARTVGQTLAEAlavggqgGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQR 444
Cdd:PRK09493 73 RLIRQEAGMVFQQFYlfphlTALEnvmfgPLRVRGASKEEA-------EKQARELLAKVGL-AERAHHYPSELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 445 VAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
....*..
gi 541492527 525 LAAPSHP 531
Cdd:PRK09493 224 IKNPPSQ 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
324-519 |
3.62e-39 |
|
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: 142.05 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDI---LPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP---GAGRGAPPP----VGIVFQNpySALN 393
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdSRKKINLPPqqrkIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 394 PARTVGQTLAEALAVGGQGG--AQVPDLLGAVGLPAAhAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREdrISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 472 QATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
290-545 |
5.41e-39 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 150.78 E-value: 5.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 290 VPATTVADERPIVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-- 367
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFMQEQQKIA---AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 368 -----------------ARAPGAGRGAPppVGIVFQNPYSALNPARTVGQTLAEAL-----AVGGQGGAQVPDLLGAVGL 425
Cdd:PRK10261 78 mllrrrsrqvielseqsAAQMRHVRGAD--MAMIFQEPMTSLNPVFTVGEQIAESIrlhqgASREEAMVEAKRMLDQVRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 426 PAAHA--QRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQM 503
Cdd:PRK10261 156 PEAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEI 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 541492527 504 SDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVPGRGA 545
Cdd:PRK10261 236 ADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGA 277
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
323-541 |
5.62e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 145.05 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLeAPDSGTVHVARAPGAGR---GAPPP---------VGIVFQNPYS 390
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADRFRWNGIdllKLSPRerrkiigreIAMIFQEPSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALNPARTVGQTLAEALAVGGQGG----------AQVPDLLGAVGL--PAAHAQRLPAALSGGQRQRVAIARALAARPELL 458
Cdd:COG4170 101 CLDPSAKIGDQLIEAIPSWTFKGkwwqrfkwrkKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 459 ICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLID 538
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLR 260
|
...
gi 541492527 539 AVP 541
Cdd:COG4170 261 SMP 263
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
320-540 |
1.73e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 141.72 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-------------VARApgagrgapppVGIVFQ 386
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsrreLARR----------IAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 NPYSAlnpartVGQTLAEALAVG--------GQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAAR 454
Cdd:COG1120 83 EPPAP------FGLTVRELVALGryphlglfGRPSAEdreaVEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 455 PELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLaapshpyTA 534
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-------TP 228
|
....*.
gi 541492527 535 SLIDAV 540
Cdd:COG1120 229 ELLEEV 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
44-262 |
1.82e-38 |
|
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: 141.10 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlGVAADSLRRLRGG-GIVWlpQD 122
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD---SGEVLIDGEDIS-GLSEAELYRLRRRmGMLF--QS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 P--FTSLS-------PLHRcgvqviaHRQGPRSERAERALARLAEVGLPArAARAYPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:cd03261 86 GalFDSLTvfenvafPLRE-------HTRLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
42-264 |
1.91e-38 |
|
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: 140.55 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaADSLRRLRGG-GIVwlP 120
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP---TSGEVLVDGKDIT----KKNLRELRRKvGLV--F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSL-----------SPLHRcGVqviahrqgPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDA 189
Cdd:COG1122 82 QNPDDQLfaptveedvafGPENL-GL--------PREEIRERVEEALELVGLEHLADRP-PHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
316-524 |
2.26e-38 |
|
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: 140.78 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------ARAPGAGRGAPPPVGIVFQNPy 389
Cdd:cd03256 9 TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinKLKGKALRQLRRQIGMIFQQF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 sALNPARTVGQT-LAEALA--------VGGQGGAQVP---DLLGAVGLPAAHAQRLpAALSGGQRQRVAIARALAARPEL 457
Cdd:cd03256 88 -NLIERLSVLENvLSGRLGrrstwrslFGLFPKEEKQralAALERVGLLDKAYQRA-DQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
320-519 |
2.36e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 138.72 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRgapppvgivfqnPYSALNPArtvg 399
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-----GK------------DLASLSPK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 qTLAEALAVggqggaqVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLL 479
Cdd:cd03214 70 -ELARKIAY-------VPQALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 541492527 480 RRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03214 141 RRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
46-251 |
2.75e-38 |
|
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: 139.93 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DLGVAADSLRRLRGGGIVW-----L 119
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRP---TSGEVRVDGTDIsKLSEKELAAFRRRHIGFVFqsfnlL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQdpFTSLS----PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:cd03255 95 PD--LTALEnvelPLLLAGV--------PKKERRERAEELLERVGLGDRLNH-YPSELSGGQQQRVAIARALANDPKIIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARdYGDDIVVMRGGAI 251
Cdd:cd03255 164 ADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
339-537 |
2.80e-38 |
|
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: 143.02 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 339 IVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAGRgappPVGIVFQNpySALNPARTVGQTLAEALAVGGQGG 413
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSImldgeDVTNVPPHLR----HINMVFQS--YALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 414 AQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFA 489
Cdd:TIGR01187 75 AEikprVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 490 LAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLI 537
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
46-524 |
4.82e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.33 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVA--DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQ-- 121
Cdd:COG3845 17 GVVAndDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQP---DSGEILIDGKPVRIRSPRDAIAL----GIGMVHQhf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 ---DPFT-------SLSPLHRcgvqviahrQGPRSERAERALARLAE-VGLPARAaRAYPHQLSGGMRQRVAIAAALDAA 190
Cdd:COG3845 90 mlvPNLTvaenivlGLEPTKG---------GRLDRKAARARIRELSErYGLDVDP-DAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 191 PGVLIADEPTTALdvtTQKEILTLLASLRD--ARGMALVLVTHDLALARDYGDDIVVMRGGAIVEagqarRVLARPATdy 268
Cdd:COG3845 160 ARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG-----TVDTAETS-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 269 ARQLldAQLRLDGPSPRPagaVPATTVADERPIVALRDVVkefrsgGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKT 348
Cdd:COG3845 230 EEEL--AELMVGREVLLR---VEKAPAEPGEVVLEVENLS------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 349 TLARITVGLEAPDSGTVHVarapgAGRgapppvgivfqnPYSALNPAR-----------------TVGQ-TLAEALAVGG 410
Cdd:COG3845 299 ELAEALAGLRPPASGSIRL-----DGE------------DITGLSPRErrrlgvayipedrlgrgLVPDmSVAENLILGR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 411 QGGAQVPDLL----GAVglpAAHAQRL-------------PA-ALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQ 472
Cdd:COG3845 362 YRRPPFSRGGfldrKAI---RAFAEELieefdvrtpgpdtPArSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAI 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 541492527 473 ATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:COG3845 439 EFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
328-537 |
1.19e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 138.73 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 328 SLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRgappPVGIVFQ--NPYSALNPARTVGQ 400
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdLTALPPAER----PVSMLFQenNLFPHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 401 TLAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALA-ARPeLLICDEAVSALDVSVQATIIDLL 479
Cdd:COG3840 95 GLRPGLKLTAEQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 480 RRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLI 537
Cdd:COG3840 173 DELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
302-513 |
1.66e-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: 136.37 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSggrraegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAPGAGRG 376
Cdd:cd03230 1 IEVRNLSKRYGK-------KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdiKKEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 ApppVGIVFQNPYsaLNPARTVGQTLAealavggqggaqvpdllgavglpaahaqrlpaaLSGGQRQRVAIARALAARPE 456
Cdd:cd03230 74 R---IGYLPEEPS--LYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 457 LLICDEAVSALDVSVQATIIDLLRRLQAEQGFALaFITHDLAVARQMSDRIIVMKDG 513
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTIL-LSSHILEEAERLCDRVAILNNG 171
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
48-276 |
4.43e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 138.05 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLRgggIVWlpQDPFTSL 127
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEP---TSGEILINGHKLEYGDYKYRCKHIR---MIF--QDPNTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGVQVIA----HRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:COG4167 101 NPRLNIGQILEEplrlNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQ 276
Cdd:COG4167 181 DMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIESH 253
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
42-253 |
4.69e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.71 E-value: 4.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLRRLRGG--GIVWl 119
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRP---TSGEVLIDGQDIS-SLSERELARLRRRhiGFVF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 pQDP--FTSLS-------PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAA 190
Cdd:COG1136 93 -QFFnlLPELTalenvalPLLLAGV--------SRKERRERARELLERVGLGDRL-DHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 191 PGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARdYGDDIVVMRGGAIVE 253
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
321-539 |
5.47e-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: 140.24 E-value: 5.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDI---LPGQSV-GIVGESGSGKTTLARITVGLEAPDSGTVHVARAP----GAGRGAPP---PVGIVFQNPy 389
Cdd:COG4148 8 RLRRGGFTLDVdftLPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsARGIFLPPhrrRIGYVFQEA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 sALNPARTVGQTLAEAL--AVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:COG4148 87 -RLFPHLSVRGNLLYGRkrAPRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 468 DVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDA 539
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEA 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
302-524 |
6.44e-37 |
|
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: 136.54 E-value: 6.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGL-----EAPDSGTVHVARAPGAGRG 376
Cdd:cd03260 1 IELRDLNVYY--GDKHA-----LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPP-----VGIVFQNPysalNPAR-TVGQTLAEALAVGGQGGAQVPD-----LLGAVGLPAAHAQRLPA-ALSGGQRQR 444
Cdd:cd03260 74 VDVLelrrrVGMVFQKP----NPFPgSIYDNVAYGLRLHGIKLKEELDerveeALRKAALWDEVKDRLHAlGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 445 VAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEqgFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
324-529 |
6.68e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 140.22 E-value: 6.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRgappPVGIVFQNpYsALNPARTV 398
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdVSRLHARDR----KVGFVFQH-Y-ALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLAEALAV--------GGQGGAQVPDLLGAVGLpaAH-AQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:PRK10851 92 FDNIAFGLTVlprrerpnAAAIKAKVTQLLEMVQL--AHlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 470 SVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPS 529
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
44-255 |
7.21e-37 |
|
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: 136.65 E-value: 7.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLRRLRGG-GIVWlpQD 122
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP---DSGEILVDGQDIT-GLSEKELYELRRRiGMLF--QG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 P--FTSLS-------PLHRcgvqviaHRQGPRSERAERALARLAEVGLPArAARAYPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:COG1127 91 GalFDSLTvfenvafPLRE-------HTDLSEAEIRELVLEKLELVGLPG-AADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
321-534 |
9.09e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.68 E-value: 9.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVAR---------APGAGRGAPPPVGIVFQNpYSa 391
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpSDKAIRELRRNVGMVFQQ-YN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 392 LNPARTVGQTLAEA-LAVGG----QGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK11124 93 LWPHLTVQQNLIEApCRVLGlskdQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 467 LDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALlaapSHPYTA 534
Cdd:PRK11124 172 LDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF----TQPQTE 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
310-515 |
1.05e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 310 EFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGrgAPPP-----VGIV 384
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPewrrqVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 385 FQNPysALnPARTVGQTLAEALAVGGQG--GAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDE 462
Cdd:COG4619 80 PQEP--AL-WGGTVRDNLPFPFQLRERKfdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
262-527 |
1.15e-36 |
|
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: 143.36 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 262 ARPATDYARQLLDAQlrldgPSPRPAGAVPATtvADERPIVALRDVVkeFRSGGRRAeghlALAGVSLDILPGQSVGIVG 341
Cdd:COG4988 304 GIAAAEKIFALLDAP-----EPAAPAGTAPLP--AAGPPSIELEDVS--FSYPGGRP----ALDGLSLTIPPGERVALVG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 342 ESGSGKTTLARITVGLEAPDSGTVHVARAPGagRGAPPP-----VGIVFQNPYsalnparTVGQTLAEALAVGGQG--GA 414
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDL--SDLDPAswrrqIAWVPQNPY-------LFAGTIRENLRLGRPDasDE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 415 QVPDLLGAVGLpAAHAQRLP-----------AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQ 483
Cdd:COG4988 442 ELEAALEAAGL-DEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 541492527 484 AEQgfALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAA 527
Cdd:COG4988 521 KGR--TVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
44-249 |
1.61e-36 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 134.90 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlgvaADSLRRLRGG-GIVwlPQD 122
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDLT----KLSLKELRRKvGLV--FQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSLsplhrCGVQV---IA----HRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:cd03225 84 PDDQF-----FGPTVeeeVAfgleNLGLPEEEIEERVEEALELVGLEGLRDR-SPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
30-261 |
1.66e-36 |
|
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: 136.33 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPsdpDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTI-DLGVAAdsL 108
Cdd:COG1120 2 LEAENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLaSLSRRE--L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRGggivWLPQDPFTSLsplhrcGVQV--------IAHRQGPRSERAE-RALAR--LAEVGLPARAARAYpHQLSGGM 177
Cdd:COG1120 74 ARRIA----YVPQEPPAPF------GLTVrelvalgrYPHLGLFGRPSAEdREAVEeaLERTGLEHLADRPV-DELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 178 RQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQA 257
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 541492527 258 RRVL 261
Cdd:COG1120 223 EEVL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
46-264 |
1.96e-36 |
|
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: 135.40 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLgVAADSLRRLRGG-GIVWLPQDPF 124
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL---ERPTSGSVLVDGTDLTL-LSGKELRKARRRiGMIFQHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLS-------PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:cd03258 95 SSRTvfenvalPLEIAGV--------PKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
43-361 |
2.08e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 138.29 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVA--DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLRGG-GIVwl 119
Cdd:COG1135 14 KGGPVTAldDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERP---TSGSVLVDGVDL-TALSERELRAARRKiGMI-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQDpFTSLS----------PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAArAYPHQLSGGMRQRVAIAAALDA 189
Cdd:COG1135 88 FQH-FNLLSsrtvaenvalPLEIAGV--------PKAEIRKRVAELLELVGLSDKAD-AYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYA 269
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 270 RQLLDAQLRLDGPSPRPAGAVPAttvADERPIVALRdvvkeFRsgGRRAEG----HLALA-GVSLDILPGqSVGIVGEsg 344
Cdd:COG1135 238 RRFLPTVLNDELPEELLARLREA---AGGGRLVRLT-----FV--GESADEpllsELARRfGVDVNILSG-GIEEIQG-- 304
|
330
....*....|....*..
gi 541492527 345 sgkTTLARITVGLEAPD 361
Cdd:COG1135 305 ---TPVGRLIVELEGDD 318
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
296-519 |
2.85e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 136.03 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 296 ADERPIVALRDVVKEFRSggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG- 374
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQS-----DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 --RGAPPPVGIVFQNPYSALnpartVGQTLAEALAVGGQGGA--------QVPDLLGAVGLpAAHAQRLPAALSGGQRQR 444
Cdd:PRK13648 77 nfEKLRKHIGIVFQNPDNQF-----VGSIVKYDVAFGLENHAvpydemhrRVSEALKQVDM-LERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 445 VAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEG 519
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
320-533 |
4.54e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.76 E-value: 4.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARA---------PGAGRGAPPPVGIVFQNpYS 390
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQ-YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 aLNPARTVGQTLAEA-LAVGGQGGAQVPD----LLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:COG4161 93 -LWPHLTVMENLIEApCKVLGLSKEQAREkamkLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 466 ALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALlaapSHPYT 533
Cdd:COG4161 171 ALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQT 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
301-537 |
5.40e-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: 137.32 E-value: 5.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV----------ARA 370
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQ---ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVdgqdlttlsnSEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 371 PGAGRGapppVGIVFQnpYSALNPARTVGQTLAEALAVGGQGG----AQVPDLLGAVGLPAAHaQRLPAALSGGQRQRVA 446
Cdd:TIGR02314 78 TKARRQ----IGMIFQ--HFNLLSSRTVFGNVALPLELDNTPKdeikRKVTELLALVGLGDKH-DSYPSNLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 447 IARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:TIGR02314 151 IARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFS 230
|
250
....*....|.
gi 541492527 527 APSHPYTASLI 537
Cdd:TIGR02314 231 HPKTPLAQKFI 241
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
48-271 |
6.18e-36 |
|
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: 135.08 E-value: 6.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQDpFtSL 127
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP---TSGKVLIDGQDI-AAMSRKELRELRRKKISMVFQS-F-AL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPlHRCGVQVIAHR---QG-PRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:cd03294 114 LP-HRTVLENVAFGlevQGvPRAEREERAAEALELVGLEGWEHK-YPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQ 271
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
50-273 |
8.49e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.58 E-value: 8.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGrtIDLGVAADSLRRLRGG-GIVwlpqdpFTS-- 126
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD---SGTITVDG--EDLTDSKKDINKLRRKvGMV------FQQfn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 ------------LSPLHrcgvqviaHRQGPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:COG1126 88 lfphltvlenvtLAPIK--------VKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
302-513 |
1.52e-35 |
|
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: 130.97 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVkeFRSGGRraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG------R 375
Cdd:cd03228 1 IEFKNVS--FSYPGR---PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldleslR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GApppVGIVFQNPY--SAlnpartvgqTLAEALavggqggaqvpdllgavglpaahaqrlpaaLSGGQRQRVAIARALAA 453
Cdd:cd03228 76 KN---IAYVPQDPFlfSG---------TIRENI------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQMsDRIIVMKDG 513
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-281 |
1.66e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 133.29 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVAnpsdPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFT-TSGTVELAGRTIdlgvaadSL 108
Cdd:PRK10418 5 IELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGRVLLDGKPV-------AP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRGGGIVWLPQDPFTSLSPLHRCGVQVIAH-RQGPRSERAERALARLAEVGL--PARAARAYPHQLSGGMRQRVAIAA 185
Cdd:PRK10418 74 CALRGRKIATIMQNPRSAFNPLHTMHTHARETcLALGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 186 ALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
250
....*....|....*.
gi 541492527 266 TDYARQLLDAQLRLDG 281
Cdd:PRK10418 234 HAVTRSLVSAHLALYG 249
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
317-510 |
3.74e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 132.68 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV----HVARAPGAGRGapppvgIVFQNpySAL 392
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgVPVTGPGADRG------VVFQK--DAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 NPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:COG4525 88 LPWLNVLDNVAFGLRLRGVPKAErrarAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 541492527 469 VSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVM 510
Cdd:COG4525 167 ALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
310-513 |
6.08e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 128.90 E-value: 6.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 310 EFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPP---PVGIVFQ 386
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 npysalnpartvgqtlaealavggqggaqvpdllgavglpaahaqrlpaaLSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 541492527 467 LDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:cd00267 111 LDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
302-516 |
1.00e-34 |
|
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: 128.32 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRgapppv 381
Cdd:cd03216 1 LELRGITKRF-------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GK------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 givfqnPYSALNPArtvgqtlaEALAVGgqggaqvpdlLGAVglpaahAQrlpaaLSGGQRQRVAIARALAARPELLICD 461
Cdd:cd03216 63 ------EVSFASPR--------DARRAG----------IAMV------YQ-----LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 462 EAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIV 516
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
324-537 |
1.16e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 130.53 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVhvaRAPGAGRGAPPP----VGIVFQNpySALNPARTVG 399
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI---LLNGKDITNLPPekrdISYVPQN--YALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGG----QGGAQVPDLLGAVGLpaAHA-QRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQAT 474
Cdd:cd03299 90 KNIAYGLKKRKvdkkEIERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 475 IIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLI 537
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
63-284 |
1.32e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 133.11 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 63 IVGESGAGKSMLARAICGLAPAQFTTSgtvelAGR----TIDL-GVAADSLRRLRGGGIVWLPQDPFTSLSPLHRCG--- 134
Cdd:COG4170 38 LVGESGSGKSLIAKAICGITKDNWHVT-----ADRfrwnGIDLlKLSPRERRKIIGREIAMIFQEPSSCLDPSAKIGdql 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 135 VQVIAHRQGPRS------ERAERALARLAEVGL--PARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVT 206
Cdd:COG4170 113 IEAIPSWTFKGKwwqrfkWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 207 TQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLDGPSP 284
Cdd:COG4170 193 TQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPDFRQPLP 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
57-524 |
2.15e-34 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 135.95 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 57 PGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRtidlgvaadSLRRLRGG-----GIVWLPQDP--FTSLSP 129
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGN---------PCARLTPAkahqlGIYLVPQEPllFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LhrcgvQVIAHRQgPRSERAERAL-ARLAEVG----LPARAArayphQLSGGMRQRVAIAAALDAAPGVLIADEPTTALd 204
Cdd:PRK15439 104 K-----ENILFGL-PKRQASMQKMkQLLAALGcqldLDSSAG-----SLEVADRQIVEILRGLMRDSRILILDEPTASL- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 205 vtTQKEILTLLASLRD--ARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARR----VLARPATDYAR--QLLDAQ 276
Cdd:PRK15439 172 --TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADlstdDIIQAITPAARekSLSASQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 277 -LRLDGPSPRPagavpatTVADERPIVALRDVVKE-FRSggrraeghlalagVSLDILPGQSVGIVGESGSGKTTLARIT 354
Cdd:PRK15439 250 kLWLELPGNRR-------QQAAGAPVLTVEDLTGEgFRN-------------ISLEVRAGEILGLAGVVGAGRTELAETL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 355 VGLEAPDSGTVHV------ARAPGAGRGApppvGIVFqnpysaLNPARTVGQTLAEA--------LAVGGQG-------- 412
Cdd:PRK15439 310 YGLRPARGGRIMLngkeinALSTAQRLAR----GLVY------LPEDRQSSGLYLDAplawnvcaLTHNRRGfwikpare 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 413 GAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAF 492
Cdd:PRK15439 380 NAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLF 458
|
490 500 510
....*....|....*....|....*....|..
gi 541492527 493 ITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:PRK15439 459 ISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
320-524 |
4.67e-34 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 128.96 E-value: 4.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAG-RGAPPPVGIVFQNpySALN 393
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtDITKLRGKKlRKLRRRIGMIFQH--YNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 394 PARTVGQTLAEAlAVGGQGGAQVP-------------DLLGAVGLPAAHAQRLpAALSGGQRQRVAIARALAARPELLIC 460
Cdd:TIGR02315 92 ERLTVLENVLHG-RLGYKPTWRSLlgrfseedkeralSALERVGLADKAYQRA-DQLSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
315-539 |
1.02e-33 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 128.66 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 315 GRRAEGHLAL-AGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPD----SGTVH---VARAPGAGRGAPppVGIVFQ 386
Cdd:PRK10418 9 NIALQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLldgKPVAPCALRGRK--IATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 NPYSALNPARTVGQTLAEALAVGGQGG--AQVPDLLGAVGLPAAH--AQRLPAALSGGQRQRVAIARALAARPELLICDE 462
Cdd:PRK10418 87 NPRSAFNPLHTMHTHARETCLALGKPAddATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDA 539
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-261 |
1.39e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 128.31 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVanpSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIDlGVAADSL 108
Cdd:COG4559 2 LEAENLSV---RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTP----SSGEVRLNGRPLA-AWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRGggiVwLPQD-----PFTSLsplhrcgvQVIA----HRQGPRSERAERALARLAEVGLPARAARAYPhQLSGGMRQ 179
Cdd:COG4559 74 ARRRA---V-LPQHsslafPFTVE--------EVVAlgraPHGSSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 180 RVAIA-------AALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIV 252
Cdd:COG4559 141 RVQLArvlaqlwEPVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
....*....
gi 541492527 253 EAGQARRVL 261
Cdd:COG4559 220 AQGTPEEVL 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
284-540 |
1.74e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.11 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 284 PRPAGAVPATTvadeRPIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSG 363
Cdd:PRK11607 6 PRPQAKTRKAL----TPLLEIRNLTKSF-------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 364 TV-----HVARAPGAGRgappPVGIVFQNpySALNPARTVGQTLAEALA----VGGQGGAQVPDLLGAVGLpAAHAQRLP 434
Cdd:PRK11607 75 QImldgvDLSHVPPYQR----PINMMFQS--YALFPHMTVEQNIAFGLKqdklPKAEIASRVNEMLGLVHM-QEFAKRKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 435 AALSGGQRQRVAIARALAARPELLICDEAVSALDVSV----QATIIDLLRRLqaeqGFALAFITHDLAVARQMSDRIIVM 510
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIM 223
|
250 260 270
....*....|....*....|....*....|
gi 541492527 511 KDGAIVEEGATEALLAAPSHPYTASLIDAV 540
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
270-527 |
2.36e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 133.75 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 270 RQLLDAQLRLdgpsPRPAGAVPATTVADErpiVALRDVvkEFRSGGrraeGHLALAGVSLDILPGQSVGIVGESGSGKTT 349
Cdd:COG1132 315 FELLDEPPEI----PDPPGAVPLPPVRGE---IEFENV--SFSYPG----DRPVLKDISLTIPPGETVALVGPSGSGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 350 LARITVGLEAPDSGTV--------HVARApgAGRGApppVGIVFQNPY--SAlnpartvgqTLAEALAVGgQGGAQVPDL 419
Cdd:COG1132 382 LVNLLLRFYDPTSGRIlidgvdirDLTLE--SLRRQ---IGVVPQDTFlfSG---------TIRENIRYG-RPDATDEEV 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 420 LGAVGLPAAH--AQRLP-----------AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaeQ 486
Cdd:COG1132 447 EEAAKAAQAHefIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--K 524
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 541492527 487 GFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAA 527
Cdd:COG1132 525 GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEELLAR 564
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-517 |
2.50e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.27 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAgrtidlgvaadslRRLRgggIVWLPQD 122
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP---DSGEVSIP-------------KGLR---IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PF------------TSLSPLHRCGVQV--IAHRQG---PRSERAERALARLAEVG---LPARAAR---------AYPHQ- 172
Cdd:COG0488 70 PPldddltvldtvlDGDAELRALEAELeeLEAKLAepdEDLERLAELQEEFEALGgweAEARAEEilsglgfpeEDLDRp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 173 ---LSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTqkeILTLLASLRDARGmALVLVTHDlalaRDYGDDIV----- 244
Cdd:COG0488 150 vseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPG-TVLVVSHD----RYFLDRVAtrile 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 245 VMRGGAI---------VEAGQARrvLARPATDYARQ------LL----------------------------------DA 275
Cdd:COG0488 222 LDRGKLTlypgnysayLEQRAER--LEQEAAAYAKQqkkiakEEefirrfrakarkakqaqsrikaleklereepprrDK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 276 QLRLDGPSPRPAGavpattvadeRPIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITV 355
Cdd:COG0488 300 TVEIRFPPPERLG----------KKVLELEGLSKSY-------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 356 GLEAPDSGTVHVarapGAGrgapppVGIVF--QNpYSALNPARTVGQTLAEalavGGQGGAQVP--DLLGAVGLPAAHAQ 431
Cdd:COG0488 363 GELEPDSGTVKL----GET------VKIGYfdQH-QEELDPDKTVLDELRD----GAPGGTEQEvrGYLGRFLFSGDDAF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 432 RLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV-SVQAtIIDLLrrlqaeQGF--ALAFITHDLAVARQMSDRII 508
Cdd:COG0488 428 KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEAL------DDFpgTVLLVSHDRYFLDRVATRIL 500
|
....*....
gi 541492527 509 VMKDGAIVE 517
Cdd:COG0488 501 EFEDGGVRE 509
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
47-259 |
2.51e-33 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 126.78 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLRRLRGGGIVWLPQDpFT- 125
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRP---TSGTVRLAGQDLF-ALDEDARARLRARHVGFVFQS-FQl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 --SLSPLHRcgVQVIAHRQGpRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:COG4181 102 lpTLTALEN--VMLPLELAG-RRDARARARALLERVGLGHRL-DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARdYGDDIVVMRGGAIVEAGQARR 259
Cdd:COG4181 178 DAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
319-516 |
4.85e-33 |
|
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: 125.06 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPPVGIVFQNPYSALNPArTV 398
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLFTD-SV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDL 478
Cdd:cd03226 90 REELLLGLKELDAGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 541492527 479 LRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIV 516
Cdd:cd03226 169 IRELAA-QGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
302-515 |
7.48e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 126.33 E-value: 7.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGrgAPPPV 381
Cdd:PRK11247 13 LLLNAVSKRY--GERTV-----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 GIVFQNpySALNPARTVGQTLAeaLAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICD 461
Cdd:PRK11247 84 RLMFQD--ARLLPWKKVIDNVG--LGLKGQWRDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 462 EAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
46-255 |
1.05e-32 |
|
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: 124.55 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAAdslrRLRGGGIVWlpQDP-- 123
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP---DSGEILIDGRDV-TGVPP----ERRNIGMVF--QDYal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLhrcgvQVIA----HRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:cd03259 84 FPHLTVA-----ENIAfglkLRGVPKAEIRARVRELLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 200 TTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
43-255 |
1.16e-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: 123.31 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADsLRRLRGggivWLPQd 122
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKE-LARKIA----YVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 pftslsPLHRCGVQVIAHRqgprseraeralarlaevglparaaraYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03214 81 ------ALELLGLAHLADR---------------------------PFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 541492527 203 LDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
304-526 |
1.26e-32 |
|
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: 124.97 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSggrraegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapGAGRGAPPP--- 380
Cdd:COG4555 4 VENLSKKYGK-------VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID---GEDVRKEPRear 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 --VGIVFQNPYSalnPARTVGQTLAEALA-----VGGQGGAQVPDLLGAVGLPAaHAQRLPAALSGGQRQRVAIARALAA 453
Cdd:COG4555 74 rqIGVLPDERGL---YDRLTVRENIRYFAelyglFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
44-269 |
1.38e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.91 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADslRRlrggGIVWLPQDP 123
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP---DSGRILLDGRDVT-GLPPE--KR----NVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 --FTSLS-------PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:COG3842 87 alFPHLTvaenvafGLRMRGV--------PKAEIRARVAELLELVGLEGLADR-YPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDL--ALArdYGDDIVVMRGGAIVEAGQARRVLARPATDYA 269
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQeeALA--LADRIAVMNDGRIEQVGTPEEIYERPATRFV 232
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
320-540 |
2.32e-32 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 127.66 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------ARAPGAGRGAP-PPVGIVFQNpySAL 392
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdgenimKQSPVELREVRrKKIGMVFQQ--FAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 NPARTVGQTLAEALAVGG----QGGAQVPDLLGAVGLPAaHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:TIGR01186 83 FPHMTILQNTSLGPELLGwpeqERKEKALELLKLVGLEE-YEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 469 VSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAV 540
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
48-286 |
2.69e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.13 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLgVAADSLRRLRGGgIVWLPQDPFTSL 127
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ---GGEIIFNGQRIDT-LSPGKLQALRRD-IQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGVQVI----AHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:PRK10261 415 DPRQTVGDSIMeplrVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLDGPS 283
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSR 574
|
...
gi 541492527 284 PRP 286
Cdd:PRK10261 575 QRP 577
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
44-278 |
3.45e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.64 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtiDLGVAADSLRRLrgggIVWLPQDP 123
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP---TSGEVRVLGE--DVARDPAEVRRR----IGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTslsPLHRCGVQVIAH----RQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:COG1131 83 AL---YPDLTVRENLRFfarlYGLPRKEARERIDELLELFGLTDAADR-KVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 200 TTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLR 278
Cdd:COG1131 159 TSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEAR 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
324-532 |
3.78e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 126.77 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDI---LPGQSV-GIVGESGSGKTTLARITVGLEAPDSGTVHVA----RAPGAGRGAPP---PVGIVFQNpySAL 392
Cdd:TIGR02142 9 LGDFSLDAdftLPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlFDSRKGIFLPPekrRIGYVFQE--ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 NPARTVGQTLAEAL--AVGGQGG---AQVPDLLGAVGLpaahAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:TIGR02142 87 FPHLSVRGNLRYGMkrARPSERRisfERVIELLGIGHL----LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 468 DVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPY 532
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
42-253 |
4.00e-32 |
|
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: 122.97 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaadslRRLRGGGIVwlPQ 121
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP---TSGEVLVDGEPVT--------GPGPDRGYV--FQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPftSLSPlHRCGVQVIA----HRQGPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:cd03293 81 QD--ALLP-WLTVLDNVAlgleLQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVM--RGGAIVE 253
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
44-253 |
5.29e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.05 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdlgvaadslrRLRGGGIVWLPQDP 123
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP---TSGEVLVDGKPV----------TGPGPDRGVVFQEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftSLSP-----------LHRCGVqviahrqgPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPG 192
Cdd:COG1116 90 --ALLPwltvldnvalgLELRGV--------PKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 193 VLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHD----LALArdygDDIVVM--RGGAIVE 253
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvdeaVFLA----DRVVVLsaRPGRIVE 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
303-528 |
6.44e-32 |
|
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: 122.93 E-value: 6.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 303 ALRDVVKEFRsggrraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRgapPPVG 382
Cdd:cd03219 2 EVRGLTKRFG-------GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL---PPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 383 IV-------FQNP--YSALnpartvgqTLAEALAVGGQGG------------------AQVPDLLGAVGLpAAHAQRLPA 435
Cdd:cd03219 72 IArlgigrtFQIPrlFPEL--------TVLENVMVAAQARtgsglllararreerearERAEELLERVGL-ADLADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 436 ALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
250
....*....|...
gi 541492527 516 VEEGATEALLAAP 528
Cdd:cd03219 222 IAEGTPDEVRNNP 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
328-526 |
7.43e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.77 E-value: 7.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 328 SLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV------HVARAPgagrgAPPPVGIVFQ--NPYSALNPARTVG 399
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdHTTTPP-----SRRPVSMLFQenNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLL 479
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 541492527 480 RRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
320-511 |
1.04e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.49 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA-RAPGAGRGApppVGIVFQNPYSALN-PArT 397
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgKPLEKERKR---IGYVPQRRSIDRDfPI-S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 VGQTLAEALA--VGGQGGAQVPD------LLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:cd03235 87 VRDVVLMGLYghKGLFRRLSKADkakvdeALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 541492527 470 SVQATIIDLLRRLQAEqGFALAFITHDLAVARQMSDRIIVMK 511
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
44-252 |
1.07e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.86 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLRGG-GIVWlpQD 122
Cdd:COG3638 15 GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEP---TSGEILVDGQDV-TALRGRALRRLRRRiGMIF--QQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 P--FTSLSPL---------HRCGVQVIAHRQgPRSERaERALARLAEVGLPARA-ARAypHQLSGGMRQRVAIAAALDAA 190
Cdd:COG3638 89 FnlVPRLSVLtnvlagrlgRTSTWRSLLGLF-PPEDR-ERALEALERVGLADKAyQRA--DQLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 191 PGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIV 252
Cdd:COG3638 165 PKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
324-463 |
1.20e-31 |
|
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: 119.29 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPP---VGIVFQNPysALNPARTVGQ 400
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 401 TLAEALAVGGQG----GAQVPDLLGAVGLPAAHAQRL---PAALSGGQRQRVAIARALAARPELLICDEA 463
Cdd:pfam00005 79 NLRLGLLLKGLSkrekDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
300-546 |
1.59e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 124.53 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSggrrAEGHL-ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLeAPDSGTVHVAR--------- 369
Cdd:PRK15093 2 PLLDIRNLTIEFKT----SDGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRmrfddidll 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 370 --APGAGRG-APPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGG----------AQVPDLLGAVGL--PAAHAQRLP 434
Cdd:PRK15093 77 rlSPRERRKlVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGrwwqrfgwrkRRAIELLHRVGIkdHKDAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 435 AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGA 514
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260 270
....*....|....*....|....*....|..
