|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-524 |
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: 650.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDWSD 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMKQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 241 IVQRPQHPYTRQLLhdlqDAPLGLTAARHRPLATPAIRVEGISKRFSLGKQALQ-------ALDSVSFEVRRGSTHALVG 313
Cdd:COG4172 244 LFAAPQHPYTRKLL----AAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRrtvghvkAVDGVSLTLRRGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 314 ESGSGKTTLARILLGFERADaGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLK-NFERLSA 392
Cdd:COG4172 320 ESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRvHGPGLSA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 393 ATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLS 472
Cdd:COG4172 399 AERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLA 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 473 YLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAIP 524
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-526 |
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: 598.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRdAGRIVLNGEVISDWSDk 81
Cdd:COG1123 3 PLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 rlnRLRGVSISLVPQDPGNSLNPVkTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQR 161
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI 241
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 242 VQRPQhpytrQLLHDLQDAPLGLTAARHRPLATPAIRVEGISKRFSL-GKQALQALDSVSFEVRRGSTHALVGESGSGKT 320
Cdd:COG1123 231 LAAPQ-----ALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 321 TLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVE 400
Cdd:COG1123 306 TLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 401 SVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDL 480
Cdd:COG1123 386 ELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDL 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1031820327 481 ATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAIPQV 526
Cdd:COG1123 466 AVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSL 511
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-521 |
7.31e-151 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 442.61 E-value: 7.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLL-ADNARRDAGRIVLNGEVISDWS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPVVYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 DKRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMK 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 240 TIVQRPQHPYTRQLLH-DLQDAPLGLTAArhrplATPAIRVEGISKRFSLGKQAL-------QALDSVSFEVRRGSTHAL 311
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNsEPSGDPVPLPEP-----ASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 312 VGESGSGKTTLARILLGFERADaGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLK-NFERL 390
Cdd:PRK15134 318 VGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 391 SAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLG 470
Cdd:PRK15134 397 SAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQ 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 471 LSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIA 521
Cdd:PRK15134 477 LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-524 |
1.07e-130 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 394.22 E-value: 1.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLL-ADNARRDAGRIVL---NGEVI--S 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLeQAGGLVQCDKMLLrrrSRQVIelS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 77 DWSDKRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSG 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 157 GMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 237 ATETIVQRPQHPYTRQLLHDLQD--APLGLTAARHRPLAT--------------------PAIRVEGISKRFSLG----- 289
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQlgAMKGLDYPRRFPLISlehpakqeppieqdtvvdgePILQVRNLVTRFPLRsglln 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 290 --KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNPF 367
Cdd:PRK10261 332 rvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 368 ASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:PRK10261 412 ASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 448 SALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAIP 524
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-254 |
4.96e-126 |
|
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: 371.31 E-value: 4.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARrDAGRIVLNGEVISDWSDKR 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGI-TSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMKQRV 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIV 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250
....*....|..
gi 1031820327 243 QRPQHPYTRQLL 254
Cdd:COG0444 240 ENPRHPYTRALL 251
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-236 |
5.34e-103 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 309.05 E-value: 5.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISDWSDKR 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK----PTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LnRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLnLLAKVGLSHPEQRFDQYPHQLSGGMKQRV 162
Cdd:cd03257 77 R-KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
273-524 |
8.74e-98 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 299.34 E-value: 8.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSLGK-------QALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG 345
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 346 HLSREAQRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQR 425
Cdd:COG4608 84 GLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 426 QRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVN 505
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
250
....*....|....*....
gi 1031820327 506 RLFAAPQQAYTRELIAAIP 524
Cdd:COG4608 244 ELYARPLHPYTQALLSAVP 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-525 |
7.09e-91 |
|
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: 278.61 E-value: 7.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQL 355
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERlsaATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALI 435
Cdd:COG1124 78 RRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGL---PDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 436 LEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAY 515
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
250
....*....|
gi 1031820327 516 TRELIAAIPQ 525
Cdd:COG1124 235 TRELLAASLA 244
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
277-529 |
2.40e-89 |
|
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: 277.32 E-value: 2.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERA---DAGQVTIDGIDAGHLSREAQR 353
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 QLR-RKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVAL--APELLSRTPRELSGGQRQRVAI 430
Cdd:COG0444 82 KIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 431 ARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
250
....*....|....*....
gi 1031820327 511 PQQAYTRELIAAIPQVSSR 529
Cdd:COG0444 242 PRHPYTRALLSSIPRLDPD 260
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
282-524 |
7.15e-85 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 266.06 E-value: 7.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 282 ISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRRKIQF 361
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 362 VYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAIL 441
Cdd:PRK11308 97 VFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 442 VLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIA 521
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
...
gi 1031820327 522 AIP 524
Cdd:PRK11308 257 ATP 259
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-254 |
4.02e-84 |
|
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: 261.28 E-value: 4.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRL 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSlsaAERRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRVL 163
Cdd:COG1124 78 RR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGL---PDREERIAELLEQVGL--PPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|.