gi 541492527 515 IVEEGATEALLAAPSHPYTASLIDAVPGRGAP 546
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALIRAIPDFGSA 268
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
44-251 |
1.62e-31 |
|
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: 121.10 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDL-GVAADSLRRlrGGGIVWLPQD 122
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD---SGTIIIDGLKLTDdKKNINELRQ--KVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSLSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLPARAArAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03262 87 LFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKAD-AYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 541492527 203 LDVTTQKEILTLLASLrdAR-GMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:cd03262 166 LDPELVGEVLDVMKDL--AEeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
317-527 |
2.11e-31 |
|
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: 121.44 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVaraPGAGRGAPPP------VGIVFQNpyS 390
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV---DGHDLALADPawlrrqVGVVLQE--N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALnpartVGQTLAEALAVGGQGgAQVPDLLGAVGLPAAHA--QRLP-----------AALSGGQRQRVAIARALAARPEL 457
Cdd:cd03252 86 VL-----FNRSIRDNIALADPG-MSMERVIEAAKLAGAHDfiSELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAeqGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
323-529 |
2.21e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.99 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPP------PVGIVFQNPYSALnpar 396
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdireKVGIVFQNPDNQF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 tVGQTLAEALAVGGQGgAQVP---------DLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:PRK13640 98 -VGATVGDDVAFGLEN-RAVPrpemikivrDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 468 DVSVQATIIDLLRRLQAEQGFALAFITHDLAVArQMSDRIIVMKDGAIVEEGATEALLAAPS 529
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
319-529 |
2.43e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 122.40 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV----ARAPGAGRGAPPPVGIVFQNPYSALnp 394
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidTGDFSKLQGIRKLVGIVFQNPETQF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 artVGQTLAEALAVGGQG--------GAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK13644 91 ---VGRTVEEDLAFGPENlclppieiRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 467 LDVSVQATIIDLLRRLQaEQGFALAFITHDLAvARQMSDRIIVMKDGAIVEEGATEALLAAPS 529
Cdd:PRK13644 167 LDPDSGIAVLERIKKLH-EKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
43-291 |
2.47e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.49 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtiDLGVAADSLRRlrggGIVWLPQD 122
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETP---DSGRIVLNGR--DLFTNLPPRER----RVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 P--FTSLSplhrcgvqV---IA----HRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:COG1118 84 YalFPHMT--------VaenIAfglrVRPPSKAEIRARVEELLELVQLEGLADR-YPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
250 260
....*....|....*....|....*....
gi 541492527 274 -----------DAQLRLDGPSPRPAGAVP 291
Cdd:COG1118 235 gcvnvlrgrviGGQLEADGLTLPVAEPLP 263
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-251 |
2.68e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.31 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPsdpDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLR 109
Cdd:COG4619 1 LELEGLSFRVG---GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP---TSGEIYLDGKPLS-AMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RLrgggIVWLPQDPF----TslsplhrcgvqVIAH--------RQGPRSERAERALARLaevGLPARAARAYPHQLSGGM 177
Cdd:COG4619 74 RQ----VAYVPQEPAlwggT-----------VRDNlpfpfqlrERKFDRERALELLERL---GLPPDILDKPVERLSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 178 RQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-261 |
2.71e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdlgvaadslrRLRGGGIVWLPQD- 122
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP---TSGTVRLFGKPP----------RRARRRIGYVPQRa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 ------PFT-----SLSPLHRCGVqviahRQGPRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAP 191
Cdd:COG1121 85 evdwdfPITvrdvvLMGRYGRRGL-----FRRPSRADREAVDEALERVGLEDLADRPI-GELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGaIVEAGQARRVL 261
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVL 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-514 |
5.24e-31 |
|
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: 119.51 E-value: 5.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPPVGIVFQNPYSALNPARTVG 399
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGG--QGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIID 477
Cdd:COG4133 94 ENLRFWAALYGlrADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAE 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 541492527 478 LLRRlQAEQGFALAFITHDLAVARqmSDRIIVMKDGA 514
Cdd:COG4133 173 LIAA-HLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
298-524 |
5.49e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.90 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 298 ERPIVALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA------RAP 371
Cdd:COG1129 1 AEPLLEMRGISKSF--GGVKA-----LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrfRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 372 GAGRGAppPVGIVFQNPysALNPARTVgqtlAEALAVG---GQGG--------AQVPDLLGAVGLPAAHAQRLpAALSGG 440
Cdd:COG1129 74 RDAQAA--GIAIIHQEL--NLVPNLSV----AENIFLGrepRRGGlidwramrRRARELLARLGLDIDPDTPV-GDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 441 QRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA 520
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
....
gi 541492527 521 TEAL 524
Cdd:COG1129 224 VAEL 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
48-273 |
6.44e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 121.05 E-value: 6.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLRgggivWLPQDPFTSL 127
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP---TSGELLIDDHPLHFGDYSYRSQRIR-----MIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCG----VQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:PRK15112 101 NPRQRISqildFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
302-519 |
6.84e-31 |
|
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: 119.24 E-value: 6.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVaRAPGAGRGAPPP- 380
Cdd:cd03268 1 LKTNDLTKTY--GKKRV-----LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-DGKSYQKNIEALr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 -VGIVFQNPysALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLI 459
Cdd:cd03268 73 rIGALIEAP--GFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 460 CDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
30-261 |
1.04e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 120.26 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVanpSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIDlGVAADSL 108
Cdd:PRK13548 3 LEARNLSV---RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSP----DSGEVRLNGRPLA-DWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRGggiVwLPQD-----PFTSLsplhrcgvQVIA----HRQGPRSERAERALARLAEVGLPARAARAYPhQLSGGMRQ 179
Cdd:PRK13548 75 ARRRA---V-LPQHsslsfPFTVE--------EVVAmgraPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 180 RV------AIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVE 253
Cdd:PRK13548 142 RVqlarvlAQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
....*...
gi 541492527 254 AGQARRVL 261
Cdd:PRK13548 222 DGTPAEVL 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-546 |
1.56e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.22 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRGAPPP--------VGIVFQNPYSALnpa 395
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-----GDLLTEEnvwdirhkIGMVFQNPDNQF--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 rtVGQTLAEALAVG--GQGGA------QVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:PRK13650 95 --VGATVEDDVAFGleNKGIPheemkeRVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 468 DVSVQATIIDLLRRLQAEQGFALAFITHDL-AVArqMSDRIIVMKDGAIVEEGATEALLAAPSH--------PYTASLID 538
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDYQMTVISITHDLdEVA--LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFTTSLVQ 249
|
....*...
gi 541492527 539 AVPGRGAP 546
Cdd:PRK13650 250 SLRQNGYD 257
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
319-519 |
4.47e-30 |
|
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: 117.21 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAgVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGT-----VHVARAPGAGRgappPVGIVFQ--NPYSA 391
Cdd:cd03298 10 YGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingVDVTAAPPADR----PVSMLFQenNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 392 LNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:cd03298 85 LTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 472 QATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
298-518 |
6.28e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.22 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 298 ERPIVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----------H 366
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTD---VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklsS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 VARAPGAGRgappPVGIVFQnpYSALNPARTVGQTLAEALAVGGQGGAQVP----DLLGAVGLpAAHAQRLPAALSGGQR 442
Cdd:PRK11629 79 AAKAELRNQ----KLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINsralEMLAAVGL-EHRANHRPSELSGGER 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 443 QRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSdRIIVMKDGAIVEE 518
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAE 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
324-513 |
1.16e-29 |
|
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: 116.41 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV----ARAPGAGRGapppvgIVFQNpYSALnPARTVG 399
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILegkqITEPGPDRM------VVFQN-YSLL-PWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAeaLAVG--------GQGGAQVPDLLGAVGLPAAhAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:TIGR01184 73 ENIA--LAVDrvlpdlskSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 541492527 472 QATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
316-524 |
1.25e-29 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 116.32 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA-----RAPGAGRGApppVGIVFQnpYS 390
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvREPREVRRR---IGIVFQ--DL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLPAAhAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAErrerIDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 467 LDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
268-532 |
1.51e-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: 122.57 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 268 YARQLLDAQLRLDG--PSPRPAGAVPATTVADERPIVALRDVVkeFRsggRRAEGHLALAGVSLDILPGQSVGIVGESGS 345
Cdd:COG4987 298 HLGRVRAAARRLNEllDAPPAVTEPAEPAPAPGGPSLELEDVS--FR---YPGAGRPVLDGLSLTLPPGERVAIVGPSGS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 346 GKTTLARITVGLEAPDSGTVHV------ARAPGAGRGApppVGIVFQNPY--SAlnpartvgqTLAEALAVGGQGG--AQ 415
Cdd:COG4987 373 GKSTLLALLLRFLDPQSGSITLggvdlrDLDEDDLRRR---IAVVPQRPHlfDT---------TLRENLRLARPDAtdEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 416 VPDLLGAVGLpAAHAQRLP-----------AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQA 484
Cdd:COG4987 441 LWAALERVGL-GDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 541492527 485 EQgfALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAAPSHPY 532
Cdd:COG4987 520 GR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
320-513 |
1.82e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.72 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPpvGIVFQNpySALNPARTVG 399
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--GVVFQN--EGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGGQGGAQ----VPDLLGAVGLPAAHaQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATI 475
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQrleiAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 541492527 476 IDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
322-528 |
2.21e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.43 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVAR---APGAGRGAPPP----VGIVFQNPYSALnp 394
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKNKKLKPlrkkVGIVFQFPEHQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 artVGQTLAEALAVGGQG-GAQVPD-------LLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK13634 99 ---FEETVEKDICFGPMNfGVSEEDakqkareMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 467 LDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
42-257 |
2.28e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.53 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtidlgvaadSLRRLRGGGIvwlpq 121
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERP---TSGQVLVNGQ---------DLSRLKRREI----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 dpftslsPLHR--CGV-----QVIAHR------------QG-PRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRV 181
Cdd:COG2884 75 -------PYLRrrIGVvfqdfRLLPDRtvyenvalplrvTGkSRKEIRRRVREVLDLVGLSDKA-KALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 182 AIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQA 257
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
316-531 |
2.34e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.61 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARA----------------PGAGRGAPP 379
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 380 PVGIVFQ--NPYSALNPARTVGQTLAEALAVGGQGGAQVPDL-LGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPE 456
Cdd:PRK10619 93 RLTMVFQhfNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 457 LLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHP 531
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
44-251 |
2.52e-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: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdlgvaADSLRRlrgggIVWLPQ-- 121
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP---TSGSIRVFGKPL-----EKERKR-----IGYVPQrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 --DP--------FTSLSPLHRCGVQviahrQGPRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAP 191
Cdd:cd03235 78 siDRdfpisvrdVVLMGLYGHKGLF-----RRLSKADKAKVDEALERVGLSELADRQI-GELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
45-275 |
5.61e-29 |
|
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: 115.09 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGRTIdLGVAADSLRRLRGGGIvwlpQDp 123
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEP----TSGEIFIDGEDI-REQDPVELRRKIGYVI----QQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 fTSLSPlHRCGVQVIAH----RQGPRSERAERALARLAEVGL-PARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:cd03295 84 -IGLFP-HMTVEENIALvpklLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDA 275
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
322-519 |
8.57e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.09 E-value: 8.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------------ARAPgagrgapppVGIVFQNPY 389
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskenlkeIRKK---------IGIIFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 SALnpartVGQTLAEALAVG--------GQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICD 461
Cdd:PRK13632 94 NQF-----IGATVEDDIAFGlenkkvppKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 462 EAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEG 519
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
302-535 |
1.06e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.13 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSggrraegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAGRG 376
Cdd:PRK11432 7 VVLKNITKRFGS-------NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgeDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 apppVGIVFQNpYsALNPARTVGQTLAEALAVGGQGGA----QVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALA 452
Cdd:PRK11432 80 ----ICMVFQS-Y-ALFPHMSLGENVGYGLKMLGVPKEerkqRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPY 532
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
...
gi 541492527 533 TAS 535
Cdd:PRK11432 233 MAS 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
302-515 |
1.24e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 113.27 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrrAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG-RGAPPP 380
Cdd:cd03292 1 IEFINVTKTY------PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 -----VGIVFQNpySALNPARTVGQTLAEALAVGGQGG----AQVPDLLGAVGLpaAHAQR-LPAALSGGQRQRVAIARA 450
Cdd:cd03292 75 ylrrkIGVVFQD--FRLLPDRNVYENVAFALEVTGVPPreirKRVPAALELVGL--SHKHRaLPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
50-201 |
2.90e-28 |
|
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: 110.04 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVaadslRRLRGGGIVWLPQDPFtsLSP 129
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDDE-----RKSLRKEIGYVFQDPQ--LFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 130 LHRC------GVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:pfam00005 73 RLTVrenlrlGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
46-273 |
3.73e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.49 E-value: 3.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDLGVAADSLRRLRGGgIVWLPQDPFT 125
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE---ITSGDLIVDGLKVNDPKVDERLIRQEAG-MVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDV 205
Cdd:PRK09493 91 HLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHH-YPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 206 TTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:PRK09493 170 ELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
311-525 |
3.95e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.90 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 311 FRSGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapGAGRGAPPPV------GIV 384
Cdd:COG4559 9 VRLGGRTL-----LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN---GRPLAAWSPWelarrrAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 385 FQnpYSALNPARTVGQTLAEALAVGGQGGAQVPDL----LGAVGLpAAHAQRLPAALSGGQRQRVAIARALA-------A 453
Cdd:COG4559 81 PQ--HSSLAFPFTVEEVVALGRAPHGSSAAQDRQIvreaLALVGL-AHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
319-526 |
4.05e-28 |
|
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: 112.32 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG------RGApppVGIVFQNPYsal 392
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrkslRSM---IGVVLQDTF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 nparTVGQTLAEALAVGGQGgAQVPDLLGAVGLPAAH--AQRLP-----------AALSGGQRQRVAIARALAARPELLI 459
Cdd:cd03254 88 ----LFSGTIMENIRLGRPN-ATDEEVIEAAKEAGAHdfIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 460 CDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
49-273 |
6.22e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 112.33 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 49 ADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGR---TIDLGVAADSLRR--LRGG-GIVWlpQ 121
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAP----DAGEVHYRMRdgqLRDLYALSEAERRrlLRTEwGFVH--Q 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSLsplhRCGVQV---IAHR---QGPRSERAERALAR--LAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:PRK11701 97 HPRDGL----RMQVSAggnIGERlmaVGARHYGDIRATAGdwLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYArQLL 273
Cdd:PRK11701 173 VFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYT-QLL 251
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
301-519 |
6.84e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRRAEgHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------------- 367
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTE-KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsdeenlwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 368 --ARApgagrgapppvGIVFQNPYSALnpartVGQTLAEALAVGGQG--------GAQVPDLLGAVGLPA--AHAqrlPA 435
Cdd:PRK13633 83 irNKA-----------GMVFQNPDNQI-----VATIVEEDVAFGPENlgippeeiRERVDESLKKVGMYEyrRHA---PH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 436 ALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAI 515
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
....
gi 541492527 516 VEEG 519
Cdd:PRK13633 223 VMEG 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
43-275 |
8.53e-28 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 113.74 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPI--VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSgtvelAGR----TID-LGVAADSLRRLRGGG 115
Cdd:PRK15093 16 SDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVT-----ADRmrfdDIDlLRLSPRERRKLVGHN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 116 IVWLPQDPFTSLSPLHRCGVQVIAHRQGPRSE---------RAERALARLAEVGL--PARAARAYPHQLSGGMRQRVAIA 184
Cdd:PRK15093 91 VSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKgrwwqrfgwRKRRAIELLHRVGIkdHKDAMRSFPYELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 185 AALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
250
....*....|.
gi 541492527 265 ATDYARQLLDA 275
Cdd:PRK15093 251 HHPYTQALIRA 261
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
317-528 |
1.26e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 117.36 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG---RGAPPPVGIVFQN----PY 389
Cdd:TIGR03797 462 RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldvQAVRRQLGVVLQNgrlmSG 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 SAL-NPARTVGQTLAEALAVggqggAQVpdllgaVGLpAAHAQRLP-----------AALSGGQRQRVAIARALAARPEL 457
Cdd:TIGR03797 542 SIFeNIAGGAPLTLDEAWEA-----ARM------AGL-AEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRI 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAEQgfalAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:TIGR03797 610 LLFDEATSALDNRTQAIVSESLERLKVTR----IVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
302-537 |
1.36e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.97 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraeGHLALA-GVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARA-----PGAGR 375
Cdd:PRK11000 4 VTLRNVTKAY--------GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GapppVGIVFQNpYsALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVG--LPAAHA-QRLPAALSGGQRQRVAIARALA 452
Cdd:PRK11000 76 G----VGMVFQS-Y-ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAevLQLAHLlDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 453 ARPELLICDEAVSALD----VSVQATIIDLLRRLQAeqgfALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
....*....
gi 541492527 529 SHPYTASLI 537
Cdd:PRK11000 226 ANRFVAGFI 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
51-274 |
1.86e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.00 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTID----LGVAADSLRRLRGG-GIVWLPQDPFT 125
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLL---EQPEAGTIRVGDITIDtarsLSQQKGLIRQLRQHvGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLPARAArAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDV 205
Cdd:PRK11264 99 HRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET-SYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 206 TTQKEILTLLASLRDARgMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLD 274
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
324-526 |
3.00e-27 |
|
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: 116.38 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVaraPGAGRGAPPP------VGIVFQNpysALNPART 397
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLV---DGVDLAIADPawlrrqMGVVLQE---NVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 VGQTLAEalavgGQGGAQVPDLLGAVGLPAAHA--QRLP-----------AALSGGQRQRVAIARALAARPELLICDEAV 464
Cdd:TIGR01846 547 IRDNIAL-----CNPGAPFEHVIHAAKLAGAHDfiSELPqgyntevgekgANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 465 SALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:TIGR01846 622 SALDYESEALIMRNMREIC--RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
50-265 |
3.25e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGRTIDLGVAADSLRRLRGG-GIVWlpQDPFTSL 127
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQP----TSGTVTIGERVITAGKKNKKLKPLRKKvGIVF--QFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 -----------SPLHrCGVqviahrqgPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:PRK13634 99 feetvekdicfGPMN-FGV--------SEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
317-546 |
5.46e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG---------RGAPPpvgivfQn 387
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaelarrRAVLP------Q- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 388 pYSALNPARTVGQTLAEALAVGGQGGAQVPDL----LGAVGLpAAHAQRLPAALSGGQRQRVAIARALA------ARPEL 457
Cdd:PRK13548 84 -HSSLSFPFTVEEVVAMGRAPHGLSRAEDDALvaaaLAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLaapshpyTASLI 537
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-------TPETL 234
|
250
....*....|....*....
gi 541492527 538 DAV----------PGRGAP 546
Cdd:PRK13548 235 RRVygadvlvqphPETGAP 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
302-527 |
6.20e-27 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.86 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVkeFRSGGrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPP-- 379
Cdd:cd03251 1 VEFKNVT--FRYPG---DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 380 -PVGIVFQNPYsalnparTVGQTLAEALAVGGQGGAQvPDLLGAVGLPAAHA--QRLP-----------AALSGGQRQRV 445
Cdd:cd03251 76 rQIGLVSQDVF-------LFNDTVAENIAYGRPGATR-EEVEEAARAANAHEfiMELPegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQ-GFALAfitHDLAVARQmSDRIIVMKDGAIVEEGATEAL 524
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRtTFVIA---HRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
...
gi 541492527 525 LAA 527
Cdd:cd03251 224 LAQ 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-518 |
8.48e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 113.73 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPSDPDRPIVA--DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRrlR 112
Cdd:PRK09700 6 ISMAGIGKSFGPVHAlkSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNINYNKLDHKLAAQ--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 113 GGGIVWLPQDPFTSLSPLHR-----------CGVQVIAHRqgprsERAERALARLAEVGLpARAARAYPHQLSGGMRQRV 181
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENlyigrhltkkvCGVNIIDWR-----EMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 182 AIAAALDAAPGVLIADEPTTALdvtTQKEILTLLASLRDAR--GMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARR 259
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 260 VlarPATDYARQLLDAQLRLDGPSPRpagavPATTVADERPIVALRDVVKefRSGGRraeghlaLAGVSLDILPGQSVGI 339
Cdd:PRK09700 232 V---SNDDIVRLMVGRELQNRFNAMK-----ENVSNLAHETVFEVRNVTS--RDRKK-------VRDISFSVCRGEILGF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 340 VGESGSGKTTLARITVGLEAPDSGTVHVarapgAGRGAPPpvgivfQNPYSALN----------------PARTVGQTLA 403
Cdd:PRK09700 295 AGLVGSGRTELMNCLFGVDKRAGGEIRL-----NGKDISP------RSPLDAVKkgmayitesrrdngffPNFSIAQNMA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 404 --EALAVGGQGgaqvpdllGAVGL-------PAAHAQRLPAA------------LSGGQRQRVAIARALAARPELLICDE 462
Cdd:PRK09700 364 isRSLKDGGYK--------GAMGLfhevdeqRTAENQRELLAlkchsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDE 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 463 AVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEE 518
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
48-271 |
1.36e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 111.73 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLRgggivwlpqdpftsl 127
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEP---TAGEVLIDGEDI-TKLSKKELRELR--------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 spLHRCG-V-QVIA---HR------------QG-PRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDA 189
Cdd:COG4175 104 --RKKMSmVfQHFAllpHRtvlenvafgleiQGvPKAERRERAREALELVGLAGWEDS-YPDELSGGMQQRVGLARALAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 190 APGVLIADEPTTALD----VTTQKEILTLLASLRdaRGMalVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:COG4175 181 DPDILLMDEAFSALDplirREMQDELLELQAKLK--KTI--VFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPA 256
|
....*.
gi 541492527 266 TDYARQ 271
Cdd:COG4175 257 NDYVAD 262
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-255 |
1.47e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPS----DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSLRR 110
Cdd:PRK13635 6 IRVEHISfrypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE---AGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 111 LrggGIVWlpQDP---FTSLS-------PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQR 180
Cdd:PRK13635 83 V---GMVF--QNPdnqFVGATvqddvafGLENIGV--------PREEMVERVDQALRQVGMEDFLNRE-PHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 181 VAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDyGDDIVVMRGGAIVEAG 255
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
43-304 |
2.16e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 110.28 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVA--DVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGRTIdLGVAADSLRRLRGG-GIVW 118
Cdd:PRK11153 14 GGRTIHAlnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRP----TSGRVLVDGQDL-TALSEKELRKARRQiGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 119 lpQDpFTSLS----------PLHRCGVqviahrqgPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALD 188
Cdd:PRK11153 89 --QH-FNLLSsrtvfdnvalPLELAGT--------PKAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 189 AAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDY 268
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 541492527 269 ARQLLDAQLRLDGPSPRPAGAVPaTTVADERPIVAL 304
Cdd:PRK11153 237 TREFIQSTLHLDLPEDYLARLQA-EPTTGSGPLLRL 271
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
324-526 |
2.38e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGA---PPPVGIVFQNPYSALnpartVGQ 400
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlRRKIGMVFQNPDNQF-----VGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 401 TLAEALAVGGQGGA--------QVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQ 472
Cdd:PRK13642 98 TVEDDVAFGMENQGipreemikRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 473 ATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
320-537 |
3.08e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.43 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTL-------------ARITvgleapdsGTVHVARAPGAGRGAPPP-----V 381
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrmndlipgARVE--------GEILLDGEDIYDPDVDVVelrrrV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 GIVFQNPysalNP------------ARTVG----QTLAEAlavggqggaqVPDLLGAVGLPAAHAQRL--PA-ALSGGQR 442
Cdd:COG1117 95 GMVFQKP----NPfpksiydnvaygLRLHGikskSELDEI----------VEESLRKAALWDEVKDRLkkSAlGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 443 QRVAIARALAARPELLICDEAVSALD-VSVqATIIDLLRRLQAEqgFALAFITHDLAVARQMSDRIIVMKDGAIVEEGAT 521
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPT 237
|
250
....*....|....*.
gi 541492527 522 EALLAAPSHPYTASLI 537
Cdd:COG1117 238 EQIFTNPKDKRTEDYI 253
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
43-249 |
5.46e-26 |
|
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: 103.86 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLrgggivwlpqd 122
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP---TSGEILIDGKDIAKLPLEELRRRI----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 pftslsplhrcgvqviahrqgprseraeralarlaevglparaarAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd00267 76 ---------------------------------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 541492527 203 LDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:cd00267 111 LDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
44-249 |
6.13e-26 |
|
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: 104.58 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLRGGGIVwlpQDP 123
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP---DSGSILIDGEDLTDLEDELPPLRRRIGMVF---QDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftslsplhrcgvQVIAHrqgprseraeraLARLAEVGLParaarayphqLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:cd03229 86 ------------ALFPH------------LTVLENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
44-252 |
6.35e-26 |
|
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: 106.11 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADS-LRRLRGG-GIVW--- 118
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP---TSGSVLIDG--TDINKLKGKaLRQLRRQiGMIFqqf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 119 ----------------LPQDPFtslsplhrcgVQVIAhRQGPRSERaERALARLAEVGLPARA-ARAypHQLSGGMRQRV 181
Cdd:cd03256 88 nlierlsvlenvlsgrLGRRST----------WRSLF-GLFPKEEK-QRALAALERVGLLDKAyQRA--DQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 182 AIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIV 252
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
34-273 |
8.87e-26 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 105.88 E-value: 8.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 34 AIRVANPSD--PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTidlgvAADSLRRL 111
Cdd:cd03296 2 SIEVRNVSKrfGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP---DSGTILFGGED-----ATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 112 RGGGIVWLPQDPFTSLSPLHRCG----VQVIAHRQgPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAAL 187
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAfglrVKPRSERP-PEAEIRAKVHELLKLVQLDWLADR-YPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 188 DAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATD 267
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
....*.
gi 541492527 268 YARQLL 273
Cdd:cd03296 232 FVYSFL 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
321-519 |
1.21e-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: 104.98 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVhvaRAPGAGRGAPPP------VGIVFQNPysalnp 394
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV---LLDGTDIRQLDPadlrrnIGYVPQDV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 aRTVGQTLAEALAVGGQGgAQVPDLLGAVGLPAAH--AQRLP-----------AALSGGQRQRVAIARALAARPELLICD 461
Cdd:cd03245 88 -TLFYGTLRDNITLGAPL-ADDERILRAAELAGVTdfVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 462 EAVSALDVSVQATIIDLLRRLQAEQgfALAFITHDLAVArQMSDRIIVMKDGAIVEEG 519
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
326-530 |
1.22e-25 |
|
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: 111.57 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 326 GVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVhvaRAPGAGRGAPPP------VGIVFQNpysALNPARTVG 399
Cdd:TIGR03796 497 NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI---LFDGIPREEIPRevlansVAMVDQD---IFLFEGTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 Q-------TLAEALAVGGQGGAQVPDLLGAvgLPAAHAQRLP---AALSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:TIGR03796 571 DnltlwdpTIPDADLVRACKDAAIHDVITS--RPGGYDAELAeggANLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 470 SVQATIIDLLRRlqaeQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLAAPSH 530
Cdd:TIGR03796 649 ETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVGGA 704
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-526 |
1.68e-25 |
|
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: 105.00 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-------------ARApgagrgapppVGIVFQNpyS 390
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldslRRA----------IGVVPQD--T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 AL------------NPARTVGQTLAEALAvggqggAQVPDLLgaVGLPAAHAQRLPA---ALSGGQRQRVAIARALAARP 455
Cdd:cd03253 85 VLfndtigynirygRPDATDEEVIEAAKA------AQIHDKI--MRFPDGYDTIVGErglKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 456 ELLICDEAVSALDVSVQATIIDLLRRLQAeqGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
43-277 |
1.75e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.92 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APAQfttsGTVELAGRtiDLGVAADSLRRLRGGGIVWLPQ 121
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQ----GNVSWRGE--PLAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSLSPLHRCGvQVIA----HRQG-PRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:PRK10419 97 DSISAVNPRKTVR-EIIReplrHLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAgQARRVLARPATDYARQLLDAQ 276
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET-QPVGDKLTFSSPAGRVLQNAV 254
|
.
gi 541492527 277 L 277
Cdd:PRK10419 255 L 255
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
50-277 |
2.01e-25 |
|
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: 105.30 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDLGVAADSLRRL---RGGGIVwlPQDPFTS 126
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRlmrTEWGFV--HQNPRDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LsplhRCGVQV---IAHRQ---GPRSERAERALAR--LAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:TIGR02323 99 L----RMRVSAganIGERLmaiGARHYGNIRATAQdwLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQL 277
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSIL 253
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
320-526 |
2.07e-25 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 104.54 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARapgagrgapppVGIVFQNPYSALNPARTVG 399
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG-----------VDIRDLNLRWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 Q-------TLAEALAVGgQGGAQVPDLLGAVGLPAAHA--QRLP-----------AALSGGQRQRVAIARALAARPELLI 459
Cdd:cd03249 84 QepvlfdgTIAENIRYG-KPDATDEEVEEAAKKANIHDfiMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 460 CDEAVSALDVSVQATIIDLLRRlqAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
311-515 |
2.36e-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: 102.68 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 311 FRSGGrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgAGRGAP----PPVGIVFQ 386
Cdd:cd03246 8 FRYPG---AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD-ISQWDPnelgDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 NpysalnpARTVGQTLAEALavggqggaqvpdllgavglpaahaqrlpaaLSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:cd03246 84 D-------DELFSGSIAENI------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 467 LDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMsDRIIVMKDGAI 515
Cdd:cd03246 127 LDVEGERALNQAIAALKA-AGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
51-253 |
2.98e-25 |
|
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: 103.97 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLRRLRGG--GIVW-----LPQdp 123
Cdd:TIGR02211 24 VSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNP---TSGEVLFNGQSLS-KLSSNERAKLRNKklGFIYqfhhlLPD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLS----PLhrcgvqVIAHRQgpRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:TIGR02211 98 FTALEnvamPL------LIGKKS--VKEAKERAYEMLEKVGLEHRINH-RPSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 200 TTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYgDDIVVMRGGAIVE 253
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
44-240 |
3.11e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDLGVAadslrRLRGGGIvwLPQDP 123
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTALPA-----EQRRIGI--LFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 --FTSLSplhrcgvqvIAH-------RQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:COG4136 86 llFPHLS---------VGEnlafalpPTIGRAQRRARVEQALEEAGLAGFADR-DPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYG 240
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
304-513 |
3.80e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 103.35 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSGGRraeghLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgAGRG------- 376
Cdd:cd03263 3 IRNLTKTYKKGTK-----PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI-----NGYSirtdrka 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPPVGIVFQnpYSALNPARTVGQTLA-EALAVG---GQGGAQVPDLLGAVGLPaAHAQRLPAALSGGQRQRVAIARALA 452
Cdd:cd03263 73 ARQSLGYCPQ--FDALFDELTVREHLRfYARLKGlpkSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAfiTHDLAVARQMSDRIIVMKDG 513
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILT--THSMDEAEALCDRIAIMSDG 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
319-520 |
4.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP-----GAGRGAPPPVGIVFQNPYSALN 393
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkKSLLEVRKTVGIVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 394 pARTVGQTLA-EALAVG---GQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:PRK13639 93 -APTVEEDVAfGPLNLGlskEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 470 SVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA 520
Cdd:PRK13639 171 MGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
35-263 |
4.57e-25 |
|
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: 104.43 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPS----DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqFTTSGTVELAG-RTIDlgvaADSLR 109
Cdd:TIGR04520 1 IEVENVSfsypESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLL---LPTSGKVTVDGlDTLD----EENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RLRGG-GIVWlpQDPFTSLsplhrCGVQV---IA----HRQGPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRV 181
Cdd:TIGR04520 74 EIRKKvGMVF--QNPDNQF-----VGATVeddVAfgleNLGVPREEMRKRVDEALKLVGMEDFRDRE-PHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 182 AIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDL---ALArdygDDIVVMRGGAIVEAGQAR 258
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeeaVLA----DRVIVMNKGKIVAEGTPR 221
|
....*
gi 541492527 259 RVLAR 263
Cdd:TIGR04520 222 EIFSQ 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
328-521 |
5.10e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.02 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 328 SLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGrgAPP---PVGIVFQ--NPYSALNPARTVGQTL 402
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPyqrPVSMLFQenNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 403 AEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRL 482
Cdd:TIGR01277 96 HPGLKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 541492527 483 QAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGAT 521
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
301-519 |
5.32e-25 |
|
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: 102.83 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGGRRAeghLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA--RAPGAGRGAP 378
Cdd:cd03266 1 MITADALTKRFRDVKKTV---QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 PPVGIVFQNpySALNPARTVGQTLAEALAVGGQGG----AQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAAR 454
Cdd:cd03266 78 RRLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGdeltARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 455 PELLICDEAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
50-279 |
5.45e-25 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 103.73 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTidlgVAADSLRRlRGGGIVWLPQDPFTSLSP 129
Cdd:TIGR00968 18 DVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL---EQPDSGRIRLNGQD----ATRVHARD-RKIGFVFQHYALFKHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LHRC--GVQVIAHRQGPRSERAERALARLAEVGLPARaaraYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTT 207
Cdd:TIGR00968 90 RDNIafGLEIRKHPKAKIKARVEELLELVQLEGLGDR----YPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 208 QKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRL 279
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
50-264 |
5.73e-25 |
|
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: 104.46 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGRTIDLGVAADsLRRLRgggivwlpqdpftsls 128
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLlKP----TSGTVTIDGRDITAKKKKK-LKDLR---------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 plHRCGV-------QV--------IAHrqGPRS------ERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAAL 187
Cdd:TIGR04521 82 --KKVGLvfqfpehQLfeetvykdIAF--GPKNlglseeEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 188 DAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
44-260 |
7.13e-25 |
|
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: 103.03 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL--APAQFTTSGTVELAGRTI-DLGVAADSLRRLRGggIVWLP 120
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGAPDEGEVLLDGKDIyDLDVDVLELRRRVG--MVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPF-TSLSPLHRCGVQViaHRQGPRSERAERALARLAEVGLPARAA-RAYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:cd03260 90 PNPFpGSIYDNVAYGLRL--HGIKLKEELDERVEEALRKAALWDEVKdRLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 199 PTTALDVTTQKEILTLLASLRDArgMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRV 260
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
304-524 |
7.34e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagRGAPPPVGI 383
Cdd:COG4152 4 LKGLTKRF-------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-------DGEPLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 384 VFQNPY----SALNPARTV-----------GQTLAEALAvggqggaQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVAIA 448
Cdd:COG4152 70 RRRIGYlpeeRGLYPKMKVgeqlvylarlkGLSKAEAKR-------RADEWLERLGLGDRANKKV-EELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 449 RALAARPELLICDEAVSALD-VSVQaTIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpVNVE-LLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
323-519 |
7.46e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.36 E-value: 7.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAG------------RGAPPPVGIVFQNPYS 390
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIaarnrigylpeeRGLYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 alnpARTVGQTLAEALavggqggAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVS 470
Cdd:cd03269 95 ----AQLKGLKKEEAR-------RRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 471 VQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03269 163 NVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-515 |
8.62e-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: 101.35 E-value: 8.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgagrgapppvgIVFQNPYSALNpa 395
Cdd:cd03215 8 RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP-----------VTRRSPRDAIR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 rtvgqtlaealavggQGGAQVPD---LLGAV-GLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:cd03215 75 ---------------AGIAYVPEdrkREGLVlDLSVAENIALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 541492527 472 QATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:cd03215 140 KAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
50-273 |
1.25e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.79 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAAD--SLRRLRGG-GIV------WlP 120
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPR---SGTLNIAGNHFDFSKTPSdkAIRELRRNvGMVfqqynlW-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QdpFTSLSPLHRCGVQVIAHRQGPRSERAERALARLAevgLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:PRK11124 96 H--LTVQQNLIEAPCRVLGLSKDQALARAEKLLERLR---LKPYADR-FPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 201 TALD--VTTQkeILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRvLARPATDYARQLL 273
Cdd:PRK11124 170 AALDpeITAQ--IVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
44-249 |
1.67e-24 |
|
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: 100.16 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRLrgggIVWLPQDP 123
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP---DSGEIKVLG--KDIKKEPEEVKRR----IGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 --FTSLSPLhrcgvQVIahrqgprseraeralarlaevglparaarayphQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:cd03230 83 slYENLTVR-----ENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 202 ALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:cd03230 125 GLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-526 |
1.74e-24 |
|
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: 101.74 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGR---GAPPP------VGIVFQNPysALN 393
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-----GRditGLPPHeraragIGYVPEGR--RIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 394 PARTVGQTLAeaLAVGGQGGAQVPDLLGAV-GL-PAAHAQRLPAA--LSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:cd03224 88 PELTVEENLL--LGAYARRRAKRKARLERVyELfPRLKERRKQLAgtLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 470 SVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:cd03224 166 KIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
44-232 |
1.93e-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: 101.02 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLgvAADSLRRLrgggIVWLPQDP 123
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP---SAGEVLWNGEPIRD--AREDYRRR----LAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 --FTSLSP---LHrcgvqvIAHRQGPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:COG4133 85 glKPELTVrenLR------FWAALYGLRADREAIDEALEAVGLAGLADLP-VRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMAlVLVTHD 232
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
300-522 |
3.19e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsgGrraeGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV------------ 367
Cdd:COG3845 4 PALELRGITKRF---G----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvrirsprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 368 ARAPGagrgapppVGIVFQNPysALNPARTVgqtlAEALAVGGQGG-----------AQVPDLLGAVGL---PAAHAQRL 433
Cdd:COG3845 77 AIALG--------IGMVHQHF--MLVPNLTV----AENIVLGLEPTkggrldrkaarARIRELSERYGLdvdPDAKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 434 PAalsgGQRQRVAIARALAARPELLICDEAVSALdvSVQAT--IIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMK 511
Cdd:COG3845 143 SV----GEQQRVEILKALYRGARILILDEPTAVL--TPQEAdeLFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLR 215
|
250
....*....|.
gi 541492527 512 DGAIVEEGATE 522
Cdd:COG3845 216 RGKVVGTVDTA 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
279-530 |
3.47e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 106.34 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 279 LDGPSPRPAGAVPATTVadeRPIVALRDVVKEFRSGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLE 358
Cdd:TIGR02203 311 LDSPPEKDTGTRAIERA---RGDVEFRNVTFRYPGRDRPA-----LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 359 APDSGTVHVARAPGAG---RGAPPPVGIVFQNpysalnpARTVGQTLAEALAVGGQGGAQVPDLLGAvgLPAAHAQ---- 431
Cdd:TIGR02203 383 EPDSGQILLDGHDLADytlASLRRQVALVSQD-------VVLFNDTIANNIAYGRTEQADRAEIERA--LAAAYAQdfvd 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 432 RLP-----------AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVA 500
Cdd:TIGR02203 454 KLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTI 531
|
250 260 270
....*....|....*....|....*....|
gi 541492527 501 rQMSDRIIVMKDGAIVEEGATEALLAAPSH 530
Cdd:TIGR02203 532 -EKADRIVVMDDGRIVERGTHNELLARNGL 560
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
323-524 |
5.18e-24 |
|
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: 100.68 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapGAGRGAPPP-------VGIVFQNpySALNPA 395
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLD---GEDITKLPPheraragIAYVPQG--REIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 RTVGQTLAEALAVGGQGGAQVPDLLGAVgLPAAHA--QRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQA 473
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSRKIPDEIYEL-FPVLKEmlGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 474 TIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:TIGR03410 169 DIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-263 |
5.24e-24 |
|
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: 105.61 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 1 MDVLEREGRTVTARAERIGTAGSTGtgtgLRARAIRVAnpSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG 80
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPPS----IELEDVSFS--YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 81 LAPAqftTSGTVELAGRTIDlGVAADSLRRLrgggIVWLPQDPftslsplhrcgvqVIAH----------RQGPRSERAE 150
Cdd:COG4988 386 FLPP---YSGSILINGVDLS-DLDPASWRRQ----IAWVPQNP-------------YLFAgtirenlrlgRPDASDEELE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 151 RAL--ARLAEV--GLPA--------RAARayphqLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASL 218
Cdd:COG4988 445 AALeaAGLDEFvaALPDgldtplgeGGRG-----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 541492527 219 rdARGMALVLVTHDLALARDYgDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:COG4988 520 --AKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
41-277 |
5.92e-24 |
|
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: 106.07 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAG---RTIDLgvaaDSLRRLrgggIV 117
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP---TSGRILIDGidlRQIDP----ASLRRQ----IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 WLPQDPFtslspLHRCGVQ--VIAHRQGPRSERAERAlARLAEVglpARAARAYPH-----------QLSGGMRQRVAIA 184
Cdd:COG2274 553 VVLQDVF-----LFSGTIRenITLGDPDATDEEIIEA-ARLAGL---HDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 185 AALDAAPGVLIADEPTTALDVTTQKEILTLLASLrdARGMALVLVTHDLALARDYgDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEELLARK 700
|
250
....*....|...
gi 541492527 265 AtdYARQLLDAQL 277
Cdd:COG2274 701 G--LYAELVQQQL 711
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
44-249 |
6.00e-24 |
|
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: 98.61 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlGVAADSLRRLrgggIVWLPQDP 123
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLR-DLDLESLRKN----IAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 F---TSLsplhrcgvqviahrqgprseraeralarlAEVGLparaarayphqlSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:cd03228 86 FlfsGTI-----------------------------RENIL------------SGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 201 TALDVTTQKEILTLLASLRdaRGMALVLVTHDLALARDYgDDIVVMRGG 249
Cdd:cd03228 125 SALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
301-527 |
7.92e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFR---------------SGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV 365
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 366 HVarapgAGRGAPP-PVGIVFQNPYSA-----LNpARTVGQTLAEALAVggqggaqVPDL-----LG-AVGLPAAHaqrl 433
Cdd:COG1134 84 EV-----NGRVSALlELGAGFHPELTGreniyLN-GRLLGLSRKEIDEK-------FDEIvefaeLGdFIDQPVKT---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 434 paaLSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:COG1134 147 ---YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|....
gi 541492527 514 AIVEEGATEALLAA 527
Cdd:COG1134 223 RLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
319-525 |
9.10e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.97 E-value: 9.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRGAPPP--------VGIVFQNPYS 390
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-----GREVNAEnekwvrskVGLVFQDPDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALNPArtvgqTLAEALAVG----GQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDE 462
Cdd:PRK13647 91 QVFSS-----TVWDDVAFGpvnmGLDKDEverrVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
304-526 |
9.31e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSGgrrAEGHL-ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-------HVARAPGAGR 375
Cdd:PRK13651 5 VKNIVKIFNKK---LPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GAPPP--------------------VGIVFQ-NPYSALNP---------ARTVGQTLAEALAvggqggaQVPDLLGAVGL 425
Cdd:PRK13651 82 KVLEKlviqktrfkkikkikeirrrVGVVFQfAEYQLFEQtiekdiifgPVSMGVSKEEAKK-------RAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 426 PAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSD 505
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTK 233
|
250 260
....*....|....*....|.
gi 541492527 506 RIIVMKDGAIVEEGATEALLA 526
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILS 254
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
63-305 |
9.86e-24 |
|
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: 102.19 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 63 IVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLgVAADslrrLRGGGIVwlpqdpFTS--LSPlHRCGVQVIAH 140
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF---EQPDSGSIMLDGEDVTN-VPPH----LRHINMV------FQSyaLFP-HMTVEENVAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 141 ----RQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLA 216
Cdd:TIGR01187 66 glkmRKVPRAEIKPRVLEALRLVQLEEFADR-KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 217 SLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL--------------DAQLRLDGP 282
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIgeinvfeatvierkSEQVVLAGV 224
|
250 260
....*....|....*....|....
gi 541492527 283 SPRPAGAVPATTVADERPI-VALR 305
Cdd:TIGR01187 225 EGRRCDIYTDVPVEKDQPLhVVLR 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
44-268 |
1.01e-23 |
|
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: 99.62 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIdLGVAADSlrrlRGGGIVWLPQDP 123
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF---ETPTSGEILLDGKDI-TNLPPHK----RPVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLS-------PLHRcgvqviahRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:cd03300 84 FPHLTvfeniafGLRL--------KKLPKAEIKERVAEALDLVQLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDY 268
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
46-266 |
1.10e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDL--GVAADSLRRLRGG-GIV----- 117
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPD---SGQLNIAGHQFDFsqKPSEKAIRLLRQKvGMVfqqyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 -WlPQdpFTSLSPLHRCGVQVIAHRQGPRSERAERALARLaevGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:COG4161 93 lW-PH--LTVMENLIEAPCKVLGLSKEQAREKAMKLLARL---RLTDKADR-FPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQArRVLARPAT 266
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQT 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
321-526 |
1.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSG-------TVHVARAPGAGRGAPPPVGIVFQNPYSAL- 392
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvddiTITHKTKDKYIRPVRKRIGMVFQFPESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 --NPARTV-------GQTLAEAlavggqgGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEA 463
Cdd:PRK13646 100 edTVEREIifgpknfKMNLDEV-------KNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 464 VSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
324-518 |
1.36e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.47 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP-----GAGRGA--PPPVGIVFQN--PYSALNP 394
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdEEARAKlrAKHVGFVFQSfmLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 ARTVGqtlAEALAVG---GQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:PRK10584 106 LENVE---LPALLRGessRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 541492527 472 QATIIDLLRRLQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEE 518
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
302-547 |
1.37e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.23 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrrAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA------RAPgAGR 375
Cdd:PRK11650 4 LKLQAVRKSY------DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGgrvvneLEP-ADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 GapppVGIVFQNpYsALNPARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARAL 451
Cdd:PRK11650 77 D----IAMVFQN-Y-ALYPHMSVRENMAYGLKIRGMPKAEieerVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 452 AARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHP 531
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPAST 229
|
250
....*....|....*.
gi 541492527 532 YTASLIdavpgrGAPA 547
Cdd:PRK11650 230 FVASFI------GSPA 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
322-540 |
1.51e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAG--RGAPPPVGIVFQNpySALNP 394
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvDIAKISDAElrEVRRKKIAMVFQS--FALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 ARTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVS 470
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEErrekALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 471 VQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAV 540
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
47-252 |
1.67e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 98.48 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLGvaadslRRLRGGGIVwlPQDP--- 123
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL---IKESSGSILLNGKPIKAK------ERRKSIGYV--MQDVdyq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLHRCGvqvIAHRQGPRS-ERAERALARLAevglPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03226 84 LFTDSVREELL---LGLKELDAGnEQAETVLKDLD----LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 541492527 203 LDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIV 252
Cdd:cd03226 157 LDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
47-278 |
2.31e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.27 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLGVAAD---------SLRRLRGGGIV 117
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL---EKPSEGSIVVNGQTINLVRDKDgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 WLPQ----DPFTSLSPLHRCGVQVIAHRqgpRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:PRK10619 97 VFQHfnlwSHMTVLENVMEAPIQVLGLS---KQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
....*
gi 541492527 274 DAQLR 278
Cdd:PRK10619 253 KGSLK 257
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
45-252 |
5.47e-23 |
|
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: 97.40 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlGVAADSLRRLRGG-GIVWLPQDP 123
Cdd:TIGR02982 18 KQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQ---EGSLKVLGQELH-GASKKQLVQLRRRiGYIFQAHNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPlhRCGVQVIA--HRQGPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:TIGR02982 94 LGFLTA--RQNVQMALelQPNLSYQEARERARAMLEAVGLGDHL-NYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALArDYGDDIVVMRGGAIV 252
Cdd:TIGR02982 171 ALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRIL-DVADRILQMEDGKLL 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
50-264 |
5.79e-23 |
|
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: 97.79 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLgvaADSLRRlrggGIVWLPQDpfTSLSP 129
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD---SGKILLNGKDITN---LPPEKR----DISYVPQN--YALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 lHRCGVQVIA----HRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDV 205
Cdd:cd03299 85 -HMTVYKNIAyglkKRKVDKKEIERKVLEIAEMLGIDHLLNR-KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 206 TTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
317-510 |
5.91e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.78 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPD---SGTV-----HVARAPGAGRGapppVGIVFQNP 388
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVllngrRLTALPAEQRR----IGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 389 YsaLNPARTVGQTLAEALAVGGQGG---AQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:COG4136 86 L--LFPHLSVGENLAFALPPTIGRAqrrARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 466 ALDVSVQATIIDLLR-RLQAEQGFALaFITHDLAVARQMSdRIIVM 510
Cdd:COG4136 163 KLDAALRAQFREFVFeQIRQRGIPAL-LVTHDEEDAPAAG-RVLDL 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
323-520 |
6.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.93 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA--RAPGAGRGAPP------PVGIVFQNPYSALnp 394
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKIKEvkrlrkEIGLVFQFPEYQL-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 artVGQTLAEALAVG--------GQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK13645 104 ---FQETIEKDIAFGpvnlgenkQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 467 LDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA 520
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
304-516 |
1.80e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSGGrrAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRGAP 378
Cdd:COG1101 4 LKNLSKTFNPGT--VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 ppVGIVFQNPYSALNPARTVGQTLAEALAVGGQGG----------AQVPDLLGAVGLPAAHaqRLPA---ALSGGQRQRV 445
Cdd:COG1101 82 --IGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGlrrgltkkrrELFRELLATLGLGLEN--RLDTkvgLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIV 516
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
46-262 |
2.32e-22 |
|
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: 95.58 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLRRLrggGIVWLPQDP-- 123
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP---RSGSIRFDGRDIT-GLPPHERARA---GIGYVPEGRri 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLHRCGVQVIAHRQGPRSERAERALA---RLAEVglpaRAARAYphQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:cd03224 87 FPELTVEENLLLGAYARRRAKRKARLERVYElfpRLKER----RKQLAG--TLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 201 TALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-274 |
2.53e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSD-PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIDlGVAADS 107
Cdd:COG4525 4 LTVRHVSVRYPGGgQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAP----SSGEITLDGVPVT-GPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 108 lrrlrggGIV--------WLPQDPFTSLsPLHRCGVqviahrqgPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQ 179
Cdd:COG4525 79 -------GVVfqkdallpWLNVLDNVAF-GLRLRGV--------PKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 180 RVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGaiveagqARR 259
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG-------PGR 214
|
250
....*....|....*
gi 541492527 260 VLARPATDYARQLLD 274
Cdd:COG4525 215 IVERLELDFSRRFLA 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
44-263 |
2.68e-22 |
|
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: 96.08 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRLrgggIVWLPQDP 123
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP---DSGSILIDG--EDVRKEPREARRQ----IGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FtslSPLHRCGVQVIAH----RQGPRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:COG4555 84 G---LYDRLTVRENIRYfaelYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 200 TTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:COG4555 160 TNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
47-281 |
2.73e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDlGVAAdslrRLRGGGIVWLPQDPFTS 126
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQTSGHIRFHGTDVS-RLHA----RDRKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LSPLHRC--GVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALD 204
Cdd:PRK10851 89 MTVFDNIafGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 205 VTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLDG 281
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQG 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
57-527 |
2.84e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.08 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 57 PGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSlrRLRGGGIV-----WLPQ-----DPFTS 126
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRD---AGSILYLGKEVTFNGPKSS--QEAGIGIIhqelnLIPQltiaeNIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LSPLHRCGVqvIAHRQgpRSERAERALARLaevGLPaRAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALdvt 206
Cdd:PRK10762 104 REFVNRFGR--IDWKK--MYAEADKLLARL---NLR-FSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 207 TQKEILTLLASLRD--ARGMALVLVTHDLALARDYGDDIVVMR-GGAIVEagqarrvlaRPATDY----------ARQLL 273
Cdd:PRK10762 173 TDTETESLFRVIRElkSQGRGIVYISHRLKEIFEICDDVTVFRdGQFIAE---------REVADLtedsliemmvGRKLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 274 DAQLRLDgpspRPAGAVpattvaderpivalRDVVKEFRSGGrraeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARI 353
Cdd:PRK10762 244 DQYPRLD----KAPGEV--------------RLKVDNLSGPG--------VNDVSFTLRKGEILGVSGLMGAGRTELMKV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 354 TVGLEAPDSGTVH------VARAPGAGRGApppvGIVF-----------------QN-PYSALNPARTVGQTL---AEAL 406
Cdd:PRK10762 298 LYGALPRTSGYVTldghevVTRSPQDGLAN----GIVYisedrkrdglvlgmsvkENmSLTALRYFSRAGGSLkhaDEQQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 407 AVGgqggaqvpDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEq 486
Cdd:PRK10762 374 AVS--------DFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE- 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 541492527 487 GFALAFITHDLAVARQMSDRIIVMKDGAI-----VEEGATEALLAA 527
Cdd:PRK10762 445 GLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMAA 490
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
323-519 |
3.07e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAP-----PPVGIVFQNPYSALnpart 397
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdirKKVGLVFQYPEYQL----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 VGQTLAEALAVG--------GQGGAQVPDLLGAVGLP-AAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:PRK13637 97 FEETIEKDIAFGpinlglseEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 469 VSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
324-527 |
3.39e-22 |
|
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: 100.28 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV--------HVARApgAGRGApppVGIVfqnpysalnPA 395
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirDVTQA--SLRAA---IGIV---------PQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 RTV--GQTLAEALAVGgQGGAQVPDLLGAVGLPAAHA--QRLPAA-----------LSGGQRQRVAIARALAARPELLIC 460
Cdd:COG5265 440 DTVlfNDTIAYNIAYG-RPDASEEEVEAAARAAQIHDfiESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLQAEQGfALAfITHDLA-VARqmSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRT-TLV-IAHRLStIVD--ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
296-525 |
3.87e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.59 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 296 ADERPIVALRDVVKEFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV--ARAPGA 373
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 374 GRGAPPPVGIVFQnpYSALNPARTVGQTLaeaLAVGGQGG-------AQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVA 446
Cdd:PRK13536 109 ARLARARIGVVPQ--FDNLDLEFTVRENL---LVFGRYFGmstreieAVIPSLLEFARLESKADARV-SDLSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 447 IARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
47-260 |
4.11e-22 |
|
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: 95.44 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDlGVAADSLRRLRG--GGIvwlpqdpF 124
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL---VEPSSGSILLEGTDIT-KLRGKKLRKLRRriGMI-------F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLSPLHRCGV--QVIAHRQG------------PRSERaERALARLAEVGLPARAA-RAypHQLSGGMRQRVAIAAALDA 189
Cdd:TIGR02315 86 QHYNLIERLTVleNVLHGRLGykptwrsllgrfSEEDK-ERALSALERVGLADKAYqRA--DQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRV 260
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
42-263 |
4.29e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 95.37 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAIcglapAQF--TTSGTVELAGRTIDlGVAADSLRRLRGggIVwl 119
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-----FRFydVSSGSILIDGQDIR-EVTLDSLRRAIG--VV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQDpftslSPLHRcgvQVIAH-----RQGPRSERAERAlARLAEV-----GLParaaRAYPHQ-------LSGGMRQRVA 182
Cdd:cd03253 81 PQD-----TVLFN---DTIGYnirygRPDATDEEVIEA-AKAAQIhdkimRFP----DGYDTIvgerglkLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 183 IAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARgmALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
.
gi 541492527 263 R 263
Cdd:cd03253 225 K 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
300-514 |
5.33e-22 |
|
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: 94.81 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFR---SGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPG---- 372
Cdd:COG4778 3 TLLEVENLSKTFTlhlQGGKRLP---VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 373 AGrgAPP---------PVGIVFQN----P-YSALN----PARTVGQTLAEALAvggqggaQVPDLLGAVGLPaahaQRL- 433
Cdd:COG4778 80 AQ--ASPreilalrrrTIGYVSQFlrviPrVSALDvvaePLLERGVDREEARA-------RARELLARLNLP----ERLw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 434 ---PAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVM 510
Cdd:COG4778 147 dlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDV 225
|
....
gi 541492527 511 KDGA 514
Cdd:COG4778 226 TPFS 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
47-237 |
5.53e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.88 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGRTID-LGVAADSLRRLRGGGIVW-----L 119
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTP----TSGDVIFNGQPMSkLSSAAKAELRNQKLGFIYqfhhlL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQdpFTSLS----PLhrcgvqVIAHRqgPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:PRK11629 100 PD--FTALEnvamPL------LIGKK--KPAEINSRALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALAR 237
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
50-265 |
6.47e-22 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 97.07 E-value: 6.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRtiDLGVAADSLRrlrggGIVWLPQDpfTSLSP 129
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPD---SGKIYLDGK--DITNLPPEKR-----GIAYVYQN--YMLFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 lHRCGVQVIAH----RQGPRSERAERALaRLAEV-GLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALD 204
Cdd:NF040840 86 -HKTVFENIAFglklRKVPKEEIERKVK-EIMELlGISHLLHR-KPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 205 VTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPK 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-528 |
8.12e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagRGAPPP----------VGIVFQNPYSAL 392
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-------RGEPITkenirevrkfVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 NpARTVGQTLA----------EALAvggqggAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDE 462
Cdd:PRK13652 92 F-SPTVEQDIAfgpinlgldeETVA------HRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
56-255 |
8.13e-22 |
|
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: 93.90 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 56 APGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaaDSLRRL------RGGGIVWLPQDPFTSLSP 129
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKP---DGGTIVLNGTVLF-----DSRKKInlppqqRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LHR--CGVQViaHRQGPRSERAERALARLAEVGLparaARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTT 207
Cdd:cd03297 93 RENlaFGLKR--KRNREDRISVDELLDLLGLDHL----LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 208 QKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
323-528 |
8.14e-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: 94.28 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGR---GAPPPV----GI--------VFQN 387
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-----GEditGLPPHRiarlGIgyvpegrrIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 388 ---------PYSALNPARTVGQTLAEALAVggqggaqVPDLlgavglpAAHAQRLPAALSGGQRQRVAIARALAARPELL 458
Cdd:COG0410 93 ltveenlllGAYARRDRAEVRADLERVYEL-------FPRL-------KERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 459 ICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
43-251 |
8.69e-22 |
|
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: 93.63 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqFTTSGTVELAGRTI-DLGVAADSLRRlRGGGIVWlpQ 121
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE---LPTSGTIRVNGQDVsDLRGRAIPYLR-RKIGVVF--Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DpFTSLSPLHRCGVQVIAHR--QGPRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:cd03292 86 D-FRLLPDRNVYENVAFALEvtGVPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 541492527 200 TTALDVTTQKEILTLLASLrDARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
50-252 |
9.78e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 92.11 E-value: 9.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRlrgggivwlpqdpftslsp 129
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP---DSGEILVDGKEVSFASPRDARRA------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 lhrcGVQVIahrqgprseraeralarlaevglparaaraypHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQK 209
Cdd:cd03216 76 ----GIAMV--------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 541492527 210 EILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIV 252
Cdd:cd03216 120 RLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
43-249 |
9.80e-22 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 93.47 E-value: 9.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DL-GVAADSLRRlrGGGIVWlp 120
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTP---SRGQVRIAGEDVnRLrGRQLPLLRR--RIGVVF-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDpFTSLspLHRCGVQVIA---HRQG-PRSERAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:TIGR02673 86 QD-FRLL--PDRTVYENVAlplEVRGkKEREIQRRVGAALRQVGLEHKA-DAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 541492527 197 DEPTTALDVTTQKEILTLLASLrDARGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
300-516 |
1.40e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGGRRAEghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGA------ 373
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVE---VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldada 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 374 -GRGAPPPVGIVFQNPY--SALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:PRK10535 80 lAQLRREHFGFIFQRYHllSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQmSDRIIVMKDGAIV 516
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
300-525 |
1.44e-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: 94.00 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVkeFRSGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSG-TVHVArapGAGRGAP 378
Cdd:COG1119 2 PLLELRNVT--VRRGGKTI-----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLF---GERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 ------PPVGIVfqnpYSALNPARTVGQTLAEALAVGGQGG------------AQVPDLLGAVGLpAAHAQRLPAALSGG 440
Cdd:COG1119 72 dvwelrKRIGLV----SPALQLRFPRDETVLDVVLSGFFDSiglyreptdeqrERARELLELLGL-AHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 441 QRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA 520
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
....*
gi 541492527 521 TEALL 525
Cdd:COG1119 227 KEEVL 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
297-496 |
1.63e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 297 DERPIVALRDVvkefrsgGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapGAGRG 376
Cdd:PRK10247 3 ENSPLLQLQNV-------GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE---GEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPPVGIVFQNPYSALNPArTVGQTLAEALAVGGQGGAQVPDL------LGAVGLPAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:PRK10247 73 TLKPEIYRQQVSYCAQTPT-LFGDTVYDNLIFPWQIRNQQPDPaiflddLERFALPDTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHD 496
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
324-527 |
1.72e-21 |
|
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: 97.90 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAGRGapPPVGIVFQNPysALNPArtv 398
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSQWDREELG--RHIGYLPQDV--ELFDG--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 gqTLAEALAvgGQGGAQVPDLLGAVGLPAAHA--QRLP-----------AALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:COG4618 421 --TIAENIA--RFGDADPEKVVAAAKLAGVHEmiLRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 466 ALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAA 527
Cdd:COG4618 497 NLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
323-537 |
3.01e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLAR-----------ITV---------GLEAPDSGTVHVARApgagrgapppVG 382
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRsinrmndlnpeVTItgsivynghNIYSPRTDTVDLRKE----------IG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 383 IVFQNPysalNP-ARTVGQTLAEALAVGGQGGAQVPDLLGAVGLPAA----------HAQRLpaALSGGQRQRVAIARAL 451
Cdd:PRK14239 90 MVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGAsiwdevkdrlHDSAL--GLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 452 AARPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHP 531
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
....*.
gi 541492527 532 YTASLI 537
Cdd:PRK14239 242 ETEDYI 247
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
279-481 |
4.83e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 279 LDGPSPRPAGAVPATTVADERpiVALRDV-VkefrsggRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGL 357
Cdd:COG4178 342 LEAADALPEAASRIETSEDGA--LALEDLtL-------RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 358 EAPDSGTVHVarapgagrgaPPPVGIVF--QNPYsaLNPArtvgqTLAEALAVGGQGG----AQVPDLLGAVGLPAaHAQ 431
Cdd:COG4178 413 WPYGSGRIAR----------PAGARVLFlpQRPY--LPLG-----TLREALLYPATAEafsdAELREALEAVGLGH-LAE 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 432 RL------PAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRR 481
Cdd:COG4178 475 RLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
310-527 |
5.06e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 310 EFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA--RAPGAGRGAPPPVGIVFQn 387
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCgePVPSRARHARQRVGVVPQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 388 pYSALNPARTVGQTLaeaLAVG-------GQGGAQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVAIARALAARPELLIC 460
Cdd:PRK13537 88 -FDNLDPDFTVRENL---LVFGryfglsaAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
51-513 |
5.75e-21 |
|
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: 96.05 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfTTSGTVELAGRTIdlgvAADSLRRLRGGGIVWLPQDP--FTSLS 128
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPL----KASNIRDTERAGIVIIHQELtlVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 PLHRCGVQVIAHRQGPRSERAE---RALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALdv 205
Cdd:TIGR02633 95 VAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 206 tTQKEILTLLASLRD--ARGMALVLVTHDLALARDYGDDIVVMRGGAIVeAGQARRVLARPatDYARQLLDAQLRLDGPS 283
Cdd:TIGR02633 173 -TEKETEILLDIIRDlkAHGVACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMSED--DIITMMVGREITSLYPH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 284 -PRPAGAVpattVADERPIVAlRDVVKEFRsggRRAEghlalaGVSLDILPGQSVGIVGESGSGKTTLARITVGL-EAPD 361
Cdd:TIGR02633 249 ePHEIGDV----ILEARNLTC-WDVINPHR---KRVD------DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 362 SGTVHVARAPGAGRGAPPPV--GIVF---QNPYSALNPARTVGQ--TLAEALAVGGQGGAQVPDLLGAVG-------LPA 427
Cdd:TIGR02633 315 EGNVFINGKPVDIRNPAQAIraGIAMvpeDRKRHGIVPILGVGKniTLSVLKSFCFKMRIDAAAELQIIGsaiqrlkVKT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 428 AHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRI 507
Cdd:TIGR02633 395 ASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRV 473
|
....*.
gi 541492527 508 IVMKDG 513
Cdd:TIGR02633 474 LVIGEG 479
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
319-508 |
6.31e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgagrgappPVGIVFQNpySALnpARTV 398
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--------RVAYVPQR--SEV--PDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLAEALAVG------------GQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:NF040873 71 PLTVRDLVAMGrwarrglwrrltRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 541492527 467 LDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRII 508
Cdd:NF040873 150 LDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVL 190
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
48-273 |
7.39e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.71 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADS-LRRLRGGGIVWLPQD---- 122
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDG--VDIAKISDAeLREVRRKKIAMVFQSfalm 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSLSPLHRCGVQVIAHrqgPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGI---NAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 203 LDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
302-519 |
1.06e-20 |
|
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: 90.67 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSGGRRA---------------EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH 366
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 VarapgAGRGAPPP-VGIVFQNPYSALNPARTVGqtlaealAVGGQGGAQVPDLLGAV----GLPAAHAQRLpAALSGGQ 441
Cdd:cd03220 81 V-----RGRVSSLLgLGGGFNPELTGRENIYLNG-------RLLGLSRKEIDEKIDEIiefsELGDFIDLPV-KTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 442 RQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
283-510 |
1.15e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.43 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 283 SPRPAGAVPATTVADERPIVaLRDVvkEFRSGGRRAeghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDS 362
Cdd:TIGR02857 304 APRPLAGKAPVTAAPASSLE-FSGV--SVAYPGRRP----ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 363 GTVHVARAPGAGRGAP---PPVGIVFQNPYsalnparTVGQTLAE--ALAVGGQGGAQVPDLLGAVG-------LPAAHA 430
Cdd:TIGR02857 377 GSIAVNGVPLADADADswrDQIAWVPQHPF-------LFAGTIAEniRLARPDASDAEIREALERAGldefvaaLPQGLD 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 431 QRL---PAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQMsDRI 507
Cdd:TIGR02857 450 TPIgegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALA-DRI 526
|
...
gi 541492527 508 IVM 510
Cdd:TIGR02857 527 VVL 529
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
45-275 |
1.18e-20 |
|
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: 93.52 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTsGTVELAGRtiDLGVAADSLRRLrggGIVWLPQDPF 124
Cdd:TIGR03258 18 NTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLT-GRIAIADR--DLTHAPPHKRGL---ALLFQNYALF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLSPLHRCGVQVIAHRQgPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALD 204
Cdd:TIGR03258 92 PHLKVEDNVAFGLRAQKM-PKADIAERVADALKLVGLGDAAAH-LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 205 VTTQKEILTLLASL-RDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDA 275
Cdd:TIGR03258 170 ANIRANMREEIAALhEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGA 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
302-526 |
1.25e-20 |
|
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: 95.25 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEA--PDSGTV--HVARAPGAGR-- 375
Cdd:TIGR03269 1 IEVKNLTKKF-------DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyHVALCEKCGYve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 376 -----GAPPPV---------------------------GIVFQNPYsALNPARTVGQTLAEALAVGGQGGAQ----VPDL 419
Cdd:TIGR03269 74 rpskvGEPCPVcggtlepeevdfwnlsdklrrrirkriAIMLQRTF-ALYGDDTVLDNVLEALEEIGYEGKEavgrAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 420 LGAVGLP--AAHAQRlpaALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDL 497
Cdd:TIGR03269 153 IEMVQLShrITHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 541492527 498 AVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
322-519 |
1.64e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgagrgapppvgivfqnpysalnpARTVGQT 401
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----------------------VSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 402 LAEALAVGGQGgaqvPDLLGAVGLpaahaQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLrr 481
Cdd:cd03247 73 LSSLISVLNQR----PYLFDTTLR-----NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI-- 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 541492527 482 LQAEQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEG 519
Cdd:cd03247 142 FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-495 |
1.73e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVAraPGAGRGAPPPVGIVFQNPYSALNPARTVG 399
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD--GGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGGQGGAQVPDLLGAVGLpaAHAQRLPAA-LSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDL 478
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAALEAVGL--APLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
170
....*....|....*..