gi 1031820327 244 RPQHPYTRQLL 254
Cdd:COG1124 229 GPKHPYTRELL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
277-502 |
6.77e-84 |
|
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: 259.75 E-value: 6.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAAR-VALAPELLSRTPRELSGGQRQRVAIARALI 435
Cdd:cd03257 82 KEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 436 LEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-254 |
1.23e-80 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 255.04 E-value: 1.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEW----REVVH---NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVI 75
Cdd:COG4608 7 LLEVRDLKKHFPVRGGLfgrtVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE----EPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 76 SDWSDKRLNRLRgVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLShPEQrFDQYPHQLS 155
Cdd:COG4608 83 TGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PEH-ADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250
....*....|....*....
gi 1031820327 236 GATETIVQRPQHPYTRQLL 254
Cdd:COG4608 240 APRDELYARPLHPYTQALL 258
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-255 |
2.98e-80 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 250.75 E-value: 2.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDwsdkrlNRLRGVSISLVPQDPGNSL 102
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLP------LSIRGRHIATIMQNPRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVEEILRLHQSLSAaERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTS 182
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 183 ALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLLH 255
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-254 |
4.55e-77 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 246.17 E-value: 4.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDaGRIVLNGEVISDWSD 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG-GSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMKQ 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET 240
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250
....*....|....
gi 1031820327 241 IVQRPQHPYTRQLL 254
Cdd:PRK09473 249 VFYQPSHPYSIGLL 262
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-257 |
6.65e-76 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 242.73 E-value: 6.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDWSD 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMKQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*..
gi 1031820327 241 IVQRPQHPYTRQLLHDL 257
Cdd:PRK11022 241 IFRAPRHPYTQALLRAL 257
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-255 |
2.27e-70 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 226.26 E-value: 2.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEW-----REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVI 75
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGII----EPTSGEILINGHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 76 SDWSDKRLNRLrgvsISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLsHPEQRFDqYPHQLS 155
Cdd:COG4167 78 EYGDYKYRCKH----IRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGL-LPEHANF-YPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250 260
....*....|....*....|
gi 1031820327 236 GATETIVQRPQHPYTRQLLH 255
Cdd:COG4167 232 GKTAEVFANPQHEVTKRLIE 251
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-288 |
1.09e-67 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 221.38 E-value: 1.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYR-SRGEWR-----EVVHNISFSIQRGEMLAFVGESGSGKTTTAQaiigLLADNARRDAGRIVLNGEV 74
Cdd:PRK11308 3 QPLLQAIDLKKHYPvKRGLFKperlvKALDGVSFTLERGKTLAVVGESGCGKSTLAR----LLTMIETPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 75 ISDwSDKRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLsHPEQrFDQYPHQL 154
Cdd:PRK11308 79 LLK-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPEH-YDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQE 234
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 235 QGATETIVQRPQHPYTRQLLHdlqdaplgltaarhrplATPAIRVEGISKRFSL 288
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLS-----------------ATPRLNPDDRRERIKL 272
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
277-525 |
2.37e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.71 E-value: 2.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFASLDPRQrLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:COG1135 82 RKIGMIFQH-FNLLSSRT-VAENVALPLE-IAGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 437 EPAILVLDEATSALD-------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAGQ 497
Cdd:COG1135 158 NPKVLLCDEATSALDpettrsildllkdinrelgLTI-------------------VLITHEMDVVRRICDRVAVLENGR 218
|
250 260
....*....|....*....|....*...
gi 1031820327 498 VVEHGDVNRLFAAPQQAYTRELIAAIPQ 525
Cdd:COG1135 219 IVEQGPVLDVFANPQSELTRRFLPTVLN 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
273-536 |
7.75e-65 |
|
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: 219.94 E-value: 7.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGF----ERADAGQVTIDGIDAGHLS 348
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 349 REAQRQLR-RKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVAL-APE-LLSRTPRELSGGQR 425
Cdd:COG4172 83 ERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpDPErRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 426 QRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVN 505
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250 260 270
....*....|....*....|....*....|.
gi 1031820327 506 RLFAAPQQAYTRELIAAIPQVSSRLAQAHTE 536
Cdd:COG4172 243 ELFAAPQHPYTRKLLAAEPRGDPRPVPPDAP 273
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
290-524 |
1.03e-64 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 213.80 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 290 KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNPFAS 369
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 370 LDPRQRLFAIIEEPLKNFE-RLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATS 448
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 449 ALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAIP 524
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
274-538 |
1.26e-63 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 208.54 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFS-----LGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAGH 346
Cdd:COG4167 2 SALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 347 LSREAQRqlrrkIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQ 426
Cdd:COG4167 82 YKYRCKH-----IRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNR 506
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250 260 270
....*....|....*....|....*....|..