gi 541492527 479 LRRLQAEQGFALAfITH 495
Cdd:PRK13539 170 IRAHLAQGGIVIA-ATH 185
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
302-519 |
1.77e-20 |
|
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: 89.94 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSGgrraeghLALAGVSLDILPGQSvGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRG 376
Cdd:cd03264 1 LQLENLTKRYGKK-------RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdVLKQPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 ApppVGIVFQ--NPYSALnparTVGQTLAEALAVGG----QGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARA 450
Cdd:cd03264 73 R---IGYLPQefGVYPNF----TVREFLDYIAWLKGipskEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAfiTHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILS--THIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
316-526 |
1.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP--GAGRGA---PPPVGIVFQNPYS 390
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidYSRKGLmklRESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALNPARTVGQTLAEALAVG---GQGGAQVPDLLGAVGLpaAHAQRLPA-ALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK13636 94 QLFSASVYQDVSFGAVNLKlpeDEVRKRVDNALKRTGI--EHLKDKPThCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 467 LDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
48-265 |
2.87e-20 |
|
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: 89.80 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdLGVAADSLRRLrggGIVWLPQDP--FT 125
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP---TSGSVLFDGEDI-TGLPPHEIARL---GIGRTFQIPrlFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVIAHRQGP-------RSERAERALAR--LAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:cd03219 89 ELTVLENVMVAAQARTGSGlllararREEREARERAEelLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
301-526 |
3.09e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.69 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFR-----SGGRRAEGHL---------ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH 366
Cdd:COG4586 1 IIEVENLSKTYRvyekePGLKGALKGLfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 VA-------RAPGAGRgapppVGIVFqnpysalnpartvGQ--------TLAEALavggqggaqvpDLLGAV-GLP-AAH 429
Cdd:COG4586 81 VLgyvpfkrRKEFARR-----IGVVF-------------GQrsqlwwdlPAIDSF-----------RLLKAIyRIPdAEY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 430 AQRL---------------PA-ALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFI 493
Cdd:COG4586 132 KKRLdelvelldlgelldtPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLT 211
|
250 260 270
....*....|....*....|....*....|...
gi 541492527 494 THDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:COG4586 212 SHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
43-271 |
3.53e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlGVAADSlrrlrggGIVWlpQD 122
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVE-GPGAER-------GVVF--QN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 ----PFTSLSPLHRCGVQViahRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:PRK11248 79 egllPWRNVQDNVAFGLQL---AGVEKMQRLEIAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGaiveagqARRVLARPATDYARQ 271
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVERLPLNFARR 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
50-281 |
3.55e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.09 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIdlgvaADSLRRlrgggiVWLP--------- 120
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD---SGRIRLGGEVL-----QDSARG------IFLPphrrrigyv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 -QDPftSLSPlHRcGVQ---VIAHRQGPRSERAERaLARLAEV-GLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:COG4148 83 fQEA--RLFP-HL-SVRgnlLYGRKRAPRAERRIS-FDEVVELlGIGHLLDR-RPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLA----LArdygDDIVVMRGGAIVEAGQARRVLARPATDYARQ 271
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDevarLA----DHVVLLEQGRVVASGPLAEVLSRPDLLPLAG 232
|
250
....*....|
gi 541492527 272 LLDAQLRLDG 281
Cdd:COG4148 233 GEEAGSVLEA 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-542 |
3.56e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.54 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGA---------PPPVGIVFQ--NP 388
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIfnyrdvlefRRRVGMLFQrpNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 389 YSALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLPAAHAQRL---PAALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 466 ALDVSVQATIIDLLRRLQAEqgFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLIDAVPG 542
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
286-526 |
3.78e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.87 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 286 PAGAVPATTVADErpiVALRDVvkEFRSGGRRAeghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV 365
Cdd:PRK13657 322 PPGAIDLGRVKGA---VEFDDV--SFSYDNSRQ----GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 366 H--------VARApgAGRGApppVGIVFQNpysALNPARTVgqtlAEALAVGgQGGAQVPDLLGAVGLPAAHA--QRLPA 435
Cdd:PRK13657 393 LidgtdirtVTRA--SLRRN---IAVVFQD---AGLFNRSI----EDNIRVG-RPDATDEEMRAAAERAQAHDfiERKPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 436 -----------ALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQmS 504
Cdd:PRK13657 460 gydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-A 536
|
250 260
....*....|....*....|..
gi 541492527 505 DRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK13657 537 DRILVFDNGRVVESGSFDELVA 558
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
304-519 |
4.58e-20 |
|
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: 87.99 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSGGRRAeghlALAGVSLDILPGQSVGIVGESGSGKTTLARITVGL--EAPDSGTVHVARAPGAGRGAPPPV 381
Cdd:cd03213 9 LTVTVKSSPSKSGKQ----LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 GIVFQNPYsaLNPARTVGQTLAEALAVGGqggaqvpdllgavglpaahaqrlpaaLSGGQRQRVAIARALAARPELLICD 461
Cdd:cd03213 85 GYVPQDDI--LHPTLTVRETLMFAAKLRG--------------------------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 462 EAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVAR-QMSDRIIVMKDGAIVEEG 519
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
48-262 |
4.92e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLRGG-GIVWlpQDPFTS 126
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP---TTGTVTVDDITITHKTKDKYIRPVRKRiGMVF--QFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LsplhrcgVQVIAHRQ---GPRS------ERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:PRK13646 98 L-------FEDTVEREiifGPKNfkmnldEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
43-507 |
6.73e-20 |
|
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: 93.08 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL----------AP-------AQ-------FTTSGTVELAgrt 98
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngearpQPgikvgylPQepqldptKTVRENVEEG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 99 idLGVAADSLRRLRGggiVWL----PQDPFTSLsplhrcgvqviAHRQGPRSERAERA----LARLAEVGlpARAARAYP 170
Cdd:TIGR03719 93 --VAEIKDALDRFNE---ISAkyaePDADFDKL-----------AAEQAELQEIIDAAdawdLDSQLEIA--MDALRCPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 171 -----HQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTqkeILTLLASLRDARGmALVLVTHDlalaRDYGDDIV- 244
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPG-TVVAVTHD----RYFLDNVAg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 245 ----VMRGGAI---------VEAGQAR------------RVLARP--------------------------ATDYARQLL 273
Cdd:TIGR03719 227 wileLDRGRGIpwegnysswLEQKQKRleqeekeesarqKTLKRElewvrqspkgrqakskarlaryeellSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 274 DAQLRLDgPSPRPAGAVpattvaderpiVALRDVVKEFrsGGRraeghLALAGVSLDILPGQSVGIVGESGSGKTTLARI 353
Cdd:TIGR03719 307 TAEIYIP-PGPRLGDKV-----------IEAENLTKAF--GDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 354 TVGLEAPDSGTVHVarapgagrGAPPPVGIVFQNpYSALNPARTVGQTLAEALAVGGQGGAQVPD--LLGAVGLPAAHAQ 431
Cdd:TIGR03719 368 ITGQEQPDSGTIEI--------GETVKLAYVDQS-RDALDPNKTVWEEISGGLDIIKLGKREIPSraYVGRFNFKGSDQQ 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 432 RLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVsvqatiiDLLRRL-QAEQGFA-LAF-ITHDlavaRQMSDRI 507
Cdd:TIGR03719 439 KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV-------ETLRALeEALLNFAgCAVvISHD----RWFLDRI 506
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
44-295 |
7.49e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.90 E-value: 7.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DLGVAAdslrrlRGGGIVwlPQD 122
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP---TSGEILIGGRDVtDLPPKD------RNIAMV--FQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 ----PFTS-----LSPLHRCGVqviahrqgPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:COG3839 84 yalyPHMTvyeniAFPLKLRKV--------PKAEIDRRVREAAELLGLEDLLDR-KPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 194 LIADEPTTALD----VTTQKEILTLLASLrdarGMALVLVTHD----LALArdygDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:COG3839 155 FLLDEPLSNLDaklrVEMRAEIKRLHRRL----GTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEELYDRPA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 541492527 266 TDY-AR------------QLLDAQLRLDG---PSPRPAGAVPATTV 295
Cdd:COG3839 227 NLFvAGfigsppmnllpgTVEGGGVRLGGvrlPLPAALAAAAGGEV 272
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
324-527 |
8.03e-20 |
|
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: 92.80 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVhvaRAPGAG------RGAPPPVGIVFQNpySALNPArt 397
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV---RLDGADlkqwdrETFGKHIGYLPQD--VELFPG-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 vgqTLAEALAVGGQGgAQVPDLLGAVGLPAAHA--QRLP-----------AALSGGQRQRVAIARALAARPELLICDEAV 464
Cdd:TIGR01842 407 ---TVAENIARFGEN-ADPEKIIEAAKLAGVHEliLRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 465 SALDVSVQATIIDLLRRLQAEQGFALaFITHDLAVArQMSDRIIVMKDGAIVEEGATEALLAA 527
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVV-VITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
48-255 |
1.43e-19 |
|
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: 87.43 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRlrggGIVWLPQDPFTSL 127
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP---TSGRATVAG--HDVVREPREVRR----RIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGVQVIAHRQG-PRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVT 206
Cdd:cd03265 87 ELTGWENLYIHARLYGvPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 207 TQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
45-252 |
1.57e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQD-- 122
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA---DSGEIRLDGKPVRIRSPRDAIRA----GIAYVPEDrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 ------PFT-----SLSPLHRCGvqviahRQGPRSERAERALAR--LAEVGLPARAARAYPHQLSGGMRQRVAIAAALDA 189
Cdd:COG1129 338 geglvlDLSireniTLASLDRLS------RGGLLDRRRERALAEeyIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDL----ALArdygDDIVVMRGGAIV 252
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELpellGLS----DRILVMREGRIV 473
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
48-261 |
1.62e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.97 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttsGTVELAGRTIDlGVAADSLRRLRGggivWLPQDpfTSL 127
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ----GEILLNGRPLS-DWSAAELARHRA----YLSQQ--QSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGvQVIA-HRQ-GPRSERAERALARLAE-VGLPARAARAYpHQLSGGMRQRVAIAA-------ALDAAPGVLIAD 197
Cdd:COG4138 81 PFAMPVF-QYLAlHQPaGASSEAVEQLLAQLAEaLGLEDKLSRPL-TQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
323-500 |
1.94e-19 |
|
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: 86.64 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPPVGIVFQNPYSALNPARTVGQTL 402
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 403 AEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRL 482
Cdd:TIGR01189 95 HFWAAIHGGAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|....*...
gi 541492527 483 QAEQGFALAFITHDLAVA 500
Cdd:TIGR01189 174 LARGGIVLLTTHQDLGLV 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
324-528 |
1.99e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.09 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagRGAPPP----------VGIVFQNPysaLN 393
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-------DGVPLVqydhhylhrqVALVGQEP---VL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 394 PARTVGQTLA---------EALAVGGQGGAQvpDLLGavGLPAAHAQRLPAA---LSGGQRQRVAIARALAARPELLICD 461
Cdd:TIGR00958 567 FSGSVRENIAygltdtpdeEIMAAAKAANAH--DFIM--EFPNGYDTEVGEKgsqLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 462 EAVSALDVSVQATIIDLLRRlqaeQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:TIGR00958 643 EATSALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-237 |
2.06e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 14 RAERIGTAGSTGTGTGLRARAIRVANPSDpdRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVe 93
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY---GSGRI- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 94 lagrtidlgvaadslRRLRGGGIVWLPQDPFTSLSPLHrcgvQVIAHRQGPRSERAERALARLAEVGLPARAAR-----A 168
Cdd:COG4178 421 ---------------ARPAGARVLFLPQRPYLPLGTLR----EALLYPATAEAFSDAELREALEAVGLGHLAERldeeaD 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 169 YPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLasLRDARGMALVLVTHDLALAR 237
Cdd:COG4178 482 WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAA 548
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
323-519 |
3.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA----RAPGAGRGAPP---PVGIVFQNPYS----- 390
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtliTSTSKNKDIKQirkKVGLVFQFPESqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ------ALNPAR-TVGQTLAEALAVggqggaqvpDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEA 463
Cdd:PRK13649 102 tvlkdvAFGPQNfGVSQEEAEALAR---------EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 464 VSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
320-528 |
3.81e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.78 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAgVSLDiLPGQSV-GIVGESGSGKTTLARITVGLEAPDSGTV----HVARAPGAGRGAPPP---VGIVFQNpySA 391
Cdd:PRK11144 11 GDLCLT-VNLT-LPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIvlngRVLFDAEKGICLPPEkrrIGYVFQD--AR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 392 LNPARTVGQTLAEALAvgGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:PRK11144 87 LFPHYKVRGNLRYGMA--KSMVAQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 472 QATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
172-509 |
3.82e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 91.02 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 172 QLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVttqKEILTLLASLRD-ARGMALVLVTHDLALArDY-GDDIVVMRGg 249
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI---RQRLNVARLIRElAEGKYVLVVEHDLAVL-DYlADNVHIAYG- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 250 aivEAGqARRVLARPATdyAR----QLLDAQLRLDGPSPRPAGAV----PATTVADERPIVALRDVVKEfrsggrraegh 321
Cdd:PRK13409 287 ---EPG-AYGVVSKPKG--VRvginEYLKGYLPEENMRIRPEPIEfeerPPRDESERETLVEYPDLTKK----------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 laLAGVSLDILPGQS-----VGIVGESGSGKTTLARITVGLEAPDSGTVHvarapgagrgapPPVGIVFQNPYSALNPAR 396
Cdd:PRK13409 350 --LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------PELKISYKPQYIKPDYDG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 TVGQTLAEAlaVGGQGGAQV-PDLLGAVGLPAAHAQRLPAaLSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATI 475
Cdd:PRK13409 416 TVEDLLRSI--TDDLGSSYYkSEIIKPLQLERLLDKNVKD-LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
330 340 350
....*....|....*....|....*....|....
gi 541492527 476 IDLLRRLQAEQGFALAFITHDLAVARQMSDRIIV 509
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
50-281 |
3.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLRGG-GIVWlpQDPFTSLs 128
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP---SSGTITIAGYHITPETGNKNLKKLRKKvSLVF--QFPEAQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 pLHRCGVQVIAHrqGPRS------ERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK13641 99 -FENTVLKDVEF--GPKNfgfsedEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 203 LDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRV-----------LARPATD-YAR 270
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIfsdkewlkkhyLDEPATSrFAS 254
|
250
....*....|.
gi 541492527 271 QLLDAQLRLDG 281
Cdd:PRK13641 255 KLEKGGFKFSE 265
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
46-265 |
3.86e-19 |
|
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: 86.57 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSLRRLrggGIVWLPQDP-- 123
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP---RSGSIRFDGEDIT-GLPPHRIARL---GIGYVPEGRri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLH--RCGVQVIAHRQGPRsERAERALA---RLAEVglpaRAARAypHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:COG0410 90 FPSLTVEEnlLLGAYARRDRAEVR-ADLERVYElfpRLKER----RRQRA--GTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 199 PTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-255 |
3.90e-19 |
|
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: 86.15 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADslrrlRGGGIVWlpQD 122
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEP---TSGRIYIGGRDVTDLPPKD-----RDIAMVF--QN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 pfTSLSPlHRCGVQVIAH----RQGPRSERAERAL--ARLAEVG-LPARaaraYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:cd03301 81 --YALYP-HMTVYDNIAFglklRKVPKDEIDERVRevAELLQIEhLLDR----KPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
324-525 |
4.31e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGA--------------PPPVGIVFQ--- 386
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlarrlallpqhhLTPEGITVRelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 ----NPYSAL------NPARTVGQTLAEAlavggqggaQVPDLlgavglpaahAQRLPAALSGGQRQRVAIARALAARPE 456
Cdd:PRK11231 98 aygrSPWLSLwgrlsaEDNARVNQAMEQT---------RINHL----------ADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 457 LLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA-----TEALL 525
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmTPGLL 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
44-280 |
5.17e-19 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 87.83 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRLRGggIVwlPQDP 123
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRP---TSGTARVAG--YDVVREPRKVRRSIG--IV--PQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLHRCGVQVIAHRQG-PRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGlPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 203 LDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLD 280
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLK 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
293-524 |
5.28e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 293 TTVADERPIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPG 372
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQY-------SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 373 AGrgAPP----PVGI--VFQNPYsaLNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGL---PAAHAQRLPAAlsggQRQ 443
Cdd:PRK15439 76 AR--LTPakahQLGIylVPQEPL--LFPNLSVKENILFGLPKRQASMQKMKQLLAALGCqldLDSSAGSLEVA----DRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 444 RVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEA 523
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
.
gi 541492527 524 L 524
Cdd:PRK15439 227 L 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
327-542 |
5.83e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 327 VSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARApgAGRGAPPPVGIVFQNpysalnpARTVGQT 401
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgeHIQHY--ASKEVARRIGLLAQN-------ATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 402 LAEALAVGGQGGAQ-------------VPDLLGAVGLPAAHAQRLPAaLSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:PRK10253 97 TVQELVARGRYPHQplftrwrkedeeaVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 469 VSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGateallaAPSHPYTASLIDAVPG 542
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERIYG 242
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
51-279 |
7.35e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIDLgvAADSLRRLRGG-GIVWlpQDPFTSL- 127
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKP----TSGEVLIKGEPIKY--DKKSLLEVRKTvGIVF--QNPDDQLf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 SPLHRCGVQVIAHRQG-PRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVT 206
Cdd:PRK13639 93 APTVEEDVAFGPLNLGlSKEEVEKRVKEALKAVGMEGFENKP-PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 207 TQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATdyarqLLDAQLRL 279
Cdd:PRK13639 172 GASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET-----IRKANLRL 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
300-528 |
1.03e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHvarapgagRGAPP 379
Cdd:PRK09544 3 SLVSLENVSVSF--GQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 380 PVGIVFQNPYsaLNParTVGQTLAEALAVggQGGAQVPDLLGAVG-LPAAHAQRLP-AALSGGQRQRVAIARALAARPEL 457
Cdd:PRK09544 68 RIGYVPQKLY--LDT--TLPLTVNRFLRL--RPGTKKEDILPALKrVQAGHLIDAPmQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMkDGAIVEEGATEALLAAP 528
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
42-255 |
1.05e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAG---RTIDLgvaaDSLRRLrgggIVW 118
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP---TSGRILIDGvdiRDLTL----ESLRRQ----IGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 119 LPQDPFtsLspLH-------RCGvqviahRQGPRSERAERAlARLAEV-----GLPA--------RAARayphqLSGGMR 178
Cdd:COG1132 419 VPQDTF--L--FSgtireniRYG------RPDATDEEVEEA-AKAAQAhefieALPDgydtvvgeRGVN-----LSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 179 QRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdaRGMALVLVTHDLALARDYgDDIVVMRGGAIVEAG 255
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQG 556
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
44-263 |
1.10e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 89.42 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaaDSLRRLRGGGIVWLPQDP 123
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP---TAGSVRLDGADLS-----QWDREELGRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftSLSPlhrcG--VQVIAHRQGPRSERAERAlARLAEV-----GLParaaRAY-------PHQLSGGMRQRVAIAAALDA 189
Cdd:COG4618 416 --ELFD----GtiAENIARFGDADPEKVVAA-AKLAGVhemilRLP----DGYdtrigegGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARdYGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
321-526 |
1.50e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.92 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----------------HVArapgagrgapppvgI 383
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghdlrdytlaslrnQVA--------------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 384 VFQNPYsalnparTVGQTLAEALAVGGQGGAQVPDLLGAVglPAAHA----QRLP-----------AALSGGQRQRVAIA 448
Cdd:PRK11176 422 VSQNVH-------LFNDTIANNIAYARTEQYSREQIEEAA--RMAYAmdfiNKMDngldtvigengVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 449 RALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQgfALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
30-252 |
1.74e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPS-DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSL 108
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKP---TSGTYRVAGQDVA-TLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 109 RRLRGG--GIVWLPQDPFTSLSPLHRcgVQVIAHRQG-PRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAA 185
Cdd:PRK10535 81 AQLRREhfGFIFQRYHLLSHLTAAQN--VEVPAVYAGlERKQRLLRAQELLQRLGLEDRVEY-QPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 186 ALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDyGDDIVVMRGGAIV 252
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
48-251 |
1.81e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 83.25 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQDpftsl 127
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP---ASGEITLDGKPVTRRSPRDAIRA----GIAYVPED----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 splhrcgvqviahrqgprseRAERALArlaeVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTT 207
Cdd:cd03215 84 --------------------RKREGLV----LDLSVAENIALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 541492527 208 QKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:cd03215 140 KAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
324-528 |
2.20e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVAR---APGAGRGA----PPPVGIVFQNPYSALnpar 396
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETGNKNlkklRKKVSLVFQFPEAQL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 tVGQTLAEALAVG--------GQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:PRK13641 99 -FENTVLKDVEFGpknfgfseDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 469 VSVQATIIDLLRRLQAEqGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-513 |
2.24e-18 |
|
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: 81.73 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHvarapgagRGAPPPVGIVFQnpysalnpartv 398
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT--------WGSTVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 gqtlaealavggqggaqvpdllgavglpaahaqrlpaaLSGGQRQRVAIARALAARPELLICDEAVSALDV-SVQAtiid 477
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA---- 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 541492527 478 LLRRLQAEQGfALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:cd03221 109 LEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
44-261 |
2.54e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIdlgvAADSLRRLrGGGIVWLPQDP 123
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ---SGTVFLGDKPI----SMLSSRQL-ARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftsLSPLhrcGVQV---IAHRQGP-----------RSERAERALARLAEVGLPARAARAyphqLSGGMRQRVAIAAALDA 189
Cdd:PRK11231 86 ---LTPE---GITVrelVAYGRSPwlslwgrlsaeDNARVNQAMEQTRINHLADRRLTD----LSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
50-264 |
2.91e-18 |
|
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: 84.05 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaADSLRRLrgggIVWLPQDPFTSLSP 129
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP---TSGGVILEGKQIT----EPGPDRM----VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LHRCGVQV-IAHRQGPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQ 208
Cdd:TIGR01184 72 RENIALAVdRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 209 KEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRV-LARP 264
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
41-249 |
3.40e-18 |
|
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: 83.32 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdlgvAADSLRRLRGGGIVwlP 120
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRP---TSGTAYINGYSI----RTDRKAARQSLGYC--P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDP--FTSLSPL-HrcgVQVIAHRQG-PRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:cd03263 82 QFDalFDELTVReH---LRFYARLKGlPKSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDARgmALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-273 |
3.51e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.65 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVdaAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtiDLGVAADSLRrlrggGIVWLPQD 122
Cdd:COG3840 12 GDFPLRFDLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPP---DSGRILWNGQ--DLTALPPAER-----PVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 P--FTSLSPLHRCGvqvIAHRQGPRSERAERALAR--LAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:COG3840 80 NnlFPHLTVAQNIG---LGLRPGLKLTAEQRAQVEqaLERVGLAGLLDR-LPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLL 273
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
44-265 |
3.57e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.54 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADSlrrlRGGGIVwlpqdp 123
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETP---DSGRIMLDGQDIT-HVPAEN----RHVNTV------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTS--LSPlHRCGVQVIAH----RQGPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:PRK09452 92 FQSyaLFP-HMTVFENVAFglrmQKTPAAEITPRVMEALRMVQLEEFAQRK-PHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
304-518 |
4.02e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.47 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSGGRRAEGHLaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLE--APDSGTVHVarapgagrgappPV 381
Cdd:COG2401 27 VAIVLEAFGVELRVVERYV-LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV------------PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 382 GIVFQNpysalnpartvgQTLAEALAVGGQGGAQVpDLLGAVGLPAAHA-QRLPAALSGGQRQRVAIARALAARPELLIC 460
Cdd:COG2401 94 NQFGRE------------ASLIDAIGRKGDFKDAV-ELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKD-GAIVEE 518
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGyGGVPEE 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
47-236 |
4.05e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DLGVAADSLRRLRGGGIVWLPQDPFT 125
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDG---SSGEVSLVGQPLhQMDEEARAKLRAKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHrcGVQVIAHRQGPRSERA-ERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALD 204
Cdd:PRK10584 102 TLNALE--NVELPALLRGESSRQSrNGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|..
gi 541492527 205 VTTQKEILTLLASLRDARGMALVLVTHDLALA 236
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
49-535 |
4.08e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 49 ADVSVDAAPGRTLVIVGESGAGKSMLARAICGlapAQFTTSGTVELAGRTIDLGVAADSLrrlrGGGIV----------- 117
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSG---NYQPDAGSILIDGQEMRFASTTAAL----AAGVAiiyqelhlvpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 -------WLPQDPftslsplHRCGVQviahrqgPRSERAERALARLAEVGL---PARAARayphQLSGGMRQRVAIAAAL 187
Cdd:PRK11288 94 mtvaenlYLGQLP-------HKGGIV-------NRRLLNYEAREQLEHLGVdidPDTPLK----YLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 188 DAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVE-----AGQARRVLA 262
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAITVFKDGRYVAtfddmAQVDRDQLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 263 rpATDYARQLLDaqlrLDGPSPRPAGAVpattvaderpivalRDVVKEFRSGGRRAeghlalaGVSLDILPGQSVGIVGE 342
Cdd:PRK11288 235 --QAMVGREIGD----IYGYRPRPLGEV--------------RLRLDGLKGPGLRE-------PISFSVRAGEIVGLFGL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 343 SGSGKTTLARITVGLEAPDSGTVHVarapgagRGAPppvgIVFQNPYSALN----------------PARTVGQTL---- 402
Cdd:PRK11288 288 VGAGRSELMKLLYGATRRTAGQVYL-------DGKP----IDIRSPRDAIRagimlcpedrkaegiiPVHSVADNInisa 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 403 ------AEALAVGGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATII 476
Cdd:PRK11288 357 rrhhlrAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIY 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 477 DLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEE----GATEAL---LAAPSHPYTAS 535
Cdd:PRK11288 437 NVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGElareQATERQalsLALPRTSAAVA 501
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
63-255 |
4.95e-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: 82.63 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 63 IVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtiDLGVAADSLRRLRGggivWLPQDP-----FTSLSPL-HRCGVQ 136
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPP---SSGTIRIDGQ--DVLKQPQKLRRRIG----YLPQEFgvypnFTVREFLdYIAWLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 137 VIAHRQGPrsERAERALARlaeVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLA 216
Cdd:cd03264 101 GIPSKEVK--ARVDEVLEL---VNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLS 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 541492527 217 SLrdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03264 175 EL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
319-495 |
5.08e-18 |
|
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: 81.43 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagrgaPPPVGIVF--QNPYsaLNPAr 396
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----------PEGEDLLFlpQRPY--LPLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 tvgqTLAEALAvggqggaqvpdllgavglpaahaqrLP--AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQAT 474
Cdd:cd03223 79 ----TLREQLI-------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 541492527 475 IIDLLRrlqaEQGFALAFITH 495
Cdd:cd03223 130 LYQLLK----ELGITVISVGH 146
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
311-513 |
5.84e-18 |
|
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: 82.52 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 311 FRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagrgaPPPVGIVFQNPY- 389
Cdd:cd03250 8 FTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV----------PGSIAYVSQEPWi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 ------------SALNPARtvgqtLAEALAVGgqggAQVPDLlgavglpaahaQRLPA-----------ALSGGQRQRVA 446
Cdd:cd03250 78 qngtirenilfgKPFDEER-----YEKVIKAC----ALEPDL-----------EILPDgdlteigekgiNLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 447 IARALAARPELLICDEAVSALDVSVQATIID--LLRRLQAEQGFALafITHDLAVARQmSDRIIVMKDG 513
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRIL--VTHQLQLLPH-ADQIVVLDNG 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
279-497 |
7.06e-18 |
|
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: 86.65 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 279 LDGPSPRPAGAVP-ATTVADERPIVALRDVvkefrsGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGL 357
Cdd:TIGR02868 311 LDAAGPVAEGSAPaAGAVGLGKPTLELRDL------SAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 358 EAPDSGTVHVARAPGAGRGAPPPVGIVFQNPYSALNPARTVGQTLaeALAVGGQGGAQVPDLLGAVGLpAAHAQRLP--- 434
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL--RLARPDATDEELWAALERVGL-ADWLRALPdgl 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 435 --------AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLrrLQAEQGFALAFITHDL 497
Cdd:TIGR02868 462 dtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-533 |
7.48e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.42 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGL-----EAPDSGTVH--------------------VARAPGagrgaP 378
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYldgqdifkmdvielrrrvqmVFQIPN-----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 PPVGIVFQNPYSALNPARTVG------QTLAEALAvGGQGGAQVPDLLGAvglPAAhaqrlpaALSGGQRQRVAIARALA 452
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLVKskkelqERVRWALE-KAQLWDEVKDRLDA---PAG-------KLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRLQAEqgFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPY 532
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
.
gi 541492527 533 T 533
Cdd:PRK14247 241 T 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
320-522 |
7.71e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARApgAGRGAP---PPVGIVFQNPYSA 391
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRL--KNREVPflrRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 392 LNpaRTVGQTLAEALAVGGQGGA----QVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:PRK10908 92 MD--RTVYDNVAIPLIIAGASGDdirrRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 468 DVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATE 522
Cdd:PRK10908 169 DDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
304-528 |
9.27e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 82.59 E-value: 9.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFRSggrraegHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV----------HVARAPGA 373
Cdd:cd03218 3 AENLSKRYGK-------RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 374 GRGAPPPVGIVFQNpysalnpaRTVGQTLAEALAVGGQGGAQ----VPDLLGAVGLpaAH-AQRLPAALSGGQRQRVAIA 448
Cdd:cd03218 76 GIGYLPQEASIFRK--------LTVEENILAVLEIRGLSKKEreekLEELLEEFHI--THlRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 449 RALAARPELLICDEAVSALD-VSVQaTIIDLLRRLqAEQGFALaFIT-HDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKIL-KDRGIGV-LITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
..
gi 541492527 527 AP 528
Cdd:cd03218 223 NE 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
30-251 |
9.41e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVAnPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaaDSLR 109
Cdd:cd03246 1 LEVENVSFR-YPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP---TSGRVRLDGADIS-----QWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RLRGGGIVWLPQDpftslsplhrcgVQVIAhrqgprseraeralARLAEvglparaaraypHQLSGGMRQRVAIAAALDA 189
Cdd:cd03246 72 NELGDHVGYLPQD------------DELFS--------------GSIAE------------NILSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDyGDDIVVMRGGAI 251
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
305-528 |
9.45e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 9.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 305 RDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-------------ARAp 371
Cdd:COG1137 7 ENLVKSY--GKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdgedithlpmhkrARL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 372 gagrgapppvGI--------------VFQNPYSALnpaRTVGQTLAEALAvggqggaQVPDLLGAVGLpaAHAQRLPA-A 436
Cdd:COG1137 79 ----------GIgylpqeasifrkltVEDNILAVL---ELRKLSKKEREE-------RLEELLEEFGI--THLRKSKAyS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 437 LSGGQRQRVAIARALAARPELLICDEAVSALD-VSVqATIIDLLRRLqAEQGFALaFIT-HD----LAVArqmsDRIIVM 510
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHL-KERGIGV-LITdHNvretLGIC----DRAYII 209
|
250
....*....|....*...
gi 541492527 511 KDGAIVEEGATEALLAAP 528
Cdd:COG1137 210 SEGKVLAEGTPEEILNNP 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
42-263 |
1.01e-17 |
|
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: 86.41 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAIcglapaqF----TTSGTVELAGRTIDlGVAADSLRRLRGggIV 117
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL-------FrfydVTSGRILIDGQDIR-DVTQASLRAAIG--IV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 wlPQDPftslsplhrcgvqV---------IAH-RQGPRSERAERAlARLAEV-----GLParaaRAYPHQ-------LSG 175
Cdd:COG5265 438 --PQDT-------------VlfndtiaynIAYgRPDASEEEVEAA-ARAAQIhdfieSLP----DGYDTRvgerglkLSG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLrdARGMALVLVTHDLALARDyGDDIVVMRGGAIVEAG 255
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
....*...
gi 541492527 256 QARRVLAR 263
Cdd:COG5265 575 THAELLAQ 582
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-246 |
1.08e-17 |
|
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: 86.19 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 10 TVTARAERIGTAGSTGTGTGLRARAIRVANPSDPDR-PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftT 88
Cdd:TIGR02857 299 AVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP---T 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 89 SGTVELAGRTIDlGVAADSLRRlrggGIVWLPQDPFTSLSPLhrcgVQVIAHRQGPRSERAERALARLAEVGLPARAARA 168
Cdd:TIGR02857 376 EGSIAVNGVPLA-DADADSWRD----QIAWVPQHPFLFAGTI----AENIRLARPDASDAEIREALERAGLDEFVAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 169 Y--------PHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLrdARGMALVLVTHDLALARDYg 240
Cdd:TIGR02857 447 GldtpigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALA- 523
|
....*.
gi 541492527 241 DDIVVM 246
Cdd:TIGR02857 524 DRIVVL 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
317-528 |
1.12e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPPVGIVFQNPySALNPAR 396
Cdd:PRK10575 20 RVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP-QQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 tvGQTLAEALAVG--------GQGGA----QVPDLLGAVGL-PAAHaqRLPAALSGGQRQRVAIARALAARPELLICDEA 463
Cdd:PRK10575 99 --GMTVRELVAIGrypwhgalGRFGAadreKVEEAISLVGLkPLAH--RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 464 VSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
47-255 |
1.15e-17 |
|
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: 81.56 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRtidlGVAADSLRRlrgggIVWLPQDpfT 125
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILP----DSGEVLFDGK----PLDIAARNR-----IGYLPEE--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVI--AHRQG-PRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03269 80 GLYPKMKVIDQLVylAQLKGlKKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 541492527 203 LDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
323-519 |
1.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA----RAPGAGRGAPP---PVGIVFQNPYSALnpa 395
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvSSTSKQKEIKPvrkKVGVVFQFPESQL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 rtVGQTLAEALAVGGQ--------GGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:PRK13643 98 --FEETVLKDVAFGPQnfgipkekAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 541492527 468 DVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:PRK13643 176 DPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
301-524 |
1.49e-17 |
|
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: 85.65 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGL--EAPDSGTVHVARAPGAGRGA- 377
Cdd:TIGR02633 1 LLEMKGIVKTF-------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 378 -PPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGGA--------QVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIA 448
Cdd:TIGR02633 74 dTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRmaynamylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 449 RALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
42-255 |
1.57e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.55 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDlgvAADSLRRlrgggIVWLPQ 121
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRK---PDQFQKC-----VAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 D-------------PFTSLSPLHRCgvqviaHRQGPRSERAEraLARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALD 188
Cdd:cd03234 89 DdillpgltvretlTYTAILRLPRK------SSDAIRKKRVE--DVLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 189 AAPGVLIADEPTTALDVTTQKEILTLLASLrdARGMALVLVT-H----DLAlarDYGDDIVVMRGGAIVEAG 255
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQL--ARRNRIVILTiHqprsDLF---RLFDRILLLSSGEIVYSG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
320-525 |
1.96e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgagrgapppvgivfqnpysALNPARTVG 399
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD----------------------GLDVATTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGGQGGAQ-----VPDLLGAVGLPaaHAQ-RLPAA------------------------LSGGQRQRVAIAR 449
Cdd:COG4604 71 RELAKRLAILRQENHInsrltVRELVAFGRFP--YSKgRLTAEdreiideaiayldledladryldeLSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 450 ALAARPELLICDEAVSALDV--SVQatIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMkhSVQ--MMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
42-264 |
2.00e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.54 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDLGVAADSLRRLrggGIVWlpQ 121
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKV---GIVF--Q 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSLsplhrCGVQV-------IAHRQGPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:PRK13640 92 NPDNQF-----VGATVgddvafgLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALArDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
324-529 |
2.70e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPP---VGIVFQNPYSALN-PARTV- 398
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAsrrVASVPQDTSLSFEfDVRQVv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 --GQT--LAEALAVGGQGGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQAT 474
Cdd:PRK09536 99 emGRTphRSRFDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 475 IIDLLRRLQAEQGFALAFItHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPS 529
Cdd:PRK09536 178 TLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
44-236 |
3.06e-17 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 80.35 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDL--GVAADSLRRLRgggIVWLPQ 121
Cdd:TIGR03608 10 DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEK---FDSGQVYLNGQETPPlnSKKASKFRREK---LGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DpF------TSLSPLHrcgvQVIAHRQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:TIGR03608 84 N-FalieneTVEENLD----LGLKYKKLSKKEKREKKKEALEKVGLNLKLKQ-KIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALA 236
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVTHDPEVA 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
42-263 |
3.26e-17 |
|
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: 80.73 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 42 DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIdLGVAADSLRRLRGggIVwlPQ 121
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDI-RDISRKSLRSMIG--VV--LQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPF---TSLSPLHRCGvqviahRQGPRSERAERALARLAEVGLPARAARAYPHQ-------LSGGMRQRVAIAAALDAAP 191
Cdd:cd03254 85 DTFlfsGTIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDARgmALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-543 |
3.30e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLAR-----------------ITVG---LEAPDSGTVHVARApgagrgappp 380
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkVTFHgknLYAPDVDPVEVRRR---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 381 VGIVFQNPysalNP-ARTVGQTLAEALAVGGQGGA----------------QVPDLLGAVGLpaahaqrlpaALSGGQRQ 443
Cdd:PRK14243 93 IGMVFQKP----NPfPKSIYDNIAYGARINGYKGDmdelverslrqaalwdEVKDKLKQSGL----------SLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 444 RVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQMSDRIIVM---------KDGA 514
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGY 236
|
250 260
....*....|....*....|....*....
gi 541492527 515 IVEEGATEALLAAPSHPYTAsliDAVPGR 543
Cdd:PRK14243 237 LVEFDRTEKIFNSPQQQATR---DYVSGR 262
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
323-519 |
4.50e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.45 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA-RAPGAGR-GAPPPVGIVFqnpysalnpartvGQ 400
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAgLVPWKRRkKFLRRIGVVF-------------GQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 401 --TLAEALAVggqggAQVPDLLGAV-GLPAAHAQR----------------LPA-ALSGGQRQRVAIARALAARPELLIC 460
Cdd:cd03267 103 ktQLWWDLPV-----IDSFYLLAAIyDLPPARFKKrldelselldleelldTPVrQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
30-261 |
4.67e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.19 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPS----DPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlgvaA 105
Cdd:PRK13632 3 NKSVMIKVENVSfsypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---SGEIKIDGITIS----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 106 DSLRRLRGG-GIVWlpQDP---FTslsplhrcGVQV---IA----HRQGPRSERAERALARLAEVGLPARAARAyPHQLS 174
Cdd:PRK13632 76 ENLKEIRKKiGIIF--QNPdnqFI--------GATVeddIAfgleNKKVPPKKMKDIIDDLAKKVGMEDYLDKE-PQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 175 GGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDL--ALARDYgddIVVMRGGAIV 252
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdeAILADK---VIVFSEGKLI 221
|
....*....
gi 541492527 253 EAGQARRVL 261
Cdd:PRK13632 222 AQGKPKEIL 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-542 |
4.95e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLAR-----ITVGLEAPDSGTVHVArapgaGRGAPPP----------VGIVFQ-- 386
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLF-----GRNIYSPdvdpievrreVGMVFQyp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 NPYsalnPARTVGQTLAEALAVGG--QGGAQVPDL----LGAVGLPAAHAQRL---PAALSGGQRQRVAIARALAARPEL 457
Cdd:PRK14267 95 NPF----PHLTIYDNVAIGVKLNGlvKSKKELDERvewaLKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 458 LICDEAVSALDVSVQATIIDLLRRLQAEqgFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLI 537
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
....*
gi 541492527 538 DAVPG 542
Cdd:PRK14267 249 TGALG 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
321-524 |
6.00e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGL----EAPDS------GTVHVA-RAPGAGRGAPPPVGIVFQNpY 389
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGShiellgRTVQREgRLARDIRKSRANTGYIFQQ-F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 SALNPARTVGQTLAEALA-----------VGGQGGAQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVAIARALAARPELL 458
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGstpfwrtcfswFTREQKQRALQALTRVGMVHFAHQRV-STLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 459 ICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-264 |
6.68e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 57 PGRTLV-IVGESGAGKSMLARAICGLAP--AQFTTSGTVELAGRTIdlGVAADSLRRLRGGGIVWLPQDPFtSLSPLHRC 133
Cdd:PRK14271 45 PARAVTsLMGPTGSGKTTFLRTLNRMNDkvSGYRYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF-PMSIMDNV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 134 GVQVIAHRQGPRSERAERALARLAEVGL----PARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQK 209
Cdd:PRK14271 122 LAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDS-PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 210 EILTLLASLRDArgMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:PRK14271 201 KIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
172-509 |
6.69e-17 |
|
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: 83.68 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 172 QLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVttqKEILTLLASLRDA--RGMALVLVTHDLALArDY-GDDIVVMRG 248
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI---YQRLNVARLIRELaeEGKYVLVVEHDLAIL-DYlADYVHILYG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 249 --GA--IVeaGQARRVlaRPATDyarQLLDAQLRLDGPSPRPAGAV----PATTVADERPIVALRDVVKEFrsggrraeg 320
Cdd:COG1245 288 epGVygVV--SKPKSV--RVGIN---QYLDGYLPEENVRIRDEPIEfevhAPRREKEEETLVEYPDLTKSY--------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 hlalAGVSLDILPGQ-----SVGIVGESGSGKTTLARITVGLEAPDSGTVhvarapgagrgaPPPVGIVFQNPYSALNPA 395
Cdd:COG1245 352 ----GGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------DEDLKISYKPQYISPDYD 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 RTVGQTLAEALAVGGQGGAQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATI 475
Cdd:COG1245 416 GTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNV-KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
330 340 350
....*....|....*....|....*....|....
gi 541492527 476 IDLLRRLQAEQGFALAFITHDLAVARQMSDRIIV 509
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
44-264 |
7.74e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDLGVAADSLRRlrgggIVWLPQDP 123
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT---PTAGTVLVAGDDVEALSARAASRR-----VASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLHRCGVQVIAH----RQGPRSERAERALAR-LAEVGLPARAARAYPhQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:PRK09536 87 SLSFEFDVRQVVEMGRTphrsRFDTWTETDRAAVERaMERTGVAQFADRPVT-SLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 199 PTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
46-250 |
1.17e-16 |
|
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: 79.40 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG--LApaqftTSGTVEL--AGRTIDLGVAADS-LRRLRGGGIVWLP 120
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLP-----DSGSILVrhDGGWVDLAQASPReILALRRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QdpFtsLSPLHRCG-VQVIA----HRQGPRSE---RAERALARLaevGLPARAARAYPHQLSGGMRQRVAIAAALDAAPG 192
Cdd:COG4778 100 Q--F--LRVIPRVSaLDVVAepllERGVDREEaraRARELLARL---NLPERLWDLPPATFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 193 VLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGA 250
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
41-282 |
1.23e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSLRRLrggGIVWlp 120
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQIIIDGDLLTEENVWDIRHKI---GMVF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLsplhrCGVQV---IA---HRQG-PRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:PRK13650 88 QNPDNQF-----VGATVeddVAfglENKGiPHEEMKERVNEALELVGMQDFKERE-PARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDL---ALArdygDDIVVMRGGAIVEAGQARRVLARpatdyAR 270
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLdevALS----DRVLVMKNGQVESTSTPRELFSR-----GN 232
|
250
....*....|..
gi 541492527 271 QLLdaQLRLDGP 282
Cdd:PRK13650 233 DLL--QLGLDIP 242
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
50-260 |
1.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLGVAADSLRRLRGG-GIVWlpQDPFTSLs 128
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL---HVPTQGSVRVDDTLITSTSKNKDIKQIRKKvGLVF--QFPESQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 pLHRCGVQVIAHrqGPRS-----ERAER-ALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK13649 99 -FEETVLKDVAF--GPQNfgvsqEEAEAlAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 203 LDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRV 260
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
44-255 |
1.70e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 78.41 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRLrgGGIVWLPqdp 123
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKP---DSGEITFDG--KSYQKNIEALRRI--GALIEAP--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftSLSPlHRCGVQ---VIAHRQGPRSERAERALArlaEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:cd03268 82 --GFYP-NLTAREnlrLLARLLGIRKKRIDEVLD---VVGLKDSAKKKV-KGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 201 TALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03268 155 NGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
319-500 |
1.70e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH-----VARAPGAGRGAPPPVGivfqnPYSALN 393
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepIRRQRDEYHQDLLYLG-----HQPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 394 PARTVGQTLAEALAVGG-QGGAQVPDLLGAVGLpaAHAQRLPAA-LSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:PRK13538 87 TELTALENLRFYQRLHGpGDDEALWEALAQVGL--AGFEDVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180 190
....*....|....*....|....*....|
gi 541492527 472 QATIIDLLRRlQAEQGFALAFITH-DLAVA 500
Cdd:PRK13538 165 VARLEALLAQ-HAEQGGMVILTTHqDLPVA 193
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
316-515 |
1.82e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.67 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagRGAPPP----------VGIVF 385
Cdd:cd03248 22 PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-------DGKPISqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 386 QNPYsalnparTVGQTLAEALAVGGQggaQVPDLLGAVGLPAAHA----QRLP-----------AALSGGQRQRVAIARA 450
Cdd:cd03248 95 QEPV-------LFARSLQDNIAYGLQ---SCSFECVKEAAQKAHAhsfiSELAsgydtevgekgSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 451 LAARPELLICDEAVSALDVSVQATIIDLLRrlQAEQGFALAFITHDLAVARQmSDRIIVMKDGAI 515
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
50-260 |
2.06e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlgvaADSLRRLRGG-GIVWL-PQDPFTsl 127
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK---SGEIFYNNQAIT----DDNFEKLRKHiGIVFQnPDNQFV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 128 splhrcGVQV-------IAHRQGPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:PRK13648 98 ------GSIVkydvafgLENHAVPYDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 201 TALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRV 260
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
37-260 |
2.45e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 37 VANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqFTTSGTVELAG-RTIDLGVAADSLRRlrgGG 115
Cdd:PRK13633 15 ESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL---IPSEGKVYVDGlDTSDEENLWDIRNK---AG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 116 IVWlpQDPFTSLsplhrcgVQVIAHRQ---GPRS---------ERAERALARlaeVGLpARAARAYPHQLSGGMRQRVAI 183
Cdd:PRK13633 89 MVF--QNPDNQI-------VATIVEEDvafGPENlgippeeirERVDESLKK---VGM-YEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRV 260
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
50-527 |
2.88e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfTTSGTVELAGRTIdlgvAADSLRRLRGGGIVWLPQD----PFT 125
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG-TYEGEIIFEGEEL----QASNIRDTERAGIAIIHQElalvKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SL-------SPLHRCGV----QVIAhrqgprseRAERALARLA---EVGLPARaarayphQLSGGMRQRVAIAAALDAAP 191
Cdd:PRK13549 98 SVleniflgNEITPGGImdydAMYL--------RAQKLLAQLKldiNPATPVG-------NLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 192 GVLIADEPTTALdvtTQKEILTLLASLRD--ARGMALVLVTHDLALARDYGDDIVVMRGGaiveagqaRRVLARPAT--- 266
Cdd:PRK13549 163 RLLILDEPTASL---TESETAVLLDIIRDlkAHGIACIYISHKLNEVKAISDTICVIRDG--------RHIGTRPAAgmt 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 267 --DYARQLLDAQLRLDGPS-PRPAGAVpattVADERPIVALrDVVKEFRsggRRAEGhlalagVSLDILPGQSVGIVGES 343
Cdd:PRK13549 232 edDIITMMVGRELTALYPRePHTIGEV----ILEVRNLTAW-DPVNPHI---KRVDD------VSFSLRRGEILGIAGLV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 344 GSGKTTLARITVGL-EAPDSGTVHVarapgagRGAPppvgIVFQNPYSALN----------------PARTVGQ--TLA- 403
Cdd:PRK13549 298 GAGRTELVQCLFGAyPGRWEGEIFI-------DGKP----VKIRNPQQAIAqgiamvpedrkrdgivPVMGVGKniTLAa 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 404 -EALAVGGQ--GGAQVPDLLGAVG---LPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIID 477
Cdd:PRK13549 367 lDRFTGGSRidDAAELKTILESIQrlkVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 478 LLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAI----VEEGAT-EALLAA 527
Cdd:PRK13549 447 LINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKLkgdlINHNLTqEQVMEA 500
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
323-519 |
3.15e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.89 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA-------RAPGAGRGAPPP------------VGI 383
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkKNNHELITNPYSkkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 384 VFQNPYSALNpARTVGQTLA---EALAVGGQGGAQVPDL-LGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLI 459
Cdd:PRK13631 121 VFQFPEYQLF-KDTIEKDIMfgpVALGVKKSEAKKLAKFyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 460 CDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
300-519 |
3.99e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV--------HVARAP 371
Cdd:PRK09700 4 PYISMAGIGKSF--GPVHA-----LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 372 GAGRGapppVGIVFQNpYSALNPArtvgqTLAEALAVGGQG-----GAQVPD----------LLGAVGLPAAHAQRLpAA 436
Cdd:PRK09700 77 AAQLG----IGIIYQE-LSVIDEL-----TVLENLYIGRHLtkkvcGVNIIDwremrvraamMLLRVGLKVDLDEKV-AN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 437 LSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEqGFALAFITHDLAVARQMSDRIIVMKDGAIV 516
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
...
gi 541492527 517 EEG 519
Cdd:PRK09700 225 CSG 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-537 |
4.68e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 332 LPGQSV-GIVGESGSGKTTLARITVGL-EAPDSGTVHVARAPGAGRGA--------PPPVGIVFQ--NPYsalnPARTVG 399
Cdd:PRK14246 33 IPNNSIfGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVLYFGKDIfqidaiklRKEVGMVFQqpNPF----PHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGGQGGAQ-----VPDLLGAVGLPAAHAQRL--PAA-LSGGQRQRVAIARALAARPELLICDEAVSALDVSV 471
Cdd:PRK14246 109 DNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 472 QATIIDLLRRLQAEqgFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAPSHPYTASLI 537
Cdd:PRK14246 189 SQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
50-279 |
4.97e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIDLgvAADSLRRLRGG-GIVWlpQDP---F 124
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGiLKP----SSGRILFDGKPIDY--SRKGLMKLRESvGMVF--QDPdnqL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLSPLHRCGVQVIaHRQGPRSE---RAERALARLAEVGLPARAAraypHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK13636 96 FSASVYQDVSFGAV-NLKLPEDEvrkRVDNALKRTGIEHLKDKPT----HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARpatdyaRQLL-DAQLRL 279
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE------KEMLrKVNLRL 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
43-261 |
5.27e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.62 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVA----DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVelagRTIDLGVAADSLR------RLR 112
Cdd:PRK13643 13 PNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP---TEGKV----TVGDIVVSSTSKQkeikpvRKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 113 GGGIVWLPQDPFTSLSPLHrcGVQVIAHRQGPRSERAER-ALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAP 191
Cdd:PRK13643 86 VGVVFQFPESQLFEETVLK--DVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
44-261 |
5.37e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 77.82 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqfTTSGTVELAGRTidLGvaADSLRRLRG-GGIV--WLP 120
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPP--TYGNDVRLFGER--RG--GEDVWELRKrIGLVspALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLhrcgvQVIA---------HRQgPRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAP 191
Cdd:COG1119 89 LRFPRDETVL-----DVVLsgffdsiglYRE-PTDEQRERARELLELLGLAHLADRPF-GTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
44-255 |
6.62e-16 |
|
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: 76.86 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAG---RTIDLGVaadsLRRlrggGIVWLP 120
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKP---TSGSVLLDGtdiRQLDPAD----LRR----NIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPF----------TSLSPLHRcgvqviahrqgprSERAERAlARLAEVG-LPARAARAYPHQ-------LSGGMRQRVA 182
Cdd:cd03245 85 QDVTlfygtlrdniTLGAPLAD-------------DERILRA-AELAGVTdFVNKHPNGLDLQigergrgLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 183 IAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLrdARGMALVLVTHDLALArDYGDDIVVMRGGAIVEAG 255
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-267 |
7.01e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAP---AQFTTSGTVELAGRTIdlgVAADSLRRLRGGGIVWLP 120
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDI---FQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLPARA---ARAYPHQLSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDArgMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATD 267
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
63-277 |
7.03e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.57 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 63 IVGESGAGKSMLARAICGLAP--AQFTTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQDPFTSLSPLHRCGVQV--- 137
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLElnEEARVEGEVRLFGRNI-YSPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVkln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 138 -IAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLA 216
Cdd:PRK14267 114 gLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLF 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 217 SLRDArgMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQL 277
Cdd:PRK14267 194 ELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
53-277 |
8.25e-16 |
|
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: 76.81 E-value: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 53 VDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDLGVAAdslrrlrgggIVWLPQ-DPFTSLSPLH 131
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP---PAKGTVKVAGASPGKGWRH----------IGYVPQrHEFAWDFPIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 132 RCGVqVIAHRQG-----PRSERAERALAR--LAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALD 204
Cdd:TIGR03771 68 VAHT-VMSGRTGhigwlRRPCVADFAAVRdaLRRVGLTELADRPV-GELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 205 VTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIveagqarrvlarpATDYARQLLDAQL 277
Cdd:TIGR03771 146 MPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLLNGRVI-------------ADGTPQQLQDPAP 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
35-305 |
1.40e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLRRlrgg 114
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDG--VDLSHVPPYQRP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 115 gIVWLPQDpfTSLSPlHRCGVQVIA----HRQGPRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAA 190
Cdd:PRK11607 93 -INMMFQS--YALFP-HMTVEQNIAfglkQDKLPKAEIASRVNEMLGLVHMQEFAKRK-PHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 191 PGVLIADEPTTALDVT----TQKEILTLLASLrdarGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPAT 266
Cdd:PRK11607 168 PKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 267 DYA--------------RQLLDAQLRLDGPSPR-PAGAVPATTVADERPI-VALR 305
Cdd:PRK11607 244 RYSaefigsvnvfegvlKERQEDGLVIDSPGLVhPLKVDADASVVDNVPVhVALR 298
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
40-255 |
1.92e-15 |
|
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: 76.04 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 40 PSDPDRPIVADVSVDAAPGRTLVIVGESGAGKS----MLARaicglapaqF--TTSGTVELAGRTI-DLgvaadSLRRLR 112
Cdd:cd03249 11 PSRPDVPILKGLSLTIPPGKTVALVGSSGCGKStvvsLLER---------FydPTSGEILLDGVDIrDL-----NLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 113 GG-GIVwlPQDP---FTSLSPLHRCGvqviahRQGPRSERAERAlARLAE-----VGLP--------ARAArayphQLSG 175
Cdd:cd03249 77 SQiGLV--SQEPvlfDGTIAENIRYG------KPDATDEEVEEA-AKKANihdfiMSLPdgydtlvgERGS-----QLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdaRGMALVLVTHDLALARDyGDDIVVMRGGAIVEAG 255
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
43-276 |
2.12e-15 |
|
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: 75.60 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRP-IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLgVAADSLRRLRGggiVWLPQ 121
Cdd:cd03252 12 PDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP---ENGRVLVDGHDLAL-ADPAWLRRQVG---VVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFtslspLHRCGVQVIA-HRQGPRSERAERAlARLAEV-----GLPARAARAYPHQ---LSGGMRQRVAIAAALDAAPG 192
Cdd:cd03252 85 NVL-----FNRSIRDNIAlADPGMSMERVIEA-AKLAGAhdfisELPEGYDTIVGEQgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 193 VLIADEPTTALDVTTQKEILTLLASLRDARgmALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRVLARPAtdYARQL 272
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG--LYAYL 233
|
....
gi 541492527 273 LDAQ 276
Cdd:cd03252 234 YQLQ 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
310-517 |
2.24e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 310 EFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgagrgapppvgIVFQNPY 389
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----------MRFASTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 SALN-------------PARTVgqtlAEALAVGgqggaQVPDLLGAV--GLPAAHAQRL---------PAA----LSGGQ 441
Cdd:PRK11288 75 AALAagvaiiyqelhlvPEMTV----AENLYLG-----QLPHKGGIVnrRLLNYEAREQlehlgvdidPDTplkyLSIGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 442 RQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEqGFALAFITHDLAVARQMSDRIIVMKDGAIVE 517
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-537 |
2.40e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.71 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP------GAGRGApppVGIVFQNPY--S 390
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseAALRQA---ISVVSQRVHlfS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 AlnpartvgqTLAE--ALAVGGQGGAQVPDLLGAVGLpAAHAQ---RLPA-------ALSGGQRQRVAIARALAARPELL 458
Cdd:PRK11160 428 A---------TLRDnlLLAAPNASDEALIEVLQQVGL-EKLLEddkGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 459 ICDEAVSALDVSVQATIIDLLRrlQAEQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAApsHPYTASLI 537
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLA--EHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ--QGRYYQLK 571
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
50-255 |
2.43e-15 |
|
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: 74.84 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGrtIDLGVAADSLRRLrggGIVWLPQDPFTSLSP 129
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQ---SGRVLING--VDVTAAPPADRPV---SMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LHRCGVQVIA--HRQGPRSERAERALARLAEVGLPARAarayPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTT 207
Cdd:cd03298 88 EQNVGLGLSPglKLTAEDRQAIEVALARVGLAGLEKRL----PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 208 QKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-528 |
2.59e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLeAPDSGTVHV------ARAPGAGRGAPPPVGivfQNPysal 392
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKIngielrELDPESWRKHLSWVG---QNP---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 npaRTVGQTLAEALAVGGQ--GGAQVPDLLgavglPAAHAQ----RLP-----------AALSGGQRQRVAIARALAARP 455
Cdd:PRK11174 433 ---QLPHGTLRDNVLLGNPdaSDEQLQQAL-----ENAWVSeflpLLPqgldtpigdqaAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 456 ELLICDEAVSALDVSVQATIIDLLRrlQAEQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
44-263 |
2.67e-15 |
|
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: 75.34 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSmlarAICGLAPAQF-TTSGTVELAGRTIDlGVAADSLRRLRGggIVwlPQD 122
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYdVDSGRILIDGHDVR-DYTLASLRRQIG--LV--SQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSLSPLHrcgvQVIAH-RQGPRSERAERAlarlaevglpARAARAypHQ-------------------LSGGMRQRVA 182
Cdd:cd03251 85 VFLFNDTVA----ENIAYgRPGATREEVEEA----------ARAANA--HEfimelpegydtvigergvkLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 183 IAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARgMALVlVTHDLALARDyGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
.
gi 541492527 263 R 263
Cdd:cd03251 226 Q 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
51-262 |
2.69e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLApAQFttSGTVELAGRTIdlgvAADSLRRLRG--GGIVWLPQDPFTSLS 128
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLF-EEF--EGKVKIDGELL----TAENVWNLRRkiGMVFQNPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 PlhRCGVQVIAHRQG-PRSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTT 207
Cdd:PRK13642 99 V--EDDVAFGMENQGiPREEMIKRVDEALLAVNMLDFKTRE-PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 208 QKEILTLLASLRDARGMALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
300-524 |
3.49e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH------VARAPGA 373
Cdd:PRK10762 3 ALLQLKGIDKAF-------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevTFNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 374 GRGAPppVGIVFQNpysaLNparTVGQ-TLAEALAVGGQ-----GG-------AQVPDLLGAVGLPAaHAQRLPAALSGG 440
Cdd:PRK10762 76 SQEAG--IGIIHQE----LN---LIPQlTIAENIFLGREfvnrfGRidwkkmyAEADKLLARLNLRF-SSDKLVGELSIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 441 QRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGA 520
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
....
gi 541492527 521 TEAL 524
Cdd:PRK10762 225 VADL 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
300-513 |
3.50e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFrsGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLeAPD---SGTVHVARAPGAGRG 376
Cdd:PRK13549 4 YLLEMKNITKTF--GGVKA-----LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 A--PPPVGIVFQNPYSALNPARTVGQT--LAEALAVGG-----QGGAQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVAI 447
Cdd:PRK13549 76 IrdTERAGIAIIHQELALVKELSVLENifLGNEITPGGimdydAMYLRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 448 ARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-256 |
3.59e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttsgtvelAGRTIDLGVAADSLRRLRGGGIVWLPQdp 123
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD---------AGKITVLGVPVPARARLARARIGVVPQ-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSPLH--RCGVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK13536 122 FDNLDLEFtvRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 202 ALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQ 256
Cdd:PRK13536 202 GLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
56-269 |
3.72e-15 |
|
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: 77.07 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 56 APGRTlVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIdlgvaADSLRRL------RGGGIVWLPQDPFTSLSP 129
Cdd:TIGR02142 22 GQGVT-AIFGRSGSGKTTLIRLIAGLTRPD---EGEIVLNGRTL-----FDSRKGIflppekRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LHRCGVQVIAHRQGPRSERAERALARLAEVGLPARaaraYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQK 209
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGIGHLLGR----LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 210 EILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYA 269
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
50-260 |
4.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DLGVAADSLRRLRGggIVWlpQDPFTSLs 128
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP---TSGKIIIDGVDItDKKVKLSDIRKKVG--LVF--QYPEYQL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 pLHRCGVQVIAHrqGPR------SERAERALARLAEVGLPARAAR-AYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK13637 97 -FEETIEKDIAF--GPInlglseEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRV 260
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
317-524 |
7.04e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPG--AGRgapppVGIV--FQN 387
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqHIEGLPGhqIAR-----MGVVrtFQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 388 pysalnpARTVGQ-TLAEALAVGGQGGAQVPDLLGAVGLPA----------------------AHAQRLPAALSGGQRQR 444
Cdd:PRK11300 89 -------VRLFREmTVIENLLVAQHQQLKTGLFSGLLKTPAfrraesealdraatwlervgllEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 445 VAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-509 |
8.39e-15 |
|
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: 74.37 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 330 DILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARapgagrgapppVGIVFQNPYSALNPARTVGQTLAEALAVG 409
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-----------DTVSYKPQYIKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 410 GQGGAQVPDLLGAVGLPAAHAQRLPaALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFA 489
Cdd:cd03237 90 YTHPYFKTEIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF-AENNEK 167
|
170 180
....*....|....*....|.
gi 541492527 490 LAF-ITHDLAVARQMSDRIIV 509
Cdd:cd03237 168 TAFvVEHDIIMIDYLADRLIV 188
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
41-231 |
8.84e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.19 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVElagrtidlgvaadslrRLRGGGIVWLP 120
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPW---GSGRIG----------------MPEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLhrcgvqviahrqgprseraeralarlaevglpaRAARAYP--HQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:cd03223 71 QRPYLPLGTL---------------------------------REQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 541492527 199 PTTALDVTTQKEILTLLaslrDARGMALVLVTH 231
Cdd:cd03223 118 ATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
51-265 |
9.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTidlgVAADSLRRLRGG-GIVWlpQDPftslsp 129
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ---RGRVKVMGRE----VNAENEKWVRSKvGLVF--QDP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 lhrcGVQVIAHRQ------GP------RSERAERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:PRK13647 89 ----DDQVFSSTVwddvafGPvnmgldKDEVERRVEEALKAVRMWDFRDKP-PYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 198 EPTTALDVTTQKEILTLLASLrDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGqARRVLARPA 265
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
317-520 |
9.73e-15 |
|
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: 73.30 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV------------HVARAPgagrgapppVGIV 384
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglHDLRSR---------ISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 385 FQNPYsalnparTVGQTLAEALAVGGQ-GGAQVPDLLGAVGLpAAHAQRLPAAL-----------SGGQRQRVAIARALA 452
Cdd:cd03244 84 PQDPV-------LFSGTIRSNLDPFGEySDEELWQALERVGL-KEFVESLPGGLdtvveeggenlSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 453 ARPELLICDEAVSALDVSVQATIIDLLRRlqaeqgfalAF-------ITHDL-AVARqmSDRIIVMKDGAIVEEGA 520
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE---------AFkdctvltIAHRLdTIID--SDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-526 |
1.27e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 317 RAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAP--GAGRGA---PPPVGIVFQNP--- 388
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLlalRQQVATVFQDPeqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 389 --YSALNP-----ARTVGQTLAEAlavggqgGAQVPDLLGAVGlpAAHAQRLP-AALSGGQRQRVAIARALAARPELLIC 460
Cdd:PRK13638 90 ifYTDIDSdiafsLRNLGVPEAEI-------TRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-251 |
1.28e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDLGVAADSLRrlrgGGIVWLPQD--- 122
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP---RTSGYVTLDGHEVVTRSPQDGLA----NGIVYISEDrkr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 -------------PFTSLSPLHRCGVQvIAHRqgprserAERALA----RLAEVGLPARAARAypHQLSGGMRQRVAIAA 185
Cdd:PRK10762 339 dglvlgmsvkenmSLTALRYFSRAGGS-LKHA-------DEQQAVsdfiRLFNIKTPSMEQAI--GLLSGGNQQKVAIAR 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 186 ALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-264 |
1.37e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAP--AQFTTSGTVELAGRTIdLGVAADSLRRlRGGGIVWLPqDPF 124
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEARVSGEVYLDGQDI-FKMDVIELRR-RVQMVFQIP-NPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLSPLHRCGVQV----IAHRQGPRSERAERAL--ARL-AEVG--LPARAARayphqLSGGMRQRVAIAAALDAAPGVLI 195
Cdd:PRK14247 95 PNLSIFENVALGLklnrLVKSKKELQERVRWALekAQLwDEVKdrLDAPAGK-----LSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 196 ADEPTTALDVTTQKEILTLLASLRdaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARP 264
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
297-527 |
1.57e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 297 DERPI----VALRDVVKEFRsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPG 372
Cdd:PRK10790 332 DDRPLqsgrIDIDNVSFAYR------DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 373 AG---RGAPPPVGIVFQNPYSALNPAR---TVGQTLAEalavggqggAQVPDLLGAVGLpAAHAQRLPAA---------- 436
Cdd:PRK10790 406 SSlshSVLRQGVAMVQQDPVVLADTFLanvTLGRDISE---------EQVWQALETVQL-AELARSLPDGlytplgeqgn 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 437 -LSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQaeQGFALAFITHDLAVARQmSDRIIVMKDGAI 515
Cdd:PRK10790 476 nLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
250
....*....|..