gi 1031820327 507 LFAAPQQAYTRELIAaipqvsSRLAQAHTENA 538
Cdd:COG4167 237 VFANPQHEVTKRLIE------SHFGEALTADA 262
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-235 |
8.05e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 205.28 E-value: 8.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLaDNArrDAGRIVLNGEVISDWSDK 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGL-DRP--TSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGVSISLVPQDPGnsLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQR 161
Cdd:COG1136 79 ELARLRRRHIGFVFQFFN--LLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAeRADRIMVFRQGEIQEQ 235
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-259 |
1.64e-61 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 205.52 E-value: 1.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDWSD 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILrLHQSLS------AAERRQQVLNLLAKVGLSHPEQRFDQYPHQL 154
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAI-PSWTFKgkwwqrFKWRKKRAIELLHRVGIKDHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQE 234
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260
....*....|....*....|....*
gi 1031820327 235 QGATETIVQRPQHPYTRQLLHDLQD 259
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-232 |
5.59e-61 |
|
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: 200.02 E-value: 5.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAqAIIGLLAdnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLD---RPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSISLVPQDPGnsLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVL 163
Cdd:cd03255 77 AAFRRRHIGFVFQSFN--LLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALaAERADRIMVFRQGEI 232
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-254 |
5.26e-59 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 198.78 E-value: 5.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISY--RSRGEW-------REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGE 73
Cdd:PRK15079 8 LLEVADLKVHFdiKDGKQWfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 74 VISDWSDKRLNRLRGvSISLVPQDPGNSLNPVKTIGQQVEEILRLHQ-SLSAAERRQQVLNLLAKVGLShpEQRFDQYPH 152
Cdd:PRK15079 84 DLLGMKDDEWRAVRS-DIQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLL--PNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260
....*....|....*....|..
gi 1031820327 233 QEQGATETIVQRPQHPYTRQLL 254
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALM 262
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-254 |
3.69e-58 |
|
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: 193.27 E-value: 3.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKR 82
Cdd:COG1127 5 MIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL----RPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDPG--NSLnpvkTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQ 160
Cdd:COG1127 77 LYELRR-RIGMLFQGGAlfDSL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAA---DKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALD-VTVqKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
250
....*....|....*
gi 1031820327 240 TIvQRPQHPYTRQLL 254
Cdd:COG1127 228 EL-LASDDPWVRQFL 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-255 |
2.57e-57 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 191.84 E-value: 2.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRsrgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISdwsdkr 82
Cdd:PRK10418 4 QIELRNIALQAA-----QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRlhqSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGMKQRV 162
Cdd:PRK10418 73 PCALRGRKIATIMQNPRSAFNPLHTMHTHARETCL---ALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIV 242
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|...
gi 1031820327 243 QRPQHPYTRQLLH 255
Cdd:PRK10418 230 NAPKHAVTRSLVS 242
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
3-255 |
7.89e-57 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 190.79 E-value: 7.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEV-----ISD 77
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAP----TSGSVYYRDRDggprdLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 78 WSDKRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEilRLhqsLSAAER-----RQQVLNLLAKVGLshPEQRFDQYPH 152
Cdd:COG4107 84 LSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAE--RL---MAAGERhygdiRARALEWLERVEI--PLERIDDLPR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:COG4107 157 TFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRV 236
|
250 260
....*....|....*....|...
gi 1031820327 233 QEQGATETIVQRPQHPYTRQLLH 255
Cdd:COG4107 237 VESGLTDQVLEDPQHPYTQLLVS 259
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
274-500 |
1.36e-56 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 190.28 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRF-----SLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS 348
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 349 REAQRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRV 428
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 429 AIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVE 500
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
274-538 |
1.48e-56 |
|
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: 197.43 E-value: 1.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFslGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA---GQVTIDGIDAGHLSre 350
Cdd:COG1123 2 TPLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 351 aQRQLRRKIQFVYQNPFASLDPrQRLFAIIEEPLKNFeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAI 430
Cdd:COG1123 78 -EALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENL-GLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 431 ARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260
....*....|....*....|....*...
gi 1031820327 511 PQQaytrelIAAIPQVSSRLAQAHTENA 538
Cdd:COG1123 234 PQA------LAAVPRLGAARGRAAPAAA 255
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
277-512 |
6.21e-56 |
|
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: 187.40 E-value: 6.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFASLDPRQrLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:cd03258 82 RRIGMIFQH-FNLLSSRT-VFENVALPLE-IAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-246 |
2.08e-55 |
|
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: 186.00 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEvisDWSDKRL 83
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL----KPTSGEVLVDGK---DITKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDPGNSLnpvktIGQQV-EEI---LRlHQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMK 159
Cdd:COG1122 71 RELRR-KVGLVFQNPDDQL-----FAPTVeEDVafgPE-NLGLPREEIRERVEEALELVGLEHLADR---PPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
....*..