gi 541492527 516 VEEGATEALLAA 527
Cdd:PRK10790 553 VEQGTHQQLLAA 564
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
324-496 |
2.34e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarAPGAgrgappPVGIVFQNPYsaLNPARTVGQTLA 403
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGI------KVGYLPQEPQ--LDPEKTVRENVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 404 EALA-----------VGGQGG-------------AQVPDLLGAVGL--------PAAHAQRLPAA------LSGGQRQRV 445
Cdd:PRK11819 93 EGVAevkaaldrfneIYAAYAepdadfdalaaeqGELQEIIDAADAwdldsqleIAMDALRCPPWdakvtkLSGGERRRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 541492527 446 AIARALAARPELLICDEAVSALDV-SVQAtiidLLRRLQAEQGFALAfITHD 496
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAeSVAW----LEQFLHDYPGTVVA-VTHD 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-300 |
2.45e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.60 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaADSLRRlrgggIVWLPQDP 123
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP---DSGEVLWDGEPLD----PEDRRR-----IGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftSLSPLHRCGVQVI--AHRQG-PRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:COG4152 81 --GLYPKMKVGEQLVylARLKGlSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 201 TALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARpatdYARQLLdaQLRLD 280
Cdd:COG4152 158 SGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ----FGRNTL--RLEAD 230
|
250 260
....*....|....*....|
gi 541492527 281 GPSPRPAgAVPATTVADERP 300
Cdd:COG4152 231 GDAGWLR-ALPGVTVVEEDG 249
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-268 |
4.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.71 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPSD--PD-RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttsgtvelAGRTIDLGVAADSLRRL 111
Cdd:PRK13644 2 IRLENVSYsyPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ---------KGKVLVSGIDTGDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 112 RG----GGIVWlpQDPFTSLspLHRCGVQVIAHrqGPRS---------ERAERAlarLAEVGLPARAARAyPHQLSGGMR 178
Cdd:PRK13644 73 QGirklVGIVF--QNPETQF--VGRTVEEDLAF--GPENlclppieirKRVDRA---LAEIGLEKYRHRS-PKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 179 QRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDyGDDIVVMRGGAIVEAGQAR 258
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
250
....*....|
gi 541492527 259 RVLARPATDY 268
Cdd:PRK13644 221 NVLSDVSLQT 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
44-271 |
4.42e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqfTTSGTVELAGRTiDLGVAADSLRRLRgggivwlpQDp 123
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE----TPSAGELLAGTA-PLAEAREDTRLMF--------QD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 fTSLSPLHRcgvqVIAHRQ-GPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK11247 90 -ARLLPWKK----VIDNVGlGLKGQWRDAALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 203 LDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAI---------------------VEAGQARRVL 261
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltvdlprprrrgsarlaeLEAEVLQRVM 243
|
250
....*....|
gi 541492527 262 ARPATDYARQ 271
Cdd:PRK11247 244 SRGESEPTRL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
44-283 |
4.69e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIdlgvAADSLRRLRGG-GIVWlpQ 121
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKP----TSGSVLIRGEPI----TKENIREVRKFvGLVF--Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSL-SPLHRCGVQVIAHRQGPRSER-AERALARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:PRK13652 86 NPDDQIfSPTVEQDIAFGPINLGLDEETvAHRVSSALHMLGLEELRDRV-PHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 200 TTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPAtdyarqlLDAQLRL 279
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD-------LLARVHL 237
|
....
gi 541492527 280 DGPS 283
Cdd:PRK13652 238 DLPS 241
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
44-255 |
5.18e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.04 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSLRRLrggGIvwLPQDP 123
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD---SGEVLVDGLDVATTPSRELAKRL---AI--LRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLsplhRCGV-QVIA-----HRQG---PRSERA-ERALARLaevGLPARAARaYPHQLSGGMRQRvaiaaaldaapgV 193
Cdd:COG4604 85 HINS----RLTVrELVAfgrfpYSKGrltAEDREIiDEAIAYL---DLEDLADR-YLDELSGGQRQR------------A 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 194 LIA------------DEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:COG4604 145 FIAmvlaqdtdyvllDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
321-528 |
5.74e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.36 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGA--------GRGApppvgIVFQNPYsal 392
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqldswrSRLA-----VVSQTPF--- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 nparTVGQTLAEALAVGGQGGAQvPDLLGAVGLPAAHAQ--RLPAA-----------LSGGQRQRVAIARALAARPELLI 459
Cdd:PRK10789 400 ----LFSDTVANNIALGRPDATQ-QEIEHVARLASVHDDilRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 460 CDEAVSALDVSVQATIIDLLRrlQAEQGFALAFITHDLAvARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-519 |
6.10e-14 |
|
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: 70.63 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEA--PDSGTVHV-----------ARApGAGrgapppVGIVFQNPys 390
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFkgeditdlppeERA-RLG------IFLAFQYP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 alnpARTVGQTLAealavggqggaqvpDLLGAVGlpaahaqrlpAALSGGQRQRVAIARALAARPELLICDEAVSALDVS 470
Cdd:cd03217 87 ----PEIPGVKNA--------------DFLRYVN----------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 541492527 471 VQATIIDLLRRLqAEQGFALAFITHDLAVARQM-SDRIIVMKDGAIVEEG 519
Cdd:cd03217 139 ALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-249 |
6.70e-14 |
|
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: 74.09 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFttSGTVELAGRTIDLGVAADSLR 109
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF--EGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RlrggGIVWLPQD-------------PFTSLSPLHR-CGVQVI--AHRQGPRSERAERALARLAEVGLPARaarayphQL 173
Cdd:TIGR02633 336 A----GIAMVPEDrkrhgivpilgvgKNITLSVLKSfCFKMRIdaAAELQIIGSAIQRLKVKTASPFLPIG-------RL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 174 SGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
44-255 |
7.89e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 69.65 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGrtIDLGVAADSLRRLrgggIVWLPQDP 123
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDG--VPVSDLEKALSSL----ISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 F---TSLsplhrcgvqviahrqgprseraeralarLAEVGLparaarayphQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:cd03247 85 YlfdTTL----------------------------RNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 201 TALDVTTQKEILTLLASLrdARGMALVLVTHDLAlARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03247 127 VGLDPITERQLLSLIFEV--LKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
51-258 |
8.18e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDL-GVAADSLRRLRG-GGIVWLPQDPFTSLS 128
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQReGRLARDIRKSRAnTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 129 PLHRCGVQVIAHRQGPRS-------ERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK09984 103 VLENVLIGALGSTPFWRTcfswftrEQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 202 ALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQAR 258
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
172-468 |
9.80e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.51 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 172 QLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLrDARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 252 VEAGQARRVLArpatdyarQLLDAQL----RLDG-PSPRPAGAVPATTVADERPIVALRDVVKEFrsGGRRAEGHLalag 326
Cdd:PRK10938 214 AETGEREEILQ--------QALVAQLahseQLEGvQLPEPDEPSARHALPANEPRIVLNNGVVSY--NDRPILHNL---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 327 vSLDILPGQSVGIVGESGSGKTTLARITVGlEAPDSGTVHV---ARAPGAGR---GAPPPVGIV---FQNPYSALNPART 397
Cdd:PRK10938 280 -SWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSNDLtlfGRRRGSGEtiwDIKKHIGYVsssLHLDYRVSTSVRN 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 V---G--------QTLAEALAvggQGGAQVPDLLgavGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK10938 358 VilsGffdsigiyQAVSDRQQ---KLAQQWLDIL---GIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQG 431
|
..
gi 541492527 467 LD 468
Cdd:PRK10938 432 LD 433
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
301-530 |
9.83e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVvkEFRSGGRraeghLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV--ARAPGAGRG-- 376
Cdd:PRK11831 7 LVDMRGV--SFTRGNR-----CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgENIPAMSRSrl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 --APPPVGIVFQNpySALNPARTVGQTLAEALavggQGGAQVPDL---------LGAVGLPAAhAQRLPAALSGGQRQRV 445
Cdd:PRK11831 80 ytVRKRMSMLFQS--GALFTDMNVFDNVAYPL----REHTQLPAPllhstvmmkLEAVGLRGA-AKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
....*
gi 541492527 526 AAPSH 530
Cdd:PRK11831 233 ANPDP 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
43-238 |
1.08e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVelagrtidlgvaadslRRLRGGGIVWLPQ 121
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvLRP----TSGTV----------------RRAGGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DpfTSLSPLHRCGV-QVIA----HRQGP--RSERAERAL--ARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPG 192
Cdd:NF040873 63 R--SEVPDSLPLTVrDLVAmgrwARRGLwrRLTRDDRAAvdDALERVGLADLAGRQL-GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 193 VLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARD 238
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRR 184
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-264 |
1.63e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.22 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 40 PSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAG--------RTIDLGVAA----- 105
Cdd:TIGR00958 489 PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQP----TGGQVLLDGvplvqydhHYLHRQVALvgqep 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 106 ----DSLRRLRGGGIVWLPQDPFTSLSPLHRCGVQVIAHRQGPRSERAERAlarlaevglparaaraypHQLSGGMRQRV 181
Cdd:TIGR00958 565 vlfsGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG------------------SQLSGGQKQRI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 182 AIAAALDAAPGVLIADEPTTALDVttqkEILTLLASLRDARGMALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRVL 261
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLM 701
|
...
gi 541492527 262 ARP 264
Cdd:TIGR00958 702 EDQ 704
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
43-295 |
1.64e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAicgLAPAQFTTSGTVELAGRTIDLGVAADSLRRlrgggIVWLPQd 122
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKM---LGRHQPPSEGEILLDAQPLESWSSKAFARK-----VAYLPQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 pftSLSPLHRCGV-QVIAHRQGP--------RSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:PRK10575 93 ---QLPAAEGMTVrELVAIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLV-DSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 194 LIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLarpATDYARQLL 273
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM---RGETLEQIY 245
|
250 260
....*....|....*....|..
gi 541492527 274 DAQLrldGPSPRPAGAVPATTV 295
Cdd:PRK10575 246 GIPM---GILPHPAGAAPVSFV 264
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-252 |
1.76e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 8 GRTVTARAERigtAGSTGTGTGLRARAIRVANPSDpdRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqft 87
Cdd:COG3845 239 GREVLLRVEK---APAEPGEVVLEVENLSVRDDRG--VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP--- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 88 TSGTVELAGRTIdlgvAADSLRRLRGGGIVWLPQDPFT-------SLS-----------PLHRCGVQviahRQGPRSERA 149
Cdd:COG3845 311 ASGSIRLDGEDI----TGLSPRERRRLGVAYIPEDRLGrglvpdmSVAenlilgryrrpPFSRGGFL----DRKAIRAFA 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 150 ERALA----RLAEVGLPARAarayphqLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMA 225
Cdd:COG3845 383 EELIEefdvRTPGPDTPARS-------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAA 454
|
250 260 270
....*....|....*....|....*....|.
gi 541492527 226 LVLVTHDL----ALArdygDDIVVMRGGAIV 252
Cdd:COG3845 455 VLLISEDLdeilALS----DRIAVMYEGRIV 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
173-507 |
1.91e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 173 LSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTqkeILTLLASLRDARGmALVLVTHDlalaRDYGDDIV-----VMR 247
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTHD----RYFLDNVAgwileLDR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 248 GGAI---------VEAGQAR------------RVL------------ARPATDYAR-----QLL--DAQLRLDG------ 281
Cdd:PRK11819 236 GRGIpwegnysswLEQKAKRlaqeekqeaarqKALkrelewvrqspkARQAKSKARlaryeELLseEYQKRNETneifip 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 282 PSPRPAGAVpattvaderpiVALRDVVKEFrsGGRraeghLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPD 361
Cdd:PRK11819 316 PGPRLGDKV-----------IEAENLSKSF--GDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 362 SGTVHVarapgagrGAPPPVGIVFQNpYSALNPARTVGQTLAEALAVGGQGGAQVPD--LLGAVGLPAAHAQRLPAALSG 439
Cdd:PRK11819 378 SGTIKI--------GETVKLAYVDQS-RDALDPNKTVWEEISGGLDIIKVGNREIPSraYVGRFNFKGGDQQKKVGVLSG 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 440 GQRQRVAIARALAARPELLICDEAVSALDVsvqatiiDLLRRLqaEQGFaLAF------ITHDlavaRQMSDRI 507
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDV-------ETLRAL--EEAL-LEFpgcavvISHD----RWFLDRI 508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-507 |
2.11e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.06 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPPVGIVFQNPYSALNPARTVG 399
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QTLAEALAVGGQggAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLL 479
Cdd:cd03231 92 ENLRFWHADHSD--EQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180
....*....|....*....|....*...
gi 541492527 480 RRLQAEQGFALAFITHDLAVARQMSDRI 507
Cdd:cd03231 169 AGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
322-519 |
2.31e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 69.61 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPD---SGTVHVARAPGAGRGAPPPVGIVFQNPYsaLNPARTV 398
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCVAYVRQDDI--LLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLAEALAV-------GGQGGAQVPD-LLGAVGLPAAHAQRLPAaLSGGQRQRVAIARALAARPELLICDEAVSALDVS 470
Cdd:cd03234 99 RETLTYTAILrlprkssDAIRKKRVEDvLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 471 VQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
46-251 |
3.00e-13 |
|
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: 69.12 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAapGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIdLGVAADSlrrlRGGGIVWLPQDPFT 125
Cdd:TIGR01277 14 PMEFDLNVAD--GEIVAIMGPSGAGKSTLLNLIAGF---IEPASGSIKVNDQSH-TGLAPYQ----RPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQViahRQGPR--SERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:TIGR01277 84 HLTVRQNIGLGL---HPGLKlnAEQQEKVVDAAQQVGIADYLDR-LPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
47-261 |
3.03e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSLRRlrgggIVWLPQDPFTs 126
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---HGHVWLDGEHIQHYASKEVARR-----IGLLAQNATT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 lsPLHRCGVQVIAHRQGP--------RSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:PRK10253 93 --PGDITVQELVARGRYPhqplftrwRKEDEEAVTKAMQATGITHLADQSV-DTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
143-262 |
3.04e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 143 GPRS------ERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLA 216
Cdd:PRK13651 130 GPVSmgvskeEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 541492527 217 SLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:PRK13651 210 NLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-251 |
3.38e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFttSGTVELAGRTIDLGVAADSLR 109
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRW--EGEIFIDGKPVKIRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RlrggGIVWLPQD-------PFTS------LSPLHR-CGVQVIAHRQGPRSerAERALARLaevglpaRAARAYPHQ--- 172
Cdd:PRK13549 338 Q----GIAMVPEDrkrdgivPVMGvgknitLAALDRfTGGSRIDDAAELKT--ILESIQRL-------KVKTASPELaia 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 173 -LSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:PRK13549 405 rLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-255 |
4.62e-13 |
|
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: 68.71 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRT---IDLGVAAD 106
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP---PDSGTVTVRGRVsslLGLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 107 ---SLR---RLRGGgivwlpqdpftslspLHRCGVQVIAHRqgprseraERALARLAEVG----LPARaarayphQLSGG 176
Cdd:cd03220 97 pelTGReniYLNGR---------------LLGLSRKEIDEK--------IDEIIEFSELGdfidLPVK-------TYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 177 MRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
52-262 |
4.82e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 52 SVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtIDLGVAADSLR-------------RLRGGGIVW 118
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP---ASGSLTLNG--QDHTTTPPSRRpvsmlfqennlfsHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 119 LPQDPFTSLSPLHRCGVQVIAHRQGprserAERALARLaevglparaarayPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMG-----IEDLLARL-------------PGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 199 PTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
323-519 |
7.17e-13 |
|
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: 67.82 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----ARAP-GAGRGApppVGIVFQNPY------- 389
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidiSTIPlEDLRSS---LTIIPQDPTlfsgtir 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 SALNP-ARTVGQTLAEALAVGGQGgaqvpdllgavglpaahaqrlpAALSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:cd03369 100 SNLDPfDEYSDEEIYGALRVSEGG----------------------LNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 469 VSVQATIIDLLRRLQaeQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEG 519
Cdd:cd03369 158 YATDALIQKTIREEF--TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
49-251 |
7.63e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 49 ADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQDPFTS-- 126
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR---GGRIMLNGKEINALSTAQRLAR----GLVYLPEDRQSSgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 --LSPLHRCGVQVIAHRQG----PRSERA-----ERALA-RLAEVGLPARAarayphqLSGGMRQRVAIAAALDAAPGVL 194
Cdd:PRK15439 353 ylDAPLAWNVCALTHNRRGfwikPARENAvleryRRALNiKFNHAEQAART-------LSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAI 251
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
40-262 |
8.55e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 70.84 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 40 PSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDlgvaaDSLRRLRGGGIVWL 119
Cdd:TIGR01842 326 PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP---PTSGSVRLDGADLK-----QWDRETFGKHIGYL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQDpfTSLSPlhrcGV--QVIAH-RQGPRSERAERAlARLAEV-----GLP-----ARAARAYPhqLSGGMRQRVAIAAA 186
Cdd:TIGR01842 398 PQD--VELFP----GTvaENIARfGENADPEKIIEA-AKLAGVhelilRLPdgydtVIGPGGAT--LSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 187 LDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALArDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLA 542
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
45-248 |
9.19e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqfttsgtvelagrtidlgvaadslRRLRGGGIVWLPQDPF 124
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--------------------------KGTPVAGCVDVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLSPLhrcgVQVIAHRQGPRSeraerALARLAEVGLP-ARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTAL 203
Cdd:COG2401 97 GREASL----IDAIGRKGDFKD-----AVELLNAVGLSdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 541492527 204 DVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRG 248
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
45-231 |
1.02e-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: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtidlgvAADSLRRLRGGGIVWLPQDPF 124
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP---DSGEVRWNGT------PLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 --TSLSPLHRcgVQVIAHRQGPRSERAERALARlaeVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:TIGR01189 84 lkPELSALEN--LHFWAAIHGGAQRTIEDALAA---VGLTGFEDLPA-AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 541492527 203 LDVTTQKEILTLLASlRDARGMALVLVTH 231
Cdd:TIGR01189 158 LDKAGVALLAGLLRA-HLARGGIVLLTTH 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-525 |
1.36e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLeAPDSGTVHVA---------------RAPGAGRGAPPPVGIVFQnp 388
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNgrplsdwsaaelarhRAYLSQQQSPPFAMPVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 389 YSALN-PARTVGQTLAEALAvggqggaqvpDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARAL-----AARPE--LLIC 460
Cdd:COG4138 89 YLALHqPAGASSEAVEQLLA----------QLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 461 DEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
324-526 |
2.55e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARapgaGRGAPPPV-----------GIVFQNPYSAL 392
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIR----GTVAYVPQvswifnatvrdNILFGSPFDPE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 NPARTVGQT-LAEALAV--GGqggaqvpDL--LGAVGLpaahaqrlpaALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:PLN03130 709 RYERAIDVTaLQHDLDLlpGG-------DLteIGERGV----------NISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 468 DVSVQATIIDllRRLQAE-QGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLA 526
Cdd:PLN03130 772 DAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSN 828
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
46-312 |
2.66e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDLGVAADslrrlRGGGIVWlpQDpfT 125
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLER---ITSGEIWIGGRVVNELEPAD-----RDIAMVF--QN--Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPlHRCGVQVIAH----RQGPRSERAER--ALARLAEVG-LPARAarayPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:PRK11650 86 ALYP-HMSVRENMAYglkiRGMPKAEIEERvaEAARILELEpLLDRK----PRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 199 PTTALD----VTTQKEILTLLASLrdarGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDY------ 268
Cdd:PRK11650 161 PLSNLDaklrVQMRLEIQRLHRRL----KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFvasfig 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 541492527 269 --ARQLLDAQLRLDGPSPRPAGAVpATTVADERPIVALRDVVKEFR 312
Cdd:PRK11650 237 spAMNLLDGRVSADGAAFELAGGI-ALPLGGGYRQYAGRKLTLGIR 281
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
30-255 |
2.93e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 65.65 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDP---DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfTTSGTVELAGRTIDLgvaaD 106
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL-GVSGEVLINGRPLDK----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 107 SLRRLRGggivWLPQDPFTSLSPLHRCGVQVIAHRQGprseraeralarlaevglparaarayphqLSGGMRQRVAIAAA 186
Cdd:cd03213 79 SFRKIIG----YVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 187 LDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLAlARDYG--DDIVVMRGGAIVEAG 255
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPS-SEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
41-255 |
3.01e-12 |
|
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: 66.24 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVA--DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGrtidLGVAADSLRRLRGGGIVW 118
Cdd:cd03266 12 RDVKKTVQAvdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEP---DAGFATVDG----FDVVKEPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 119 LPQDPFTSLSPlhRCGVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:cd03266 85 DSTGLYDRLTA--RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 199 PTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
323-526 |
3.72e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARAPGAgRGAPPPVGIVfqnPYSALNPARt 397
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkDITDWQTA-KIMREAVAIV---PEGRRVFSR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 vgQTLAEALAVGG---------QGGAQVPDLLgavglPAAHAQRLPAA--LSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PRK11614 95 --MTVEENLAMGGffaerdqfqERIKWVYELF-----PRLHERRIQRAgtMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 467 LDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
45-255 |
4.15e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.83 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLaraICGLAPAQFTTSGTVELAGRTIDlGVAADSLRRlrGGGIVWlpQDPF 124
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVFDPQSGRILIDGTDIR-TVTRASLRR--NIAVVF--QDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 ---TSLSPLHRCGvqviahRQGPRSERAERALARLAEVGLPARAARAYP-------HQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:PRK13657 420 lfnRSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRdaRGMALVLVTHDLALARDyGDDIVVMRGGAIVEAG 255
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
35-288 |
4.80e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRTIdlgvAADSLRRL-- 111
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAP----DHGEILFDGENI----PAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 112 --RGGGIVWLPQDPFTSLSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLPArAARAYPHQLSGGMRQRVAIAAALDA 189
Cdd:PRK11831 82 vrKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRG-AAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDyA 269
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-V 239
|
250 260
....*....|....*....|.
gi 541492527 270 RQLLDAQlrLDGPSP--RPAG 288
Cdd:PRK11831 240 RQFLDGI--ADGPVPfrYPAG 258
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
57-235 |
5.72e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.28 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 57 PGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLGVAADSLRRLRGGGIVWLPQDPFTSLSPLHRCGVQ 136
Cdd:PRK10908 27 PGEMAFLTGHSGAGKSTLLKLICGI---ERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 137 -VIAHRQGPRSERaeRALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLL 215
Cdd:PRK10908 104 lIIAGASGDDIRR--RVSAALDKVGLLDKA-KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLF 180
|
170 180
....*....|....*....|
gi 541492527 216 ASLRDArGMALVLVTHDLAL 235
Cdd:PRK10908 181 EEFNRV-GVTVLMATHDIGL 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
63-282 |
6.27e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 63 IVGESGAGKSMLARAICGLApaqFTTSGTVELAGRTIDLGVAA-DSLRRLRGG-GIVW------LPQDPF---TSLSPLH 131
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLI---ISETGQTIVGDYAIPANLKKiKEVKRLRKEiGLVFqfpeyqLFQETIekdIAFGPVN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 132 rcgvqviahrQGPRSERAERALARLAE-VGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKE 210
Cdd:PRK13645 119 ----------LGENKQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 211 ILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQarrvlarPATDYARQLLDAQLRLDGP 282
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS-------PFEIFSNQELLTKIEIDPP 253
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
44-235 |
7.72e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVElagrtidlgvAADSLRrlrgggIVWLPQ- 121
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAP----DEGVIK----------RNGKLR------IGYVPQk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 ---DPFTSLSPlhrcgVQVIAHRQGPRSERAERALARLAEVGLparaaRAYPHQ-LSGGMRQRVAIAAALDAAPGVLIAD 197
Cdd:PRK09544 76 lylDTTLPLTV-----NRFLRLRPGTKKEDILPALKRVQAGHL-----IDAPMQkLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 541492527 198 EPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLAL 235
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
43-255 |
9.29e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDlgvaADSLRRLRGggivWLPQD 122
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPID----AKEMRAISA----YVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 -----PFTSLSPLhrcgvQVIAH----RQGPRSERAERALARLAEVGL-PARAAR-AYPHQ---LSGGMRQRVAIAAALD 188
Cdd:TIGR00955 108 dlfipTLTVREHL-----MFQAHlrmpRRVTKKEKRERVDEVLQALGLrKCANTRiGVPGRvkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 189 AAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLAlARDYG--DDIVVMRGGAIVEAG 255
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLG 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
320-527 |
9.43e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 9.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGagRGApppvgiVFQNPYSALNPARTVG 399
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT--RQA------LQKNLVAYVPQSEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 400 QT---LAEALAVGGQGG-------------AQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEA 463
Cdd:PRK15056 91 WSfpvLVEDVVMMGRYGhmgwlrrakkrdrQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 464 VSALDVSVQATIIDLLRRLQAEqGFALAFITHDLAVARQMSDRIIVMKdGAIVEEGATEALLAA 527
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTA 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-263 |
1.22e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.60 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqFTTSGTVELAGRTIDlGVAADSLRRLrggGIVwlPQdp 123
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT---HPDAGSISLCGEPVP-SRARHARQRV---GVV--PQ-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FTSLSP--LHRCGVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK13537 88 FDNLDPdfTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 202 ALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:PRK13537 168 GLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-253 |
1.39e-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: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELaGRTIDLGvaadslrrlrgggivWL 119
Cdd:COG0488 324 SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEP----DSGTVKL-GETVKIG---------------YF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQDpFTSLSPLHRcgvqVIAH-RQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADE 198
Cdd:COG0488 384 DQH-QEELDPDKT----VLDElRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 199 PTTALDVTTqKEILTLLasLRDARGmALVLVTHDLALARDYGDDIVVMRGGAIVE 253
Cdd:COG0488 459 PTNHLDIET-LEALEEA--LDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
44-231 |
1.42e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRLRgggivwlPQDP 123
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP---AAGTIKLDGGDIDDPDVAEACHYLG-------HRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FT-SLSPLHrcGVQVIAHRQGPRSERAERALARlaeVGLPARAARAYPHqLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK13539 84 MKpALTVAE--NLEFWAAFLGGEELDIAAALEA---VGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*....
gi 541492527 203 LDVTTQKEILTLLASLRDARGMAlVLVTH 231
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIV-IAATH 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-528 |
1.65e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTT----LARIT-VGLEAPDSGTVHV------ARAPGAGRgAPPPVGIVFQNPysAL 392
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMNeLESEVRVEGRVEFfnqniyERRVNLNR-LRRQVSMVHPKP--NL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 393 NPARTVGQTLAEALAVGGQGGAQVPDLLGAvGLPAA----------HAQRLpaALSGGQRQRVAIARALAARPELLICDE 462
Cdd:PRK14258 100 FPMSVYDNVAYGVKIVGWRPKLEIDDIVES-ALKDAdlwdeikhkiHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKD-----GAIVEEGATEALLAAP 528
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
145-468 |
1.71e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 145 RSERAERALARLAEVGL---PARAARayphQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDA 221
Cdd:NF033858 110 AAERRRRIDELLRATGLapfADRPAG----KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 222 R-GMALVLVTHDLALARDYgDDIVVMRGGAIVEAGQARRVLARPATD-----YARQLLDAQLRLDGP---SPRPAGAvpa 292
Cdd:NF033858 186 RpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGADtleaaFIALLPEEKRRGHQPvviPPRPADD--- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 293 ttvADERPIVAlRDVVKEFrsGGRRAEGHlalagVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-ARAP 371
Cdd:NF033858 262 ---DDEPAIEA-RGLTMRF--GDFTAVDH-----VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 372 GAG------RgapppVGIVFQ--NPYSALnparTVGQTL---AEALAVGG-QGGAQVPDLLGAVGLpAAHAQRLPAALSG 439
Cdd:NF033858 331 DAGdiatrrR-----VGYMSQafSLYGEL----TVRQNLelhARLFHLPAaEIAARVAEMLERFDL-ADVADALPDSLPL 400
|
330 340
....*....|....*....|....*....
gi 541492527 440 GQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
156-505 |
2.22e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 156 LAEVGLPARAARAyphQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTqkeILTLLASLRDARGmALVLVTHDLAL 235
Cdd:PRK11147 143 LAQLGLDPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQG-SIIFISHDRSF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 236 ARDYGDDIVVM-RGGAI------------------VEAGQAR---RVLARPATdYARQLLDAQlrldgpSPRPAGAVpat 293
Cdd:PRK11147 216 IRNMATRIVDLdRGKLVsypgnydqyllekeealrVEELQNAefdRKLAQEEV-WIRQGIKAR------RTRNEGRV--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 294 tvadeRPIVALRD---------------VVKEFRSG---------GRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTT 349
Cdd:PRK11147 286 -----RALKALRRerserrevmgtakmqVEEASRSGkivfemenvNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 350 LARITVGLEAPDSGTVHVarapgagrGAPPPVGiVFQNPYSALNPARTVGQTLAEA---LAVGGQ-----GGAQvpDLLg 421
Cdd:PRK11147 361 LLKLMLGQLQADSGRIHC--------GTKLEVA-YFDQHRAELDPEKTVMDNLAEGkqeVMVNGRprhvlGYLQ--DFL- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 422 avgLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVqatiIDLLRRLQAE-QGfALAFITHDlava 500
Cdd:PRK11147 429 ---FHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSyQG-TVLLVSHD---- 496
|
....*
gi 541492527 501 RQMSD 505
Cdd:PRK11147 497 RQFVD 501
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-233 |
2.74e-11 |
|
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: 65.84 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPdrPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlGVAADSLR 109
Cdd:TIGR02868 335 LELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVS-SLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 RLrgggIVWLPQDPF---TSLSPLHRCGvqviahRQGPRSERAERALARlaeVGLpARAARAYPH-----------QLSG 175
Cdd:TIGR02868 409 RR----VSVCAQDAHlfdTTVRENLRLA------RPDATDEELWAALER---VGL-ADWLRALPDgldtvlgeggaRLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDarGMALVLVTHDL 233
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
324-514 |
3.10e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 63.12 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPP-------PVGIVFQNPYsALNPar 396
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnrySVAYAAQKPW-LLNA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 tvgqTLAEALAVGGQGGAQ-----------VPDL-LGAVGLPAAHAQRlPAALSGGQRQRVAIARALAARPELLICDEAV 464
Cdd:cd03290 94 ----TVEENITFGSPFNKQrykavtdacslQPDIdLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 465 SALDVSV-----QATIIDLLRrlqaEQGFALAFITHDLAVARQmSDRIIVMKDGA 514
Cdd:cd03290 169 SALDIHLsdhlmQEGILKFLQ----DDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
44-256 |
4.43e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.67 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLapaQFTTSGTVELAGRTIDLGVAADslrrlRGGGIVWlpQD- 122
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGDLFIGEKRMNDVPPAE-----RGVGMVF--QSy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 ---PFTSLSPLHRCGVQVIAHRQGPRSERAERAlarlAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:PRK11000 85 alyPHLSVAENMSFGLKLAGAKKEEINQRVNQV----AEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 200 TTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQ 256
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
50-518 |
4.45e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfTTSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQDpfTSLSP 129
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHG-SYEGEILFDGEVCRFKDIRDSEAL----GIVIIHQE--LALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LhrcgvQVIA------HRQGPR-----SERAERALARLAEVGLparaaRAYPHQLSG----GMRQRVAIAAALDAAPGVL 194
Cdd:NF040905 92 Y-----LSIAeniflgNERAKRgvidwNETNRRARELLAKVGL-----DESPDTLVTdigvGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARrvlARPATD------- 267
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCR---ADEVTEdriirgm 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 268 YARQLLDaqlRLDGPSPRpAGAVpATTVAD---ERPIVALRDVVKefrsggrraeghlalaGVSLDILPGQSVGIVGESG 344
Cdd:NF040905 238 VGRDLED---RYPERTPK-IGEV-VFEVKNwtvYHPLHPERKVVD----------------DVSLNVRRGEIVGIAGLMG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 345 SGKTTLA----------RItvgleapdSGTVH----------VARAPGAG-------RGApppVGIVFQNPYSalnpaRT 397
Cdd:NF040905 297 AGRTELAmsvfgrsygrNI--------SGTVFkdgkevdvstVSDAIDAGlayvtedRKG---YGLNLIDDIK-----RN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 VgqTLA--EALAVGG--QGGAQV--------------PDLLGAVGlpaahaqrlpaALSGGQRQRVAIARALAARPELLI 459
Cdd:NF040905 361 I--TLAnlGKVSRRGviDENEEIkvaeeyrkkmniktPSVFQKVG-----------NLSGGNQQKVVLSKWLFTDPDVLI 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 460 CDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEE 518
Cdd:NF040905 428 LDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
324-513 |
4.87e-11 |
|
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: 61.88 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTL-----ARITVGLEapdSGTVHVARAPGaGRGAPPPVGIVFQNPysALNPARTV 398
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLldvlaGRKTAGVI---TGEILINGRPL-DKNFQRSTGYVEQQD--VHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLaealavggqggaqvpdllgavglpaahaqRLPAALSG---GQRQRVAIARALAARPELLICDEAVSALDVSVQATI 475
Cdd:cd03232 97 REAL-----------------------------RFSALLRGlsvEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 541492527 476 IDLLRRLqAEQGFALAFITHD-LAVARQMSDRIIVMKDG 513
Cdd:cd03232 148 VRFLKKL-ADSGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
301-517 |
5.12e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDS--GTVHVARAPGAGRG-- 376
Cdd:NF040905 1 ILEMRGITKTF-------PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDir 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPPVGIVFQNPYSALNPARTVgqtlAEALAVG---GQGG--------AQVPDLLGAVGLpAAHAQRLPAALSGGQRQRV 445
Cdd:NF040905 74 DSEALGIVIIHQELALIPYLSI----AENIFLGnerAKRGvidwnetnRRARELLAKVGL-DESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 446 AIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVE 517
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
44-249 |
6.49e-11 |
|
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: 60.54 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELaGRTIDLGvaadslrrlrgggivwlpqd 122
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEP----DEGIVTW-GSTVKIG-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 pftslsplhrcgvqviahrqgprseraeralarlaevglparaaraYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03221 67 ----------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 541492527 203 LDVTTqkeILTLLASLRDARGmALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:cd03221 101 LDLES---IEALEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
324-526 |
7.64e-11 |
|
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: 65.35 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRGAPPPVGIVFQNPY--------SALNPA 395
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK-----GSVAYVPQQAWIQNDSlrenilfgKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 396 RTvgQTLAEALAVggqggaqVPDLlgaVGLPAAHAQRLPAA---LSGGQRQRVAIARALAARPELLICDEAVSALDVSVQ 472
Cdd:TIGR00957 729 YY--QQVLEACAL-------LPDL---EILPSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 473 ATIID-LLRRLQAEQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLA 526
Cdd:TIGR00957 797 KHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-263 |
7.64e-11 |
|
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: 64.74 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDpDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARaicgLAPAQFT-TSGTVELAGRTI-DLGVAadS 107
Cdd:TIGR02203 331 VEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRFYEpDSGQILLDGHDLaDYTLA--S 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 108 LRRlrggGIVWLPQDPFTSLSPLHRcGVQVIAHRQGPRsERAERAL--ARLAEV--GLP--------ARAARayphqLSG 175
Cdd:TIGR02203 404 LRR----QVALVSQDVVLFNDTIAN-NIAYGRTEQADR-AEIERALaaAYAQDFvdKLPlgldtpigENGVL-----LSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdaRGMALVLVTHDLALARDyGDDIVVMRGGAIVEAG 255
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
....*...
gi 541492527 256 QARRVLAR 263
Cdd:TIGR02203 550 THNELLAR 557
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
45-265 |
7.89e-11 |
|
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: 62.18 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLgVAADSLRRLrggGIVWLPQDP- 123
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKP---DSGKILLDGQDITK-LPMHKRARL---GIGYLPQEAs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 -FTSLSplhrcgVQ-----VIAHRQGPRSERAERALARLAEVGL-PARAARAYphQLSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:cd03218 86 iFRKLT------VEenilaVLEIRGLSKKEREEKLEELLEEFHItHLRKSKAS--SLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 197 DEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
39-252 |
8.90e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.41 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 39 NPSDPD-RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlGVAADslRRLRGGGIV 117
Cdd:COG1101 12 NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP---DSGSILIDGKDVT-KLPEY--KRAKYIGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 WlpQDPFTSLSPlhrcGVQV-----IAHRQG------PRSERAERA-----LARL---------AEVGLparaarayphq 172
Cdd:COG1101 86 F--QDPMMGTAP----SMTIeenlaLAYRRGkrrglrRGLTKKRRElfrelLATLglglenrldTKVGL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 173 LSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIV 252
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
300-519 |
1.09e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 300 PIVALRDVVKEFRSGGRRAEGHLalagvSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVA--------RAP 371
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSGRPAVDRL-----NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgkdietnlDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 372 GAGRGAPPPVGIVFQNPYSA---LNPARTVGQTLAEAlavggqgGAQVPDLLGAVGLpaaHAQRLPAA--LSGGQRQRVA 446
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAehiLFYAQLKGRSWEEA-------QLEMEAMLEDTGL---HHKRNEEAqdLSGGMQRKLS 1071
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 447 IARALAARPELLICDEAVSALDVSVQATIIDLLrrLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:TIGR01257 1072 VAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-277 |
1.09e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 34 AIRVANPS---DPDRpIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAP--AQFTTSGTVELAGRTI-DLGVaadS 107
Cdd:PRK14258 7 AIKVNNLSfyyDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEleSEVRVEGRVEFFNQNIyERRV---N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 108 LRRLRGGGIVWLPQDPFTSLSPLHRC--GVQVIAHRqgPRSEraeraLARLAEVGLpaRAARAYPH----------QLSG 175
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVayGVKIVGWR--PKLE-----IDDIVESAL--KDADLWDEikhkihksalDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRG-----GA 250
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250 260
....*....|....*....|....*..
gi 541492527 251 IVEAGQARRVLARPATDYARQLLDAQL 277
Cdd:PRK14258 234 LVEFGLTKKIFNSPHDSRTREYVLSRL 260
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
144-305 |
1.18e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.20 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 144 PRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARG 223
Cdd:PRK11432 109 PKEERKQRVKEALELVDLAGFEDR-YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 224 MALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDY-ARQLLDAQL---RLDGPS--------PRPAGAvp 291
Cdd:PRK11432 188 ITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmASFMGDANIfpaTLSGDYvdiygyrlPRPAAF-- 265
|
170
....*....|....
gi 541492527 292 ATTVADERPIVALR 305
Cdd:PRK11432 266 AFNLPDGECTVGVR 279
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
324-528 |
1.29e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTL-ARITvGLeAPDSGTVHVA---------------RAPGAGRGAPPPVGIVFQn 387
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLlARMA-GL-LPGSGSIQFAgqpleawsaaelarhRAYLSQQQTPPFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 388 pYSALNPArtvgqtlaeALAVGGQGGAQVPDLLGAVGLpaahAQRLP---AALSGGQRQRVAIARAL-----AARPE--L 457
Cdd:PRK03695 89 -YLTLHQP---------DKTRTEAVASALNEVAEALGL----DDKLGrsvNQLSGGEWQRVRLAAVVlqvwpDINPAgqL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 458 LICDEAVSALDVSvQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLAAP 528
Cdd:PRK03695 155 LLLDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
301-516 |
1.59e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.74 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 301 IVALRDVVKEFRSGgrrAEGHLALAGVSLDILPGQSVGIVGESGSGKTTL----ARITVGLEAPdSGTVHVARAPGAGRG 376
Cdd:cd03233 3 TLSWRNISFTTGKG---RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEGNVSV-EGDIHYNGIPYKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 377 APPPVGIVFQNPYSALNPARTVGQTLAEALAVggQGGAQVpdllgavglpaahaqrlpAALSGGQRQRVAIARALAARPE 456
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPTLTVRETLDFALRC--KGNEFV------------------RGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 457 LLICDEAVSALDvsvQATIIDLLRRLQaeqgfALAFITHDLAVAR--QMS-------DRIIVMKDGAIV 516
Cdd:cd03233 139 VLCWDNSTRGLD---SSTALEILKCIR-----TMADVLKTTTFVSlyQASdeiydlfDKVLVLYEGRQI 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
50-265 |
1.66e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAI---CGLAPaQFTTSGTVELAGRTIdLGVAADSLRRLRGGGIVWLPQDPF-- 124
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNP-EVTITGSIVYNGHNI-YSPRTDTVDLRKEIGMVFQQPNPFpm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 ----TSLSPLHRCGVqviaHRQGPRSERAERALA----------RLAEVGLparaarayphQLSGGMRQRVAIAAALDAA 190
Cdd:PRK14239 101 siyeNVVYGLRLKGI----KDKQVLDEAVEKSLKgasiwdevkdRLHDSAL----------GLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 191 PGVLIADEPTTALDVTTQKEILTLLASLRDARGMalVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
316-525 |
1.73e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.53 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 316 RRAEGHLaLAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPD---SGTVHVArapgaGRgappPVGIVFQNPYSA- 391
Cdd:TIGR00955 34 ERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLN-----GM----PIDAKEMRAISAy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 392 ------LNPARTVGQTL---AE----ALAVGGQGGAQVPDLLGAVGL-PAAH----AQRLPAALSGGQRQRVAIARALAA 453
Cdd:TIGR00955 104 vqqddlFIPTLTVREHLmfqAHlrmpRRVTKKEKRERVDEVLQALGLrKCANtrigVPGRVKGLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHdlavarQMS-------DRIIVMKDGAIVEEGATEALL 525
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH------QPSselfelfDKIILMAEGRVAYLGSPDQAV 255
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-263 |
1.95e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.25 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPaqftTSGTVELAGRT---IDLgvaa 105
Cdd:COG1134 24 LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEP----TSGRVEVNGRVsalLEL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 106 dslrrlrGGGIvwlpqDPftSLSplhrcG---VQVIAHRQG-PRSE--RAERALARLAEVG----LPARaarayphQLSG 175
Cdd:COG1134 96 -------GAGF-----HP--ELT-----GrenIYLNGRLLGlSRKEidEKFDEIVEFAELGdfidQPVK-------TYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
....*...
gi 541492527 256 QARRVLAR 263
Cdd:COG1134 229 DPEEVIAA 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
436-532 |
1.98e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 436 ALSGGQRQRVAIARALAARPELLICDEAVSALDVS----VQATIIDLlrRLQAEQgfALAFITHDLAVARQmSDRIIVM- 510
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDI--KDKADK--TIITIAHRIASIKR-SDKIVVFn 1432
|
90 100
....*....|....*....|....*.
gi 541492527 511 ---KDGAIVE-EGATEALLAAPSHPY 532
Cdd:PTZ00265 1433 npdRTGSFVQaHGTHEELLSVQDGVY 1458
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
45-264 |
3.14e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.43 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRtlvIV---GESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DLGVAadslRRLRGGgIVWLP 120
Cdd:COG1137 16 RTVVKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKP---DSGRIFLDGEDItHLPMH----KRARLG-IGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDP--FTSLSplhrcgVQ-----VIAHRQGPRSERAERALARLAEVGL-PARAARAYphQLSGGMRQRVAIAAALDAAPG 192
Cdd:COG1137 85 QEAsiFRKLT------VEdnilaVLELRKLSKKEREERLEELLEEFGItHLRKSKAY--SLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 193 VLIADEPTTALDVTTQKEILTLLASLRDaRGMAlVLVT-HD----LALA-RDYgddivVMRGGAIVEAGQARRVLARP 264
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKE-RGIG-VLITdHNvretLGICdRAY-----IISEGKVLAEGTPEEILNNP 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
319-526 |
3.45e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV-----------ARAPgAGRGAPPPVGIVFQ- 386
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhARAR-RGIGYLPQEASIFRr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 -NPYSALNPARTVGQTLAEAlavggQGGAQVPDLLGAVGLpaAHAQ-RLPAALSGGQRQRVAIARALAARPELLICDEAV 464
Cdd:PRK10895 93 lSVYDNLMAVLQIRDDLSAE-----QREDRANELMEEFHI--EHLRdSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 465 SALD-VSVQ--ATIIDLLRrlqaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK10895 166 AGVDpISVIdiKRIIEHLR----DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
46-255 |
5.67e-10 |
|
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: 59.35 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdlgvAADSLRRLRgGGIVWLPQDPfT 125
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA---EEGKIEIDGIDI----STIPLEDLR-SSLTIIPQDP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVIAHrqgpRSERAERALARLAEVGLparaarayphQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDV 205
Cdd:cd03369 93 LFSGTIRSNLDPFDE----YSDEEIYGALRVSEGGL----------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 206 TT----QKEILTLLAslrdarGMALVLVTHDLALARDYgDDIVVMRGGAIVEAG 255
Cdd:cd03369 159 ATdaliQKTIREEFT------NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
324-524 |
6.85e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAgrgAPPPVGIVFQNPY-------SALNPAR 396
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVA---YVPQVSWIFNATVrenilfgSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 TVGQTLAEALAvggqggaqvPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATII 476
Cdd:PLN03232 710 YWRAIDVTALQ---------HDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 477 DLLRRlQAEQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEAL 524
Cdd:PLN03232 781 DSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-255 |
7.36e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPSDpdRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVaaDSLRRLRGg 114
Cdd:TIGR01257 935 VKIFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP---TSGTVLVGGKDIETNL--DAVRQSLG- 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 115 givWLPQDP--FTSLSPLHRcgVQVIAHRQGPRSERAERAL-ARLAEVGLPARAARAyPHQLSGGMRQRVAIAAALDAAP 191
Cdd:TIGR01257 1007 ---MCPQHNilFHHLTVAEH--ILFYAQLKGRSWEEAQLEMeAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDARgmALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
38-251 |
7.60e-10 |
|
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: 59.02 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 38 ANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDL--------GVAADS-- 107
Cdd:cd03248 20 AYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ---GGQVLLDGKPISQyehkylhsKVSLVGqe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 108 ----LRRLRGGGIVWLPQDPFTSLSPLhrcgvQVIAHRQGPRSERAERALARLAEVGlparaaraypHQLSGGMRQRVAI 183
Cdd:cd03248 97 pvlfARSLQDNIAYGLQSCSFECVKEA-----AQKAHAHSFISELASGYDTEVGEKG----------SQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASlrDARGMALVLVTHDLALArDYGDDIVVMRGGAI 251
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
51-261 |
8.43e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqfttSGTVELAGRTIDLGVAADsLRRLRGggivWLPQdpftSLSPL 130
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPLEAWSAAE-LARHRA----YLSQ----QQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 131 HRCGV-QVIA-HR-QGPRSERAERALARLAE-VGLPARAARAYpHQLSGGMRQRVAIAA-------ALDAAPGVLIADEP 199
Cdd:PRK03695 82 FAMPVfQYLTlHQpDKTRTEAVASALNEVAEaLGLDDKLGRSV-NQLSGGEWQRVRLAAvvlqvwpDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 200 TTALDVtTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVL 261
Cdd:PRK03695 161 MNSLDV-AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-292 |
8.43e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 30 LRARAIRVANPSdpdRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-----LAPAQFTTSGTVELAGRTIDlGVA 104
Cdd:PRK13547 2 LTADHLHVARRH---RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltggGAPRGARVTGDVTLNGEPLA-AID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 105 ADSLRRLRGggivWLPQD-----PFtSLSPLHRCGVQVIAHRQGPRSER----AERALARLAEVGLPARAARAyphqLSG 175
Cdd:PRK13547 78 APRLARLRA----VLPQAaqpafAF-SAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTT----LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVA---------IAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVM 246
Cdd:PRK13547 149 GELARVQfarvlaqlwPPHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 541492527 247 RGGAIVEAGQARRVLaRPATdYARQLLDAQLRLDGPSPRPAGAVPA 292
Cdd:PRK13547 229 ADGAIVAHGAPADVL-TPAH-IARCYGFAVRLVDAGDGVPPVIVPA 272
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
329-516 |
8.99e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 329 LDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGT------VHVARAPgagrgAPPP---VGIVFQ------------- 386
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdLIVARLQ-----QDPPrnvEGTVYDfvaegieeqaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 387 NPYSAL------NPARTVGQTLAEALAV-----GGQGGAQVPDLLGAVGLPAAhaQRLpAALSGGQRQRVAIARALAARP 455
Cdd:PRK11147 99 KRYHDIshlvetDPSEKNLNELAKLQEQldhhnLWQLENRINEVLAQLGLDPD--AAL-SSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 541492527 456 ELLICDEAVSALDVsvqATIIDLLRRLQAEQGfALAFITHDLAVARQMSDRIIVMKDGAIV 516
Cdd:PRK11147 176 DVLLLDEPTNHLDI---ETIEWLEGFLKTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
144-255 |
9.24e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 144 PRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRdARG 223
Cdd:PRK13631 148 KKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANN 226
|
90 100 110
....*....|....*....|....*....|..
gi 541492527 224 MALVLVTHDLALARDYGDDIVVMRGGAIVEAG 255
Cdd:PRK13631 227 KTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
44-263 |
9.88e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLgvAADSLRRLRgGGIVWLPQDP 123
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ---KGAVLWQGKPLDY--SKRGLLALR-QQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 -----FTSLS-----PLHRCGVqviahrqgprserAERALARLAEVGLPARAARAYPHQ----LSGGMRQRVAIAAALDA 189
Cdd:PRK13638 87 eqqifYTDIDsdiafSLRNLGV-------------PEAEITRRVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRdARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
45-238 |
1.12e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.27 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTidLGVAADSLRRlrggGIVWLPQDPF 124
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP---LAGRVLLNGGP--LDFQRDSIAR----GLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 --TSLSPLHRCgvqVIAHRQGPRsERAERALARLAEVGLPARAAraypHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03231 84 ikTTLSVLENL---RFWHADHSD-EQVEEALARVGLNGFEDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 541492527 203 LDVTTQKEILTLLASLRDARGMALVLVTHDLALARD 238
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
322-515 |
1.34e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGApppvgivfQNPYSALNPARTVGQT 401
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFA--------QHQLEFLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 402 LAE-ALAVGGQggaQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLR 480
Cdd:PRK10636 398 LARlAPQELEQ---KLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
170 180 190
....*....|....*....|....*....|....*
gi 541492527 481 RLQAeqgfALAFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:PRK10636 475 DFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
333-513 |
1.37e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 333 PGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagrgapppvgivfqnpysaLNPARTVGQTLAEALAVGGQG 412
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------IDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 413 GaqvpdllgavglpaahaqrlPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLR-----RLQAEQG 487
Cdd:smart00382 57 K--------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKN 116
|
170 180 190
....*....|....*....|....*....|.
gi 541492527 488 FALAFITHDL-----AVARQMSDRIIVMKDG 513
Cdd:smart00382 117 LTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
44-264 |
1.43e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.89 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG---LAPaQFTTSGTVELAGRTI-DLGVAADSLRRLRGggivWL 119
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIP-GARVEGEILLDGEDIyDPDVDVVELRRRVG----MV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 PQ--DPFtslsP------------LHrcgvqviahrqGPRS-----ERAERALARLA---EVG--LPARAARayphqLSG 175
Cdd:COG1117 98 FQkpNPF----PksiydnvayglrLH-----------GIKSkseldEIVEESLRKAAlwdEVKdrLKKSALG-----LSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 176 GMRQRVAIAAALDAAPGVLIADEPTTALD-VTTQKeILTLLASLRDArgMALVLVTHDLALARDYGDDIVVMRGGAIVEA 254
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEF 234
|
250
....*....|
gi 541492527 255 GQARRVLARP 264
Cdd:COG1117 235 GPTEQIFTNP 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
44-232 |
1.89e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGrtidlgvaadslrrlrgggivwlpqD 122
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSP----TSGTLLFEG-------------------------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSLSPlHRCGVQVIAHRQGP-----------------RSERAERA--LARLAEVGLPARAARAYPHQLSGGMRQRVAI 183
Cdd:PRK10247 70 DISTLKP-EIYRQQVSYCAQTPtlfgdtvydnlifpwqiRNQQPDPAifLDDLERFALPDTILTKNIAELSGGEKQRISL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHD 232
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
43-250 |
1.90e-09 |
|
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: 57.73 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 43 PDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGlapAQFTTSGTVELAGRTIDLGVAADSLRRLRGGgIVWLPQD 122
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNKNESEPSFEATRSRNRYS-VAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PF----------TSLSPLHR---------CGVQ----VIAHrqGPRSERAERALarlaevglparaarayphQLSGGMRQ 179
Cdd:cd03290 88 PWllnatveeniTFGSPFNKqrykavtdaCSLQpdidLLPF--GDQTEIGERGI------------------NLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 541492527 180 RVAIAAALDAAPGVLIADEPTTALDVTTQKEILT--LLASLRDARgMALVLVTHDLALArDYGDDIVVMRGGA 250
Cdd:cd03290 148 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYL-PHADWIIAMKDGS 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
279-526 |
2.11e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 279 LDGPSPRPAgavpatTVADERPI--------VALRDVVKEFRSGGRRAeghlaLAGVSLDILPGQSVGIVGESGSGKTTL 350
Cdd:PLN03232 1210 IDLPSEATA------IIENNRPVsgwpsrgsIKFEDVHLRYRPGLPPV-----LHGLSFFVSPSEKVGVVGRTGAGKSSM 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 351 ------------ARITV-GLEAPDSGTVHVARAPGAGRGAPppvgIVFQ-------NPYSALNPArtvgqTLAEALAvgg 410
Cdd:PLN03232 1279 lnalfrivelekGRIMIdDCDVAKFGLTDLRRVLSIIPQSP----VLFSgtvrfniDPFSEHNDA-----DLWEALE--- 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 411 qgGAQVPDLL--GAVGLPAAHAQRlPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRrlQAEQGF 488
Cdd:PLN03232 1347 --RAHIKDVIdrNPFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSC 1421
|
250 260 270
....*....|....*....|....*....|....*...
gi 541492527 489 ALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PLN03232 1422 TMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
269-365 |
2.27e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.81 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 269 ARQLLDAQLRLDGPSPRPAGAVPATTVADERPIvALRDVvkEFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKT 348
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPADFQTL-ELRGV--TYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKS 372
|
90
....*....|....*..
gi 541492527 349 TLARITVGLEAPDSGTV 365
Cdd:COG4615 373 TLAKLLTGLYRPESGEI 389
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
323-519 |
2.36e-09 |
|
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: 56.56 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 323 ALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEApdsgtvhvARAPGAGRGAPPPVGIVFqnpysalnpartVGQtL 402
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASG--------KARLISFLPKFSRNKLIF------------IDQ-L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 403 AEALAVGgqggaqvpdlLGAVGLpaahaQRLPAALSGGQRQRVAIARALAARPE--LLICDEAVSALDVSVQATIIDLLR 480
Cdd:cd03238 69 QFLIDVG----------LGYLTL-----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 541492527 481 RLqAEQGFALAFITHDLAVARQmSDRIIVMKDGA------IVEEG 519
Cdd:cd03238 134 GL-IDLGNTVILIEHNLDVLSS-ADWIIDFGPGSgksggkVVFSG 176
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
44-263 |
2.82e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAaPGRTLV-IVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTidlgVAADSLRRLRGGgIVWLPQD 122
Cdd:PRK10790 353 DNLVLQNINLSV-PSRGFVaLVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRP----LSSLSHSVLRQG-VAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTsLSPLHRCGVQViahrqgPRSERAERALARLAEVGLpARAARAYP-----------HQLSGGMRQRVAIAAALDAAP 191
Cdd:PRK10790 424 PVV-LADTFLANVTL------GRDISEEQVWQALETVQL-AELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 192 GVLIADEPTTALDVTTQKEILTLLASLRDArgMALVLVTHDLALARDyGDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
56-255 |
6.91e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 56 APGRTLVIVGESGAGKSMLARAICGLAPAQ--FTTSGtVELagRTIDLgvaaDSLRRLrgggIVWLPQDPftSLspLHRC 133
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGFLPYQgsLKING-IEL--RELDP----ESWRKH----LSWVGQNP--QL--PHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 134 GVQVIAHRQGPRSERAERALARLAEV-----GLPA--------RAARayphqLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVseflpLLPQgldtpigdQAAG-----LSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 201 TALDVTTQKEILTLLASLrdARGMALVLVTHDLALARDYgDDIVVMRGGAIVEAG 255
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
270-545 |
6.95e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 270 RQLLDAQLRLDGPSPRPAGAV---PAT-TVADERPIVA----LRDVVKEFRSGGRraeghLALAGVSLDILPGQSVGIVG 341
Cdd:PTZ00243 1269 DEEVDALERRTGMAADVTGTVviePASpTSAAPHPVQAgslvFEGVQMRYREGLP-----LVLRGVSFRIAPREKVGIVG 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 342 ESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRG-----------APPPV---GIVFQN--PYSALNPARtvgqtLAEA 405
Cdd:PTZ00243 1344 RTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlrelrrqfsmiPQDPVlfdGTVRQNvdPFLEASSAE-----VWAA 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 406 LavggqggaqvpDLLGAVGLPAAHAQRLPAAL-------SGGQRQRVAIARALAARPELLIC-DEAVS----ALDVSVQA 473
Cdd:PTZ00243 1419 L-----------ELVGLRERVASESEGIDSRVleggsnySVGQRQLMCMARALLKKGSGFILmDEATAnidpALDRQIQA 1487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 474 TIidllrrLQAEQGFALAFITHDLAVARQMsDRIIVMKDGAIVEEGATEALLAAPSHPYTaSLIDAVPGRGA 545
Cdd:PTZ00243 1488 TV------MSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQSIFH-SMVEALGRSEA 1551
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
302-526 |
7.64e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 302 VALRDVVKEFRSggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAP--- 378
Cdd:PLN03130 1238 IKFEDVVLRYRP-----ELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlr 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 PPVGIVFQ-------------NPYSALNPArtvgqTLAEALAvggqgGAQVPDLL--GAVGLPAAHAQRlPAALSGGQRQ 443
Cdd:PLN03130 1313 KVLGIIPQapvlfsgtvrfnlDPFNEHNDA-----DLWESLE-----RAHLKDVIrrNSLGLDAEVSEA-GENFSVGQRQ 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 444 RVAIARALAARPELLICDEAVSALDVSVQATIIDLLRrlQAEQGFALAFITHDLAVARQmSDRIIVMKDGAIVEEGATEA 523
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR--EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPEN 1458
|
...
gi 541492527 524 LLA 526
Cdd:PLN03130 1459 LLS 1461
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
44-255 |
9.36e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.61 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLaPAQFTTSGTVELAGRTI-DLGVaadSLRRLRGGGIVWlpQD 122
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGEDItDLPP---EERARLGIFLAF--QY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSlsPlhrcGVQVIAhrqgprseraeraLARLAEVGLparaarayphqlSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:cd03217 86 PPEI--P----GVKNAD-------------FLRYVNEGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 203 LDVTTQKEILTLLASLRDaRGMALVLVTHDLALArDY--GDDIVVMRGGAIVEAG 255
Cdd:cd03217 135 LDIDALRLVAEVINKLRE-EGKSVLIITHYQRLL-DYikPDRVHVLYDGRIVKSG 187
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
324-534 |
9.98e-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: 56.46 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLA------------RITVGLEAPDSGTVHVARAPgagrgapppVGIVFQNP--Y 389
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffrmvdifdgKIVIDGIDISKLPLHTLRSR---------LSIILQDPilF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 390 SA-----LNPART-VGQTLAEALAVggqggAQVPDLLGAV--GLPAAHAQRlPAALSGGQRQRVAIARALAARPELLICD 461
Cdd:cd03288 108 SGsirfnLDPECKcTDDRLWEALEI-----AQLKNMVKSLpgGLDAVVTEG-GENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 462 EAVSALDVSVQATIIDLLRRLQAEQG-FALAFITHDLAVArqmsDRIIVMKDGAIVEEGATEALLAAPSHPYTA 534
Cdd:cd03288 182 EATASIDMATENILQKVVMTAFADRTvVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLLAQEDGVFAS 251
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
46-255 |
1.11e-08 |
|
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: 55.58 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTI-DLGvaadsLRRLRGG-GIVwlPQDP 123
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---SSGSILIDGVDIsKIG-----LHDLRSRiSII--PQDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 FT-------SLSPLHRCGvqviahrqgprSERAERALAR--LAEV------GLPARAARAyPHQLSGGMRQRVAIAAALD 188
Cdd:cd03244 88 VLfsgtirsNLDPFGEYS-----------DEELWQALERvgLKEFveslpgGLDTVVEEG-GENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 189 AAPGVLIADEPTTALDVTTQKEIltlLASLRDARGMALVL-VTHDLALARDYgDDIVVMRGGAIVEAG 255
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALI---QKTIREAFKDCTVLtIAHRLDTIIDS-DRILVLDKGRVVEFD 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
50-248 |
1.21e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDlgvaadslRRLRGGGIVWLPQDPFTSLSP 129
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRL---ASGKISILGQPTR--------QALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 LHRCGVQVIAHRQG-------PRSERAERALARLAEVGLPARAARAYpHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK15056 94 PVLVEDVVMMGRYGhmgwlrrAKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 203 LDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRG 248
Cdd:PRK15056 173 VDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
46-237 |
1.24e-08 |
|
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: 55.80 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLApaqFTTSGTVELAGRTidlgVAADSLRRLRGGGIV-------- 117
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL---QPTSGEVRVAGLV----PWKRRKKFLRRIGVVfgqktqlw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 WlpqdpftSLSPLHrcGVQVIAHRQGPRSERAERALARLAE-------VGLPARaarayphQLSGGMRQRVAIAAALDAA 190
Cdd:cd03267 108 W-------DLPVID--SFYLLAAIYDLPPARFKKRLDELSElldleelLDTPVR-------QLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 191 PGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDL----ALAR 237
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkdieALAR 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-236 |
1.44e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIdlgvaadslRRLRG---GGIVWL- 119
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP---DAGEVLWQGEPI---------RRQRDeyhQDLLYLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 120 ----------PQDPFTSLSPLHRCGvqviahrqgprseRAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDA 189
Cdd:PRK13538 81 hqpgikteltALENLRFYQRLHGPG-------------DDEALWEALAQVGL-AGFEDVPVRQLSAGQQRRVALARLWLT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTLLASLRDARGMAlVLVTH-DLALA 236
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTHqDLPVA 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
299-519 |
1.73e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 299 RPIVALRDVVkeFRSGgrRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagRGAP 378
Cdd:PRK13545 19 KPFDKLKDLF--FRSK--DGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-------KGSA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 379 PPVGIvfqnpYSALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLPAAHAQRLPAAL---SGGQRQRVAIARALAARP 455
Cdd:PRK13545 88 ALIAI-----SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVktySSGMKSRLGFAISVHINP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 456 ELLICDEAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEG 519
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
330-509 |
2.31e-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: 53.73 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 330 DILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagrgapPPVGIVFQNPYsalnpartvgqtlaealavg 409
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-----------DGITPVYKPQY-------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 410 gqggaqvpdllgavglpaahaqrlpAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFA 489
Cdd:cd03222 70 -------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|
gi 541492527 490 LAFITHDLAVARQMSDRIIV 509
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHV 144
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
48-234 |
2.63e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.86 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKS----MLaraiCG-LAPaqftTSGTVELAGRT-----IDLgvaadsLRRLrggGIV 117
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSttikML----TGiLVP----TSGEVRVLGYVpfkrrKEF------ARRI---GVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 118 --------W-LP-QDPFTslspLHRC--GVqviahrqgPRSERAERaLARLAEV-GL------PARaarayphQLSGGMR 178
Cdd:COG4586 101 fgqrsqlwWdLPaIDSFR----LLKAiyRI--------PDAEYKKR-LDELVELlDLgelldtPVR-------QLSLGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 179 QRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLA 234
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
44-303 |
3.09e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPAQFTtsGTVELAGRTIdlgvAADSLRRlrgggIVWLPQD 122
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFT--GTILANNRKP----TKQILKR-----TGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 123 PFTSLSPLHRCGVQVIAHRQGPRS----ERAERALARLAEVGLP----ARAARAYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:PLN03211 149 DILYPHLTVRETLVFCSLLRLPKSltkqEKILVAESVISELGLTkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLAlARDYG--DDIVVMRGGAIVEAGQARRVLA---------- 262
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPS-SRVYQmfDSVLVLSEGRCLFFGKGSDAMAyfesvgfsps 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 541492527 263 ---RPAtDYARQLLDAQLRLDGPSPRPAGAVPATTVADERPIVA 303
Cdd:PLN03211 307 fpmNPA-DFLLDLANGVCQTDGVSEREKPNVKQSLVASYNTLLA 349
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
45-262 |
3.44e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.51 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 45 RPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQDP- 123
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDISLLPLHARARR----GIGYLPQEAs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 -FTSLSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLpARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:PRK10895 89 iFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 203 LDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLA 262
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
48-249 |
3.57e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.61 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARAICGL-APaqftTSGTVELAGRTIDlGVAADSLRRLrggGIVWLPQDP--F 124
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFyKP----TGGTILLRGQHIE-GLPGHQIARM---GVVRTFQHVrlF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 TSLSPLHRcgVQVIAHRQ-----------GPRSERAER-ALAR----LAEVGLPARAAR-----AYPHQlsggmrQRVAI 183
Cdd:PRK11300 93 REMTVIEN--LLVAQHQQlktglfsgllkTPAFRRAESeALDRaatwLERVGLLEHANRqagnlAYGQQ------RRLEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGG 249
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
333-468 |
8.83e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 333 PGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgaGRGAPPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQG 412
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT--ATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRR 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 413 GAQVP-DLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALD 468
Cdd:PRK13543 114 AKQMPgSALAIVGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
310-527 |
9.74e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 310 EFR--SGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLA----RITV---------GLEAPDSGtVHVARAPgag 374
Cdd:TIGR00957 1286 EFRnyCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTlglfRINEsaegeiiidGLNIAKIG-LHDLRFK--- 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 375 rgapppVGIVFQNP--YSA-----LNP-ARTVGQTLAEALAVggqggAQVPDLLGAvgLPAAHAQRLPAA---LSGGQRQ 443
Cdd:TIGR00957 1362 ------ITIIPQDPvlFSGslrmnLDPfSQYSDEEVWWALEL-----AHLKTFVSA--LPDKLDHECAEGgenLSVGQRQ 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 444 RVAIARALAARPELLICDEAVSALDVS----VQATIidllrRLQAEQGFALAfITHDLAVARQMSdRIIVMKDGAIVEEG 519
Cdd:TIGR00957 1429 LVCLARALLRKTKILVLDEATAAVDLEtdnlIQSTI-----RTQFEDCTVLT-IAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
....*...
gi 541492527 520 ATEALLAA 527
Cdd:TIGR00957 1502 APSNLLQQ 1509
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
320-525 |
1.20e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGlEAPDSGTVHVARAPG-----------------AGRGAPPPVG 382
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPRGARVTGdvtlngeplaaidaprlARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 383 IVFQNPYSALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALA---------A 453
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 541492527 454 RPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALL 525
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
331-514 |
1.32e-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: 54.63 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 331 ILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVArapgaGRGAPPPVGIVFQN-----PYSALNPARTVGQTLAEA 405
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA-----GKSILTNISDVHQNmgycpQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 406 LAVGGQGGAQVPDL----LGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQA----TIID 477
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVanwsIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnTIVS 2115
|
170 180 190
....*....|....*....|....*....|....*..
gi 541492527 478 LLRrlqaeQGFALAFITHDLAVARQMSDRIIVMKDGA 514
Cdd:TIGR01257 2116 IIR-----EGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-258 |
1.49e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 37 VANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTtSGTVELAGRTIDLgvaaDSLRRLRGGGI 116
Cdd:NF040905 265 VYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNI-SGTVFKDGKEVDV----STVSDAIDAGL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 117 VWLPQD-------------PFTSLSPLHRcgvqvIAHRqGPRSERAERALAR-------------LAEVGlparaarayp 170
Cdd:NF040905 340 AYVTEDrkgyglnliddikRNITLANLGK-----VSRR-GVIDENEEIKVAEeyrkkmniktpsvFQKVG---------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 171 hQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDArGMALVLVTHDLALARDYGDDIVVMRGGA 250
Cdd:NF040905 404 -NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGR 481
|
250
....*....|....
gi 541492527 251 IV------EAGQAR 258
Cdd:NF040905 482 ITgelpreEASQER 495
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-299 |
1.53e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLHRCGVQVIAHRQGPRSeRAERALARLAEVGLPARAARAYphqlSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARA-RADELLERFSLTEAAGRAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 201 TALDVTTQKEILTLLASL-RDarGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQ---------ARRVLARPAtdYAR 270
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMvRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKvdelktkvgGRTLQIRPA--HAA 248
|
170 180 190
....*....|....*....|....*....|....*...
gi 541492527 271 QL-----LDAQLRLDGPSPRPA----GAVPATTVADER 299
Cdd:NF000106 249 ELdrmvgAIAQAGLDGIAGATAdhedGVVNVPIVSDEQ 286
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
328-526 |
1.87e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 328 SLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTV-----HVARapgagrgapppvgIVFQ------------NPYS 390
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfsHITR-------------LSFEqlqklvsdewqrNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALNPART-VGQTLAEALAVGGQGGAQVPDLLGAVGLPAAHAQRLpAALSGGQRQRVAIARALAARPELLICDEAVSALDV 469
Cdd:PRK10938 90 MLSPGEDdTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRF-KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 470 SVQATIIDLLRRLQAeQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:PRK10938 169 ASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
49-547 |
1.93e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 54.11 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 49 ADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDLGVAAD--SLRRLRGGGIVWLPQDPFTS 126
Cdd:COG3321 791 VRVFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDwsALYPGRGRRRVPLPTYPFQR 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LSPLHRCGVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVT 206
Cdd:COG3321 871 EDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAA 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 207 TQKEILTLLASLRDARGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYARQLLDAQLRLDGPSPRP 286
Cdd:COG3321 951 AAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAA 1030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 287 AGAVPATTVADERPIVALRDVVKEFRSGGRRAEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVH 366
Cdd:COG3321 1031 AAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLA 1110
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 367 VARAPGAGRGAPPPVGIVFQNPYSALNPARTVGQTLAEALAVGGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVA 446
Cdd:COG3321 1111 LLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALA 1190
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 447 IARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEALLA 526
Cdd:COG3321 1191 GLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAG 1270
|
490 500
....*....|....*....|.