gi 1031820327 240 TIVQRPQ 246
Cdd:COG1122 220 EVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
273-511 |
4.28e-55 |
|
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: 185.57 E-value: 4.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ 352
Cdd:COG1127 2 SEPMIEVRNLTKSF--GDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQNP--FASLDprqrlfaiIEE----PLKNFERLSAATRRQRVESVAARVALaPELLSRTPRELSGGQRQ 426
Cdd:COG1127 78 YELRRRIGMLFQGGalFDSLT--------VFEnvafPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 427 RVAIARALILEPAILVLDEATSALD-------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIA 487
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpitsavidelirelrdelgLTS-------------------VVVTHDLDSAFAIA 209
|
250 260
....*....|....*....|....
gi 1031820327 488 DSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:COG1127 210 DRVAVLADGKIIAEGTPEELLASD 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
277-523 |
2.12e-54 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 184.62 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLG-----KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREA 351
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIA 431
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 432 RALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFK 242
|
250
....*....|..
gi 1031820327 512 QQAyTRELIAAI 523
Cdd:TIGR02769 243 HPA-GRNLQSAV 253
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-255 |
2.87e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 183.27 E-value: 2.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDwSDKR 82
Cdd:COG1126 1 MIEIENLHKSF---GD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLE----EPDSGTITVDGEDLTD-SKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQdpgnSLN--PVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQ 160
Cdd:COG1126 72 INKLRR-KVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALD-VTVQkrilDLLDILRR--ESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDpELVG----EVLDVMRDlaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250
....*....|....*...
gi 1031820327 238 TETIVQRPQHPYTRQLLH 255
Cdd:COG1126 220 PEEFFENPQHERTRAFLS 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
4.10e-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: 182.29 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDwsdkrl 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE----RPTSGEVLVDGEPVTG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlRGVSISLVPQDPgnSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVL 163
Cdd:cd03293 71 ---PGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 164 IAIAIALQPDLIIADEPTSALD-VTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVF--RQGEIQEQ 235
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDaLTREQLQEELLDIWRET-GKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-252 |
2.90e-53 |
|
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: 180.39 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL----RPDSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRgVSISLVPQDPG--NSLnpvkTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQR 161
Cdd:cd03261 73 YRLR-RRMGMLFQSGAlfDSL----TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI 241
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
250
....*....|.
gi 1031820327 242 vQRPQHPYTRQ 252
Cdd:cd03261 225 -RASDDPLVRQ 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-257 |
6.99e-53 |
|
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: 179.85 E-value: 6.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKR 82
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL----KPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLrgvsISLVPQDPGNSLnpvktiGQQVEEILRL----HQSLSA---AERRQQVLNLLAKVGLSHPEQRfdqYPHQLS 155
Cdd:COG1120 73 LARR----IAYVPQEPPAPF------GLTVRELVALgrypHLGLFGrpsAEDREAVEEALERTGLEHLADR---PVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
250 260
....*....|....*....|..
gi 1031820327 236 GATETIVqrpqhpyTRQLLHDL 257
Cdd:COG1120 220 GPPEEVL-------TPELLEEV 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-503 |
1.79e-52 |
|
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: 186.55 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLlaDNARRDAGRIV-------------- 69
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPTSGRIIyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 70 --------------LNGEVISDW--SDKRLNRLRGvSISLVPQDPgNSLNPVKTIgqqVEEILR-LHQ-SLSAAERRQQV 131
Cdd:TIGR03269 75 pskvgepcpvcggtLEPEEVDFWnlSDKLRRRIRK-RIAIMLQRT-FALYGDDTV---LDNVLEaLEEiGYEGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 132 LNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVT 211
Cdd:TIGR03269 150 VDLIEMVQLSH---RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 212 HDLALAAERADRIMVFRQGEIQEQGATETIVQRpqhpytrqllhDLQDAPLgLTAARHRPLATPAIRVEGISKRF-SLGK 290
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV-----------FMEGVSE-VEKECEVEVGEPIIKVRNVSKRYiSVDR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 291 QALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTI----DGIDAGHLSREAQRQLRRKIQFVYQNp 366
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAKRYIGILHQE- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 fASLDPRQRLF-----AIIEEPLKNFERLSAATRrqrVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAIL 441
Cdd:TIGR03269 374 -YDLYPHRTVLdnlteAIGLELPDELARMKAVIT---LKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 442 VLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGD 503
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-249 |
2.97e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 181.45 E-value: 2.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWS- 79
Cdd:COG3842 3 MPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE----TPDSGRILLDGRDVTGLPp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 DKRlnrlrgvSISLVPQDPgnSLNPVKTIGQQVEEILRlHQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMK 159
Cdd:COG3842 75 EKR-------NVGMVFQDY--ALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADR---YPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHD----LALaaerADRIMVFRQGEIQEQ 235
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQV 217
|
250
....*....|....
gi 1031820327 236 GATETIVQRPQHPY 249
Cdd:COG3842 218 GTPEEIYERPATRF 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
9.64e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 177.20 E-value: 9.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVIsdwsd 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP----TSGEVLVDGKPV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVsislVPQDPgnSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQ 160
Cdd:COG1116 76 TGPGPDRGV----VFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDvtVQKRIL---DLLDILRREsGTAVLFVTHDLALAAERADRIMVF--RQGEIQE 234
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALD--ALTRERlqdELLRLWQET-GKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVE 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
277-512 |
1.64e-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: 175.60 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLR 356
Cdd:COG1122 1 IELENLSFSYPGGTPAL---DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFAsldprQRLFAIIEE----PLKNFeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIAR 432
Cdd:COG1122 75 RKVGLVFQNPDD-----QLFAPTVEEdvafGPENL-GLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLR 494
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDprgrrellellkrlnkegKTV-------------------IIVTHDLDLVAELADRVIVLD 208
|
250
....*....|....*...
gi 1031820327 495 AGQVVEHGDVNRLFAAPQ 512
Cdd:COG1122 209 DGRIVADGTPREVFSDYE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-231 |
2.98e-51 |
|
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: 174.19 E-value: 2.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 5 SVEDLRISYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLN 84
Cdd:cd03225 1 ELKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL----GPTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 RLrgvsISLVPQDPGNSLnpvktIGQQV-EEI---LRlHQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQ 160
Cdd:cd03225 75 RK----VGLVFQNPDDQF-----FGPTVeEEVafgLE-NLGLPEEEIEERVEEALELVGLEGLR---DRSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
274-500 |
7.41e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 173.69 E-value: 7.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQR 353
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 QLRR-KIQFVYQNPFasLDPrqRLFAI--IEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAI 430
Cdd:COG1136 82 RLRRrHIGFVFQFFN--LLP--ELTALenVALPLL-LAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 431 ARALILEPAILVLDEATSALD-------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRiADSVT 491
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDsktgeevlellrelnrelgTTI-------------------VMVTHDPELAAR-ADRVI 215
|
....*....
gi 1031820327 492 VLRAGQVVE 500
Cdd:COG1136 216 RLRDGRIVS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-244 |
1.29e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.33 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL----RPTSGEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvsISLVPQDPGnsLNPVKTigqqVEEILRLHQSL---SAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQ 160
Cdd:COG1131 73 RR-----IGYVPQEPA--LYPDLT----VRENLRFFARLyglPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET 240
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
....
gi 1031820327 241 IVQR 244
Cdd:COG1131 218 LKAR 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-262 |
4.02e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.27 E-value: 4.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRL 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL----ERPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDPgNSLNPvKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVL 163
Cdd:COG1135 78 RAARR-KIGMIFQHF-NLLSS-RTVAENVALPLEI-AGVPKAEIRKRVAELLELVGLSD---KADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|....*....
gi 1031820327 244 RPQHPYTRQLLHDLQDAPL 262
Cdd:COG1135 231 NPQSELTRRFLPTVLNDEL 249
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
277-512 |
4.41e-50 |
|
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: 171.92 E-value: 4.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:cd03261 1 IELRGLTKSF--GGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNP--FASLDPRQRlfaiIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRtPRELSGGQRQRVAIARAL 434
Cdd:cd03261 77 RRMGMLFQSGalFDSLTVFEN----VAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLY-PAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 435 ILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
277-538 |
8.58e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.91 E-value: 8.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFASLDPRQrLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:PRK11153 82 RQIGMIFQH-FNLLSSRT-VFDNVALPLE-LAGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 437 EPAILVLDEATSALD-------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAGQ 497
Cdd:PRK11153 158 NPKVLLCDEATSALDpattrsilellkdinrelgLTI-------------------VLITHEMDVVKRICDRVAVIDAGR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1031820327 498 VVEHGDVNRLFAAPQQAYTRELIAAIPQVS---SRLAQAHTENA 538
Cdd:PRK11153 219 LVEQGTVSEVFSHPKHPLTREFIQSTLHLDlpeDYLARLQAEPT 262
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
273-520 |
1.50e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 171.43 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaq 352
Cdd:COG3842 2 AMPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 rqlRRKIQFVYQNpFAsldprqrLF------AIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQ 426
Cdd:COG3842 76 ---KRNVGMVFQD-YA-------LFphltvaENVAFGLR-MRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNR 506
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
250
....*....|....
gi 1031820327 507 LFAAPQQAYTRELI 520
Cdd:COG3842 223 IYERPATRFVADFI 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
277-502 |
6.66e-48 |
|
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: 165.39 E-value: 6.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlR 356
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfaSLDPRQRLFAIIEEPLKNfERLSAATRRQRVESVAARVALaPELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:cd03259 72 RNIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-259 |
1.12e-47 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 168.83 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDWSD 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVPQDPGNSLNPVKTIGQQVEEIL-------RLHQSLSAAERRqqVLNLLAKVGLSHPEQRFDQYPHQ 153
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWRKRR--AIELLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 154 LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQ 233
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260
....*....|....*....|....*.