gi 541492527 527 APSHPYTASLIDAVPGRGAPA 547
Cdd:COG3321 1271 LAALAAAAAAAAAALALAAAA 1291
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
333-510 |
2.38e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 333 PGQSVGIVGESGSGKTTLARITvgleapdSGTVhvarAPGAGRGAPPP-------------------------VGIVFQN 387
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGKL----KPNLGKFDDPPdwdeildefrgselqnyftkllegdVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 388 PYSALNPARTVGQTLaEALAVGGQGGAQ--VPDLLGAVGLpaahAQRLPAALSGGQRQRVAIARALAARPELLICDEAVS 465
Cdd:cd03236 94 QYVDLIPKAVKGKVG-ELLKKKDERGKLdeLVDQLELRHV----LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 541492527 466 ALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVM 510
Cdd:cd03236 169 YLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
435-501 |
2.60e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 435 AALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQGFALAFITHDLAVAR 501
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
172-263 |
2.95e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 172 QLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLrdARGMALVLVTHDLaLARDYGDDIVVMRGGAI 251
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRL-TGLEQFDRICVMDNGQI 551
|
90
....*....|..
gi 541492527 252 VEAGQARRVLAR 263
Cdd:PRK11160 552 IEQGTHQELLAQ 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
44-263 |
3.38e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIDlgvaADSLRRLRgggivwlpqdp 123
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID---EGEILLDGHDLR----DYTLASLR----------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftslsplHRCGV---QV----------IAHRQGPRSERAERALArlaevglpARAARA------YPH-----------QL 173
Cdd:PRK11176 417 -------NQVALvsqNVhlfndtiannIAYARTEQYSREQIEEA--------ARMAYAmdfinkMDNgldtvigengvLL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 174 SGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARgMALVlVTHDLALARDyGDDIVVMRGGAIVE 253
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTIEK-ADEILVVEDGEIVE 558
|
250
....*....|
gi 541492527 254 AGQARRVLAR 263
Cdd:PRK11176 559 RGTHAELLAQ 568
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
304-517 |
4.15e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVkeFRSGgrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgagrgapppVGI 383
Cdd:PRK10522 325 LRNVT--FAYQ----DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---------VTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 384 VFQNPYSALNPARTVGQTLAEALAvgGQGGAQVPDLLGAVGLpaahaQRLPAA--------------LSGGQRQRVAIAR 449
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLFDQLL--GPEGKPANPALVEKWL-----ERLKMAhkleledgrisnlkLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 450 ALAARPELLICDEAVSALDVSVQATII-DLLRRLQaEQGFALAFITHDLAVArQMSDRIIVMKDGAIVE 517
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYqVLLPLLQ-EMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
299-524 |
5.14e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 299 RPIVALRDVVKEFrsggrraeGHL-ALAGVSLDILPGQSVGIVGESGSGKTTLArITVGLEAPDSGT--------VHVAR 369
Cdd:NF000106 11 RNAVEVRGLVKHF--------GEVkAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpwrf*twCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 370 APGAGRGAPPPVGIVFQNPYSALNPARTVGQTLAEALAvggQGGAQVPDLLGAVGLPAAhAQRLPAALSGGQRQRVAIAR 449
Cdd:NF000106 82 ALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRK---DARARADELLERFSLTEA-AGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 450 ALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDGAIVEEGATEAL 524
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
319-495 |
5.23e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.44 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 319 EGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVarapgagrgaPPPVGIVF--QNPYSALNPAR 396
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----------PAKGKLFYvpQRPYMTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 T----------------VGQTLAEALAVggqggAQVPDLLG-AVGLPAAhaQRLPAALSGGQRQRVAIARALAARPELLI 459
Cdd:TIGR00954 533 DqiiypdssedmkrrglSDKDLEQILDN-----VQLTHILErEGGWSAV--QDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 541492527 460 CDEAVSALDVSVQATIIDLLRRLqaeqGFALAFITH 495
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
437-510 |
5.24e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 5.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 437 LSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVM 510
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
321-501 |
7.60e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 321 HLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGAPPPVGIVFQNPYSALNPARTVGQ 400
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 401 TLAEALAVGgQGGAQVPDLLGAVGLpaAHAQRLPAAL-SGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLL 479
Cdd:PRK13540 94 NCLYDIHFS-PGAVGITELCRLFSL--EHLIDYPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170 180
....*....|....*....|..
gi 541492527 480 RRLQAEQGFALAFITHDLAVAR 501
Cdd:PRK13540 171 QEHRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
436-521 |
8.52e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 436 ALSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQMSDRIIVMKDG-- 513
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGlv 469
|
....*....
gi 541492527 514 -AIVEEGAT 521
Cdd:PRK10982 470 aGIVDTKTT 478
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-350 |
8.64e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 153 LARLAEVGLP----ARAARAyphqLSGGMRQRVAIAAAL-DAAPGVL-IADEPTTALDvttQKEILTLLASLRDAR--GM 224
Cdd:TIGR00630 469 LGFLIDVGLDylslSRAAGT----LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLH---QRDNRRLINTLKRLRdlGN 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 225 ALVLVTHD--LALARDYGDDI---VVMRGGAIVEAGQARRVLARPATdYARQLLDAQLRLDGPSPRpagavpatTVADER 299
Cdd:TIGR00630 542 TLIVVEHDedTIRAADYVIDIgpgAGEHGGEVVASGTPEEILANPDS-LTGQYLSGRKKIEVPAER--------RPGNGK 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 541492527 300 PIVAlrdvvkefrsggRRAEGHlALAGVSLDILPGQSVGIVGESGSGKTTL 350
Cdd:TIGR00630 613 FLTL------------KGAREN-NLKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
44-276 |
1.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPAqfttSGTVELAgRTIDLG-VAADSLRRLRGGgivwlpQ 121
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPV----SGEIGLA-KGIKLGyFAQHQLEFLRAD------E 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 122 DPFTSLSplhrcgvqviahRQGPRsERAERALARLAEVGLPARAARAYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTT 201
Cdd:PRK10636 393 SPLQHLA------------RLAPQ-ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 202 ALDVTTQKeilTLLASLRDARGmALVLVTHDLALARDYGDDIVVMRGGAIveagqarRVLARPATDYARQLLDAQ 276
Cdd:PRK10636 460 HLDLDMRQ---ALTEALIDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV-------EPFDGDLEDYQQWLSDVQ 523
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
48-236 |
1.51e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 48 VADVSVDAAPGRTLVIVGESGAGKSMLARA---ICGLAPAqFTTSGTVELAGRTI-DLGVAADSLRRLRGggIVWLPQDP 123
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPG-FRVEGKVTFHGKNLyAPDVDPVEVRRRIG--MVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 F-TSLSPLHRCGVQVIAHrQGPRSERAERALARLA---EVGLPARAARAyphQLSGGMRQRVAIAAALDAAPGVLIADEP 199
Cdd:PRK14243 103 FpKSIYDNIAYGARINGY-KGDMDELVERSLRQAAlwdEVKDKLKQSGL---SLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 541492527 200 TTALDVTTQKEILTLLASLRdaRGMALVLVTHDLALA 236
Cdd:PRK14243 179 CSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQA 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
149-516 |
1.77e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 149 AE-RALARLAEVGLPAraaraypHQLSGGMRQ-------RVAIAAALDAAPGVLIADEPTTALDVTTqkeiLTLLASLRD 220
Cdd:PRK15064 131 AEaRAGELLLGVGIPE-------EQHYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 221 ARGMALVLVTHDlalaR-------------DYGDdIVVMRGGA---IVEAGQARRVL----------------------- 261
Cdd:PRK15064 200 ERNSTMIIISHD----RhflnsvcthmadlDYGE-LRVYPGNYdeyMTAATQARERLladnakkkaqiaelqsfvsrfsa 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 262 ----ARPATDYARQLLDAQLRLDGPSPRpagAVPATTVADE----RPIVALRDVVKEFrsggrraEGHLALAGVSLDILP 333
Cdd:PRK15064 275 naskAKQATSRAKQIDKIKLEEVKPSSR---QNPFIRFEQDkklhRNALEVENLTKGF-------DNGPLFKNLNLLLEA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 334 GQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPGAGRGApppvgivfQNPYSALNpartVGQTLAEALAVGGQGG 413
Cdd:PRK15064 345 GERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA--------QDHAYDFE----NDLTLFDWMSQWRQEG 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 414 ---AQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV-SVQAtiidLLRRLQAEQGfA 489
Cdd:PRK15064 413 ddeQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES----LNMALEKYEG-T 487
|
410 420
....*....|....*....|....*..
gi 541492527 490 LAFITHDLAVARQMSDRIIVMKDGAIV 516
Cdd:PRK15064 488 LIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
437-510 |
2.53e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 2.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 437 LSGGQRQRVAIARALAARPELLICDEAVSALDVSVQATIIDLLRRLQAEQgfALAFITHDLAVARQMSDRIIVM 510
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
304-513 |
3.46e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 304 LRDVVKEFrsggrraEGHLALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARAPgagrgapppvgI 383
Cdd:PRK10982 1 MSNISKSF-------PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-----------I 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 384 VFQNPYSAL-NPARTVGQTLAEALAVggqggaQVPD--LLGAV---GLPAAHAQRLP-------------------AALS 438
Cdd:PRK10982 63 DFKSSKEALeNGISMVHQELNLVLQR------SVMDnmWLGRYptkGMFVDQDKMYRdtkaifdeldididprakvATLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 439 GGQRQRVAIARALAARPELLICDEAVSAL---DVSVQATIIDLLRrlqaEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:PRK10982 137 VSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
331-508 |
4.14e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 331 ILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVaraPGAGRGA----------PPPVGIV------FQNPYSALNP 394
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---PGNWQLAwvnqetpalpQPALEYVidgdreYRQLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 395 ARTVGQTLAEALAVGGQGG-------AQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSAL 467
Cdd:PRK10636 101 ANERNDGHAIATIHGKLDAidawtirSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 541492527 468 DVSvqaTIIDLLRRLQAEQGfALAFITHDLAVARQMSDRII 508
Cdd:PRK10636 181 DLD---AVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKII 217
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
515-547 |
4.32e-06 |
|
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: 45.05 E-value: 4.32e-06
10 20 30
....*....|....*....|....*....|...
gi 541492527 515 IVEEGATEALLAAPSHPYTASLIDAVPGRGAPA 547
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTIKKRD 34
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-249 |
5.29e-06 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 47.46 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 40 PSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRtidLGVAA-------DSLRrlr 112
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK---LSGSVSVPGS---IAYVSqepwiqnGTIR--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 113 gGGIVW-LPQDPFTSLSPLHRCG----VQVIAHrqGPRSERAERALArlaevglparaarayphqLSGGMRQRVAIAAAL 187
Cdd:cd03250 84 -ENILFgKPFDEERYEKVIKACAlepdLEILPD--GDLTEIGEKGIN------------------LSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 188 DAAPGVLIADEPTTALDVTTQKEILT--LLASLRDARgmALVLVTHDLALARdYGDDIVVMRGG 249
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLP-HADQIVVLDNG 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
322-526 |
7.18e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 322 LALAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHV---------ARAPGAGRGAPPPVGI--------- 383
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmadarHRRAVCPRIAYMPQGLgknlyptls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 384 VFQNpysaLN-PARTVGQTLAEAlavggqgGAQVPDLLGAVGLpAAHAQRLPAALSGGQRQRVAIARALAARPELLICDE 462
Cdd:NF033858 95 VFEN----LDfFGRLFGQDAAER-------RRRIDELLRATGL-APFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 463 AVSALDVSVQATIIDLLRRLQAEQGfalafithdlavarQMS--------------DRIIVMKDGAIVEEGATEALLA 526
Cdd:NF033858 163 PTTGVDPLSRRQFWELIDRIRAERP--------------GMSvlvataymeeaerfDWLVAMDAGRVLATGTPAELLA 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
169-254 |
8.18e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 169 YPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARDyGDDIVVM-- 246
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnn 1433
|
90
....*....|
gi 541492527 247 --RGGAIVEA 254
Cdd:PTZ00265 1434 pdRTGSFVQA 1443
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-285 |
9.57e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 34 AIRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLaraiCGLAPAQF-TTSGTVELAGRTIDlGVAADSLRrlr 112
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTL----LSLIQRHFdVSEGDIRFHDIPLT-KLQLDSWR--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 113 gGGIVWLPQDPFtslspLHRCGV-QVIA-HRQGPRSERAERAlARLAEVG-----LParaaRAYPHQ-------LSGGMR 178
Cdd:PRK10789 389 -SRLAVVSQTPF-----LFSDTVaNNIAlGRPDATQQEIEHV-ARLASVHddilrLP----QGYDTEvgergvmLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 179 QRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARgmALVLVTHDLALARDyGDDIVVMRGGAIVEAGQAR 258
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGNHD 534
|
250 260 270
....*....|....*....|....*....|
gi 541492527 259 RVLARPA---TDYARQLLDAQLRlDGPSPR 285
Cdd:PRK10789 535 QLAQQSGwyrDMYRYQQLEAALD-DAPEIR 563
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-519 |
1.22e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVG-LEAPD-SGTVHVArapgaGRGAPPPV----GIVFQNpySALNPART 397
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILAN-----NRKPTKQIlkrtGFVTQD--DILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 398 VGQTL--AEALAVGGQGGAQVPDLLG-----AVGLPAAH----AQRLPAALSGGQRQRVAIARALAARPELLICDEAVSA 466
Cdd:PLN03211 157 VRETLvfCSLLRLPKSLTKQEKILVAesvisELGLTKCEntiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 541492527 467 LDVSVQATIIDLLRRLqAEQGFALAFITHDLAV-ARQMSDRIIVMKDGAIVEEG 519
Cdd:PLN03211 237 LDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
324-513 |
1.30e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTL-----ARITVGLEAPDSGTVHvarapGAGRGA--PPPVGIVFQNPYSAlnPAR 396
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGVITGGDRLVN-----GRPLDSsfQRSIGYVQQQDLHL--PTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 397 TVGQTLAEALAVggQGGAQVP------------DLLG-------AVGLPAAhaqrlpaALSGGQRQRVAIARALAARPEL 457
Cdd:TIGR00956 852 TVRESLRFSAYL--RQPKSVSksekmeyveeviKLLEmesyadaVVGVPGE-------GLNVEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 458 LI-CDEAVSALDVSVQATIIDLLRRLqAEQGFA-LAFITHDLAVARQMSDRIIVMKDG 513
Cdd:TIGR00956 923 LLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAiLCTIHQPSAILFEEFDRLLLLQKG 979
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-252 |
1.71e-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: 45.72 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 35 IRVANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVELAGRTIDlgvaaDSLRRLRGG 114
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYK-----EFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 115 GIvwlpqdpFTSLSPLHRcgvqviahrqgprserAERALARLAEVGLPARAaRAYPHQLSGGMRQRVAIAAALDAAPGVL 194
Cdd:cd03233 85 II-------YVSEEDVHF----------------PTLTVRETLDFALRCKG-NEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 195 IADEPTTALDVTTQKEILTLLASLRDARGMAlVLVTHDLALARDYG--DDIVVMRGGAIV 252
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTT-TFVSLYQASDEIYDlfDKVLVLYEGRQI 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-250 |
2.26e-05 |
|
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: 47.70 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGlapAQFTTSGTVELAGRTIDLGVAadSLRRLRGggivWLPQdpFT 125
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILTNIS--DVHQNMG----YCPQ--FD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPL--HRCGVQVIAHRQGPRSERAER-ALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTA 202
Cdd:TIGR01257 2022 AIDDLltGREHLYLYARLRGVPAEEIEKvANWSIQSLGLSLYADR-LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 541492527 203 LDVTTQKEIL-TLLASLRDARgmALVLVTHDLALARDYGDDIVVMRGGA 250
Cdd:TIGR01257 2101 MDPQARRMLWnTIVSIIREGR--AVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
63-265 |
2.62e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 63 IVGESGAGKSMLARAICGLAPAQfttSGTVELAGRTIdlgvaADSLRRlrgggiVWLP----------QDpfTSLSPLHR 132
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQ---KGRIVLNGRVL-----FDAEKG------ICLPpekrrigyvfQD--ARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 133 cgvqVIAH-RQGPRSERAERALARLAEVGLPARAARaYPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEI 211
Cdd:PRK11144 93 ----VRGNlRYGMAKSMVAQFDKIVALLGIEPLLDR-YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 212 LTLLASLRDARGMALVLVTHDL----ALArdygDDIVVMRGGAIVEAGQARRVLARPA 265
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLdeilRLA----DRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
516-541 |
3.04e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 42.00 E-value: 3.04e-05
10 20
....*....|....*....|....*.
gi 541492527 516 VEEGATEALLAAPSHPYTASLIDAVP 541
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVP 26
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-263 |
3.31e-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: 46.86 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPdrPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGlapAQFTTSGTVELAGrtidlgvaadslrrlrggGIVWLP 120
Cdd:TIGR00957 649 DLP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA---EMDKVEGHVHMKG------------------SVAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLhRCGVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQ----LSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:TIGR00957 706 QQAWIQNDSL-RENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 541492527 197 DEPTTALDVTTQKEIL-TLLASLRDARGMALVLVTHDLALARDYgDDIVVMRGGAIVEAGQARRVLAR 263
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
405-511 |
3.98e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.27 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 405 ALAVGGQGGAQVPDLLGAVGL--PAAHAQRLPA--ALSGGQRQRVAIARALA----ARPELLICDEAVSALDVSVQATII 476
Cdd:cd03227 42 GLALGGAQSATRRRSGVKAGCivAAVSAELIFTrlQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALA 121
|
90 100 110
....*....|....*....|....*....|....*
gi 541492527 477 DLLRRlQAEQGFALAFITHDLAVArQMSDRIIVMK 511
Cdd:cd03227 122 EAILE-HLVKGAQVIVITHLPELA-ELADKLIHIK 154
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
47-231 |
4.37e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.28 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTvelagRTIDlgvaadslrrlRGGGIVWLPQDPFTS 126
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP---VYGGR-----LTKP-----------AKGKLFYVPQRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 127 LSPLHRcgvQVI-------AHRQGPRSERAERALARLA-------EVGLpaRAARAYPHQLSGGMRQRVAIAAALDAAPG 192
Cdd:TIGR00954 528 LGTLRD---QIIypdssedMKRRGLSDKDLEQILDNVQlthilerEGGW--SAVQDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 541492527 193 VLIADEPTTALDVTTQKEILTLlasLRDArGMALVLVTH 231
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRL---CREF-GITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
326-515 |
4.74e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 326 GVSLDilpgQSVGIVGESGSGKTTLARITVGLEAPDSGTVHvarapgagRGAPPPVGIVFQNPYSALNpaRTVGQTLAEA 405
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVRMAVFSQHHVDGLD--LSSNPLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 406 LAVGGQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAARPELLICDEAVSALDV-SVQAtiidLLRRLQA 484
Cdd:PLN03073 597 RCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEA----LIQGLVL 672
|
170 180 190
....*....|....*....|....*....|.
gi 541492527 485 EQGFALaFITHDLAVARQMSDRIIVMKDGAI 515
Cdd:PLN03073 673 FQGGVL-MVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
324-547 |
6.49e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 324 LAGVSLDILPGQSVGIVGESGSGKTTLARITVGLEAPDSGTVHVARApgagrgapppVGIVFQNP-------------YS 390
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS----------IAYVPQQAwimnatvrgnilfFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 391 ALNPARtvgqtLAEALAVGgQGGAQVPDLLGavGLPAAHAQRlPAALSGGQRQRVAIARALAARPELLICDEAVSALDVS 470
Cdd:PTZ00243 746 EEDAAR-----LADAVRVS-QLEADLAQLGG--GLETEIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 471 VQATII-DLLRRLQAEQGFALAfiTHDLAVArQMSDRIIVMKDGAIVEEGATEALLAAPSHP-YTASLIDAVPGRGAPA 547
Cdd:PTZ00243 817 VGERVVeECFLGALAGKTRVLA--THQVHVV-PRADYVVALGDGRVEFSGSSADFMRTSLYAtLAAELKENKDSKEGDA 892
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-255 |
6.71e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqfTTSGTVELAGRtidlgvaadslrrlrgggIVWLP 120
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--RSDASVVIRGT------------------VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTsLSPLHRCGVQVIAHRQGPRSERAER--ALAR---------LAEVGlpARAArayphQLSGGMRQRVAIAAALDA 189
Cdd:PLN03130 686 QVSWI-FNATVRDNILFGSPFDPERYERAIDvtALQHdldllpggdLTEIG--ERGV-----NISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 190 APGVLIADEPTTALDVTTQKEILTllASLRDA-RGMALVLVTHDLALArDYGDDIVVMRGGAIVEAG 255
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFL-SQVDRIILVHEGMIKEEG 821
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-247 |
8.99e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 57 PGRTLVIVGESGAGKSMLARAICGLAPAqfTTSGTVELAGRTIDLGVAADSLRRLRGGGivwlpqdpftslsplhrcgvq 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP--PGGGVIYIDGEDILEEVLDQLLLIIVGGK--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 137 viahrqgprseraeralarlaevglparaarayPHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEIL---- 212
Cdd:smart00382 58 ---------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLllee 104
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 541492527 213 -TLLASLRDARGMALVLVTHDL-----ALARDYGDDIVVMR 247
Cdd:smart00382 105 lRLLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLL 145
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
331-524 |
9.36e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 331 ILPGQSVGIVGESGSGKTTLARI----TVGLEAPDSGTVHVarapgagrGAPPPVGIVFQNP----YSALN----PARTV 398
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTiasnTDGFHIGVEGVITY--------DGITPEEIKKHYRgdvvYNAETdvhfPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 399 GQTLAEALAVggQGGAQVPDLLGAVGLpAAHAQRLPAA-------------------LSGGQRQRVAIARALAARPELLI 459
Cdd:TIGR00956 156 GETLDFAARC--KTPQNRPDGVSREEY-AKHIADVYMAtyglshtrntkvgndfvrgVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 460 CDEAVSALDvsvQATIIDLLRRLQaeqgfALAFITHD--LAVARQMS-------DRIIVMKDGAIVEEG-ATEAL 524
Cdd:TIGR00956 233 WDNATRGLD---SATALEFIRALK-----TSANILDTtpLVAIYQCSqdayelfDKVIVLYEGYQIYFGpADKAK 299
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
432-513 |
1.28e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 432 RLPAALSGGQRQ------RVAIARALAARPELLICDEAVSALDV-SVQATIIDLLRRLQAEQGFALAFITHDLAVARQMS 504
Cdd:cd03240 111 DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAAD 190
|
....*....
gi 541492527 505 DRIIVMKDG 513
Cdd:cd03240 191 HIYRVEKDG 199
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
386-535 |
1.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 386 QNPYSALNPARTVGQTLAEALavggQGGAQVPDLLGAVGLPAAHAQRLPAALSGGQRQRVAIARALAArpELL----ICD 461
Cdd:PRK00635 430 QELFIFLSQLPSKSLSIEEVL----QGLKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGA--ELIgityILD 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 462 EAVSALDVSVQATIIDLLRRLQaEQGFALAFITHDlavaRQM---SDRIIVMKDGA------IVEEGATEALLAApSHPY 532
Cdd:PRK00635 504 EPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEHD----EQMislADRIIDIGPGAgifggeVLFNGSPREFLAK-SDSL 577
|
...
gi 541492527 533 TAS 535
Cdd:PRK00635 578 TAK 580
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
50-255 |
1.35e-04 |
|
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: 42.70 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 50 DVSVDAAPGRTLVIVGESGAGKSMLARAiCGLAPAQFTTSGTVELAGRtiDLGVAADSLRRLRGGGIVWLPqdpftslsp 129
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNE-GLYASGKARLISFLPKFSR--NKLIFIDQLQFLIDVGLGYLT--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 130 lhrcgvqviahrqgprserAERALArlaevglparaarayphQLSGGMRQRVAIAAALDAAPG--VLIADEPTTALDvtt 207
Cdd:cd03238 81 -------------------LGQKLS-----------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH--- 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 208 QKEILTLLASLRDAR--GMALVLVTHDLALArDYGDDIVVM------RGGAIVEAG 255
Cdd:cd03238 122 QQDINQLLEVIKGLIdlGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
338-513 |
1.65e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 338 GIVGESGSGKTT-LARITVGL-----EAPDSGTVHVARAPGAGRGApppVGIVFQNpysalnpartvGQTLAEalaVGGQ 411
Cdd:cd03279 32 LICGPTGAGKSTiLDAITYALygktpRYGRQENLRSVFAPGEDTAE---VSFTFQL-----------GGKKYR---VERS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 412 GGAQVPDLLGAVGLPAAHAQRL---PAA-LSGGQRQRVAIARALA----------ARPELLICDEAVSALDVSVQATIID 477
Cdd:cd03279 95 RGLDYDQFTRIVLLPQGEFDRFlarPVStLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVAT 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 541492527 478 LLRRLQaEQGFALAFITHDLAVARQMSDRIIVMKDG 513
Cdd:cd03279 175 ALELIR-TENRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
52-239 |
4.00e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 52 SVDAAPGRTLVIVGESGAGKSMLARAICglapaqfttsgtvelagrtidLGVAADSLRRLRGGGIvwlpqdpftslsplh 131
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG---------------------LALGGAQSATRRRSGV--------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 132 RCGVQVIAhrqgprsERAERALARlaevglparaaraypHQLSGGMRQRVAIA---AALDAAPGVLIA-DEPTTALDVTT 207
Cdd:cd03227 59 KAGCIVAA-------VSAELIFTR---------------LQLSGGEKELSALAlilALASLKPRPLYIlDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|..
gi 541492527 208 QKEILTLLASLRDARGMALVlVTHDLALARDY 239
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIV-ITHLPELAELA 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-255 |
4.12e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 41 SDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFTTSGTVElagrtidlgvaadslrrlrgGGIVWLP 120
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIR--------------------GSVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLhRCGVQVIAHRQGPRSERAERALARLAEVGL-PARAARAYPHQ---LSGGMRQRVAIAAALDAAPGVLIA 196
Cdd:PLN03232 686 QVSWIFNATV-RENILFGSDFESERYWRAIDVTALQHDLDLlPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 197 DEPTTALDVTTQKEILTllASLRDA-RGMALVLVTHDLALARDYgDDIVVMRGGAIVEAG 255
Cdd:PLN03232 765 DDPLSALDAHVAHQVFD--SCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
44-204 |
5.52e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAQFttSGTVELAGRTidlgvaadslrrlRGGG-IVW---- 118
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGY--SNDLTLFGRR-------------RGSGeTIWdikk 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 119 --------LPQDPFTSLSPLH--------RCGV-QVIAHRQgprseraeRALAR--LAEVGLPARAARAYPHQLSGGMRQ 179
Cdd:PRK10938 337 higyvsssLHLDYRVSTSVRNvilsgffdSIGIyQAVSDRQ--------QKLAQqwLDILGIDKRTADAPFHSLSWGQQR 408
|
170 180
....*....|....*....|....*
gi 541492527 180 RVAIAAALDAAPGVLIADEPTTALD 204
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLD 433
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
51-269 |
6.67e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.40 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 51 VSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELAGRTIDLGVAADSLRRlrggGIVWLPQ-----DPFT 125
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRA---TSGRIVFDGKDITDWQTAKIMRE----AVAIVPEgrrvfSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 126 SLSPLHRCGVQVIAHRQGPRSERAERALARLAEvglpARAARAypHQLSGGMRQRVAIAAALDAAPGVLIADEPTTALDV 205
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIKWVYELFPRLHE----RRIQRA--GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 206 TTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGGAIVEAGQARRVLARPATDYA 269
Cdd:PRK11614 171 IIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-212 |
6.84e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.59 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 46 PIVADVSVDAAPGRTLVIVGESGAGKSMLARAICG-LAPAQ--FTTSGTVELAGRT--IDLGVAADSLrrlrgggIVWLP 120
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEgkIKHSGRISFSPQTswIMPGTIKDNI-------IFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 121 QDPFTSLSPLHRCGVQviahrqGPRSERAERALARLAEVGLparaarayphQLSGGMRQRVAIAAALDAAPGVLIADEPT 200
Cdd:TIGR01271 513 YDEYRYTSVIKACQLE------EDIALFPEKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170
....*....|..
gi 541492527 201 TALDVTTQKEIL 212
Cdd:TIGR01271 577 THLDVVTEKEIF 588
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-269 |
1.06e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.24 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 47 IVADVSVDAAPGRTLVIVGESGAGKSMLAraiCGLAPAQFTTSGTVELAGrtidLGVAADSLRRLRGGgIVWLPQDPF-- 124
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG----LNIAKIGLHDLRFK-ITIIPQDPVlf 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 125 -----TSLSPLHRCGVQVI------AHRQGPRSERAERALARLAEVGlparaaraypHQLSGGMRQRVAIAAALDAAPGV 193
Cdd:TIGR00957 1373 sgslrMNLDPFSQYSDEEVwwalelAHLKTFVSALPDKLDHECAEGG----------ENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 541492527 194 LIADEPTTALDVTTQKEIltlLASLRDARGMALVL-VTHDLALARDYgDDIVVMRGGAIVEAGQARRVLARPATDYA 269
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLI---QSTIRTQFEDCTVLtIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-530 |
1.61e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 40.61 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 320 GHLALAGVSLDILPGQSVGIVGESGSGKTTL-----------ARITVGLEAPDSGTVHVARapgAGRGAPPPVGIVFQNP 388
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLlsaflrllnteGDIQIDGVSWNSVPLQKWR---KAFGVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 389 YSA-LNPartVGQ-TLAEALAVGGQGG-----AQVPDLLGAVGLPAAHaqrlpaALSGGQRQRVAIARALAARPELLICD 461
Cdd:cd03289 93 FRKnLDP---YGKwSDEEIWKVAEEVGlksviEQFPGQLDFVLVDGGC------VLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 541492527 462 EAVSALDVSVQATIIDLLRrlQAEQGFALAFITHDLAvARQMSDRIIVMKDGAIVEEGATEALLAAPSH 530
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
172-246 |
1.64e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 541492527 172 QLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDARGMALVLVTHDLALARdYGDDIVVM 246
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVL 652
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-256 |
1.70e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 37 VANPSDPDRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPaqfTTSGTVELAGRTIDLGVAADSLR------- 109
Cdd:PRK10982 253 VRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE---KSAGTITLHGKKINNHNANEAINhgfalvt 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 110 -RLRGGGIVWLPQDPFTSLsplhrcgVQVIAHRQGPRSERAERALARLAEVGLPARAARAYPHQ-----LSGGMRQRVAI 183
Cdd:PRK10982 330 eERRSTGIYAYLDIGFNSL-------ISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRtqigsLSGGNQQKVII 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 541492527 184 AAALDAAPGVLIADEPTTALDVTTQKEILTLLASLRDaRGMALVLVTHDLALARDYGDDIVVMRGG---AIVEAGQ 256
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGlvaGIVDTKT 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
44-232 |
5.34e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 44 DRPIVADVSVDAAPGRTLVIVGESGAGKSMLARAICGLAPAqftTSGTVELaGRTIDLGVAADSLRRLRGGGIVWlpqdp 123
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQP---DSGTIKI-GETVKLAYVDQSRDALDPNKTVW----- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 124 ftslsplhrcgvQVIahrqgprSERAEraLARLAEVGLPARAaraY--------PHQ------LSGGMRQRVAIAAALDA 189
Cdd:PRK11819 407 ------------EEI-------SGGLD--IIKVGNREIPSRA---YvgrfnfkgGDQqkkvgvLSGGERNRLHLAKTLKQ 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 541492527 190 APGVLIADEPTTALDVTTqkeiltlLASLRDA----RGMALVlVTHD 232
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVET-------LRALEEAllefPGCAVV-ISHD 501
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
437-519 |
5.44e-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: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 437 LSGGQRQRVAIARALAAR---PELLICDEAVSALDVSVQATIIDLLRRLqAEQGFALAFITHDLAVARQmSDRIIVM--- 510
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIKC-ADWIIDLgpe 247
|
90
....*....|..
gi 541492527 511 ---KDGAIVEEG 519
Cdd:cd03271 248 ggdGGGQVVASG 259
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|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
335-363 |
6.56e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 38.12 E-value: 6.56e-03
10 20
....*....|....*....|....*....
gi 541492527 335 QSVGIVGESGSGKTTLARITVGLEAPDSG 363
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEG 42
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|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
172-244 |
8.17e-03 |
|
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: 38.12 E-value: 8.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 541492527 172 QLSGGMRQRVAIAAALDAAPGVLIADEPTTALDVTTQKEILTLLASL-RDARgmALVLVTHDLALArDYGDDIV 244
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELaEDDN--YVLVVEHDLAVL-DYLSDYI 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-350 |
9.79e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 153 LARLAEVGLPARAARAYPHQLSGGMRQRVAIAA-ALDAAPGVL-IADEPTTALDVTTQKEILTLLASLRDaRGMALVLVT 230
Cdd:PRK00635 457 LSILIDLGLPYLTPERALATLSGGEQERTALAKhLGAELIGITyILDEPSIGLHPQDTHKLINVIKKLRD-QGNTVLLVE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 541492527 231 HD---LALArDYGDDI---VVMRGGAIVEAGQARRVLARPATDYArQLLDAQLRLDGPSPRPAGavPATTVADERPIVAL 304
Cdd:PRK00635 536 HDeqmISLA-DRIIDIgpgAGIFGGEVLFNGSPREFLAKSDSLTA-KYLRQELTIPIPEKRTNS--LGTLTLSKATKHNL 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 541492527 305 RDVVkefrsggrraeghlalagVSLDIlpGQSVGIVGESGSGKTTL 350
Cdd:PRK00635 612 KDLT------------------ISLPL--GRLTVVTGVSGSGKSSL 637
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