gi 1031820327 234 EQGATETIVQRPQHPYTRQLLHDLQD 259
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPD 264
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-254 |
1.71e-47 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 165.17 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 14 RSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRLNRlrgvSISL 93
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP----TSGEIFIDGEDIREQDPVELRR----KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 VPQDPGnsLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLShPEQRFDQYPHQLSGGMKQRVLIAIAIALQPD 173
Cdd:cd03295 80 VIQQIG--LFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 174 LIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQL 253
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
.
gi 1031820327 254 L 254
Cdd:cd03295 236 V 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
277-507 |
3.14e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqlR 356
Cdd:COG1131 1 IEVRGLTKRY--GDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfaSLDPRQRlfaiIEEPLKNFERL---SAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARA 433
Cdd:COG1131 73 RRIGYVPQEP--ALYPDLT----VRENLRFFARLyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 434 LILEPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRA 495
Cdd:COG1131 146 LLHDPELLILDEPTSGLDpearrelwellrelaaegKTV-------------------LLSTHYLEEAERLCDRVAIIDK 206
|
250
....*....|..
gi 1031820327 496 GQVVEHGDVNRL 507
Cdd:COG1131 207 GRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-236 |
1.32e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 161.92 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE----RPDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NrlrgvsISLVPQDPgnSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVL 163
Cdd:cd03259 73 N------IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-498 |
1.53e-46 |
|
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: 161.89 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RK-IQFVYQNPfaSLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALI 435
Cdd:cd03255 81 RRhIGFVFQSF--NLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 436 LEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLaTVRRIADSVTVLRAGQV 498
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-232 |
1.78e-46 |
|
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: 160.26 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL----KPDSGEIKVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvsISLVPQDPgnslnpvktigqqveeilRLHQSLSAAErrqqvlNLlakvglshpeqrfdqyphQLSGGMKQRVL 163
Cdd:cd03230 73 RR-----IGYLPEEP------------------SLYENLTVRE------NL------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-254 |
2.64e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 165.32 E-value: 2.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEvisDWSDKRL 83
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE----TPDSGRIVLNGR---DLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSisLVPQDPGnsLNPVKTIGQQVEEILRlHQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVL 163
Cdd:COG1118 72 PRERRVG--FVFQHYA--LFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLL-DILRRESGTAVlFVTHDLALAAERADRIMVFRQGEIQEQGATETIV 242
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLrRLHDELGGTTV-FVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
250
....*....|..
gi 1031820327 243 QRPQHPYTRQLL 254
Cdd:COG1118 223 DRPATPFVARFL 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
2.88e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.18 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIsdwsd 80
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL----PPTSGTVRLFGKPP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 krlnRLRGVSISLVPQDPGNSLN-PVKtigqqVEEI--------LRLHQSLSAAERrQQVLNLLAKVGLSHPEQRfdQYp 151
Cdd:COG1121 71 ----RRARRRIGYVPQRAEVDWDfPIT-----VRDVvlmgrygrRGLFRRPSRADR-EAVDEALERVGLEDLADR--PI- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
250
....*....|
gi 1031820327 232 IQEqGATETI 241
Cdd:COG1121 217 VAH-GPPEEV 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
277-523 |
3.12e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 161.70 E-value: 3.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHlSREAQRQLR 356
Cdd:COG1126 2 IEIENLHKSFG----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFAsldprqrLFA-------IIEEPLKNfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVA 429
Cdd:COG1126 77 RKVGMVFQQ-FN-------LFPhltvlenVTLAPIKV-KKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 430 IARALILEPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVT 491
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelvgevldvmrdlakegMTM-------------------VVVTHEMGFAREVADRVV 207
|
250 260 270
....*....|....*....|....*....|..
gi 1031820327 492 VLRAGQVVEHGDVNRLFAAPQQAYTRELIAAI 523
Cdd:COG1126 208 FMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-253 |
6.42e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 162.16 E-value: 6.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRS-----RGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVI 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL----ESPSQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 76 SDWSDKRLNRLRGvSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLshPEQRFDQYPHQLS 155
Cdd:PRK10419 77 AKLNRAQRKAFRR-DIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDL--DDSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250
....*....|....*...
gi 1031820327 236 gATETIVQRPQHPYTRQL 253
Cdd:PRK10419 234 -QPVGDKLTFSSPAGRVL 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-452 |
1.02e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 167.50 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISdWSDKRLNRLRGVSIslVPQDPgnS 101
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKST----LMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAGIAI--IHQEL--N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPVKTIGQQV---EEILRLHqSLSAAERRQQVLNLLAKVGLS-HPEQRFDQyphqLSGGMKQRVLIAIAIALQPDLIIA 177
Cdd:COG1129 90 LVPNLSVAENIflgREPRRGG-LIDWRAMRRRARELLARLGLDiDPDTPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 178 DEPTSALDVT-VQKrildLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIvqrpqhpyTRQLL 254
Cdd:COG1129 165 DEPTASLTEReVER----LFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL--------TEDEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 255 ------HDLQDaplgLTAARHRPLATPAIRVEGISKRfslgkqalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLG 328
Cdd:COG1129 233 vrlmvgRELED----LFPKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 329 FERADAGQVTIDGIDAGHLS-REAqrqLRRKIQFVYQNpfasldpRQR--LFAI--IEE-----PLKNFER---LSAATR 395
Cdd:COG1129 301 ADPADSGEIRLDGKPVRIRSpRDA---IRAGIAYVPED-------RKGegLVLDlsIREnitlaSLDRLSRgglLDRRRE 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 396 RQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:COG1129 371 RALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-254 |
1.02e-45 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 161.25 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVvhniSFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdagrivlnGEVISDWSDKRL 83
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDV----SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDA----------GEVHYRMRDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSIS-----------LVPQDPGNSLNPVKTIGQQVEEilRLhqsLSAAER-----RQQVLNLLAKVGLshPEQRF 147
Cdd:PRK11701 73 RDLYALSEAerrrllrtewgFVHQHPRDGLRMQVSAGGNIGE--RL---MAVGARhygdiRATAGDWLERVEI--DAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 148 DQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVF 227
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|....*..
gi 1031820327 228 RQGEIQEQGATETIVQRPQHPYTrQLL 254
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQHPYT-QLL 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-257 |
1.45e-45 |
|
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: 160.89 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDPGnsL 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI----EPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFA--L 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTS 182
Cdd:cd03294 114 LPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 183 ALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLLHDL 257
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
277-522 |
4.60e-45 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 159.57 E-value: 4.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISK--RFSLG---KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAGHLSR 349
Cdd:PRK15112 5 LEVRNLSKtfRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 350 EAQRqlrrkIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVA 429
Cdd:PRK15112 85 RSQR-----IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 430 IARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|...
gi 1031820327 510 APQQAYTRELIAA 522
Cdd:PRK15112 240 SPLHELTKRLIAG 252
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-234 |
4.69e-45 |
|
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: 158.28 E-value: 4.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLlaDNArrDAGRIVLNGEVISDWSDKR 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL--DNP--TSGEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGVSISLVPQdpGNSLNPVKTIGQQVEEILRL-HQSLSAAERRQQvlNLLAKVGLSHpeqRFDQYPHQLSGGMKQR 161
Cdd:TIGR02211 77 RAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLIgKKSVKEAKERAY--EMLEKVGLEH---RINHRPSELSGGERQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALaAERADRIMVFRQGEIQE 234
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
273-523 |
5.48e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.10 E-value: 5.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsrEAQ 352
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQNPfaSLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIAR 432
Cdd:COG1116 76 TGPGPDRGVVFQEP--ALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALDV-------------------TVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVL 493
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDAltrerlqdellrlwqetgkTV-------------------LFVTHDVDEAVFLADRVVVL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1031820327 494 RA--GQVVEHGDVN-------RLFAAPQ-QAYTRELIAAI 523
Cdd:COG1116 213 SArpGRIVEEIDVDlprprdrELRTSPEfAALRAEILDLL 252
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-246 |
7.49e-45 |
|
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: 157.88 E-value: 7.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISyrsrgeWRE-VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWS-DK 81
Cdd:cd03299 1 LKVENLSKD------WKEfKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI----KPDSGKILLNGKDITNLPpEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RlnrlrgvSISLVPQDpgNSLNPVKTIGQQVEEILRlHQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQR 161
Cdd:cd03299 71 R-------DISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI 241
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
....*
gi 1031820327 242 VQRPQ 246
Cdd:cd03299 218 FKKPK 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-246 |
5.17e-44 |
|
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: 155.82 E-value: 5.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKR 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL----ERPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDpGNSLNPvKTIGQQVEEILRLHqSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRV 162
Cdd:cd03258 77 LRKARR-RIGMIFQH-FNLLSS-RTVFENVALPLEIA-GVPKAEIEERVLELLELVGLED---KADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIV 242
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
....
gi 1031820327 243 QRPQ 246
Cdd:cd03258 230 ANPQ 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-258 |
8.43e-44 |
|
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: 156.44 E-value: 8.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLriSYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDwsDKRL 83
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLP----TSGKVTVDGLDTLD--EENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDPGNSLnpvktIGQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLShpEQRfDQYPHQLSGGMKQ 160
Cdd:TIGR04520 73 WEIRK-KVGMVFQNPDNQF-----VGATVEDDVAFgleNLGVPREEMRKRVDEALKLVGME--DFR-DREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAErADRIMVFRQGEIQEQGATET 240
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222
|
250 260
....*....|....*....|....*.
gi 1031820327 241 IVQRPQH--------PYTRQLLHDLQ 258
Cdd:TIGR04520 223 IFSQVELlkeigldvPFITELAKALK 248
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
277-500 |
1.06e-43 |
|
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: 154.55 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsrEAQRQLR 356
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfaSLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:cd03293 73 PDRGYVFQQD--ALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL--RAGQVVE 500
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-254 |
1.52e-43 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 155.72 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRGEW-----REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVIS 76
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS----GELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 77 --DWSdkrlnrLRGVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFdqYPHQL 154
Cdd:PRK15112 79 fgDYS------YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY--YPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQE 234
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|
gi 1031820327 235 QGATETIVQRPQHPYTRQLL 254
Cdd:PRK15112 231 RGSTADVLASPLHELTKRLI 250
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-236 |
1.60e-43 |
|
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: 152.59 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 5 SVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLN 84
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----KPSSGEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 RLrgvsISLVPQdpgnslnpvktigqqveeilrlhqslsaaerrqqvlnLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLI 164
Cdd:cd03214 73 RK----IAYVPQ-------------------------------------ALELLGLAHLADR---PFNELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 165 AIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
278-497 |
1.77e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.39 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 278 RVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReaqRQLRR 357
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL---KELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 358 KIQFVYQNPfasldpRQRLFA--IIEE---PLKNFeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIAR 432
Cdd:cd03225 76 KVGLVFQNP------DDQFFGptVEEEvafGLENL-GLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 433 ALILEPAILVLDEATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQ 497
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLD-PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-239 |
2.81e-43 |
|
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: 153.74 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDK 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKST----LLGLLAGLDRPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGVSISLVPQDpgnslnpvktigqqveeiLRLHQSLSA-------------AERRQQVLNLLAKVGLSHpeqRFD 148
Cdd:COG4181 83 ARARLRARHVGFVFQS------------------FQLLPTLTAlenvmlplelagrRDARARARALLERVGLGH---RLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 149 QYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAeRADRIMVFR 228
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLR 220
|
250
....*....|.
gi 1031820327 229 QGEIQEQGATE 239
Cdd:COG4181 221 AGRLVEDTAAT 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-237 |
7.42e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.13 E-value: 7.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRLNRLR---GVsislVPQ 96
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRrriGV----VFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 97 DPGnsLNPVKTIGQQVEEILRLHqSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLII 176
Cdd:COG2884 87 DFR--LLPDRTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGLSD---KAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-232 |
7.47e-43 |
|
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: 151.91 E-value: 7.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDwSDKRL 83
Cdd:cd03262 1 IEIKNLHKSF---GD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPDSGTIIIDGLKLTD-DKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDpgNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVL 163
Cdd:cd03262 72 NELRQ-KVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-501 |
9.77e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 159.85 E-value: 9.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 6 VEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNgevisdwsdkrlnr 85
Cdd:COG0488 1 LENLSKSF---GG-RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP----DSGEVSIP-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 86 lRGVSISLVPQDPGnsLNPVKTIGQQVE----EILRLHQSLSAAERR---------------------------QQVLNL 134
Cdd:COG0488 59 -KGLRIGYLPQEPP--LDDDLTVLDTVLdgdaELRALEAELEELEAKlaepdedlerlaelqeefealggweaeARAEEI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 135 LAKVGLshPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDV-TVQKrildLLDILRRESGTaVLFVTHD 213
Cdd:COG0488 136 LSGLGF--PEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW----LEEFLKNYPGT-VLVVSHD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 214 LALAAERADRIMVFRQGEI-------------------QEQGA----------TETIVQRPQHPYTR--------QLLHD 256
Cdd:COG0488 209 RYFLDRVATRILELDRGKLtlypgnysayleqraerleQEAAAyakqqkkiakEEEFIRRFRAKARKakqaqsriKALEK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 257 LQ-------DAPLGLTAARHRPLATPAIRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGF 329
Cdd:COG0488 289 LEreepprrDKTVEIRFPPPERLGKKVLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 330 ERADAGQVTI-DGIDAGHLsreAQRQlrrkiqfvyqnpfASLDPRQRlfaiieePLKNFERLSAATRRQRVESVAARVAL 408
Cdd:COG0488 365 LEPDSGTVKLgETVKIGYF---DQHQ-------------EELDPDKT-------VLDELRDGAPGGTEQEVRGYLGRFLF 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 409 APELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV---------------TVqaqilallqqlqqqlglsy 473
Cdd:COG0488 422 SGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIetlealeealddfpgTV------------------- 482
|
570 580
....*....|....*....|....*...
gi 1031820327 474 LFITHDLATVRRIADSVTVLRAGQVVEH 501
Cdd:COG0488 483 LLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
277-507 |
1.73e-42 |
|
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: 151.93 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqlR 356
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasLDPRQRLFAIIEEpLKNFERLSAATRRQRVESVAARVALaPELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:COG4555 74 RQIGVLPDERG--LYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 437 EPAILVLDEATSALDVtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:COG4555 150 DPKVLLLDEPTNGLDV-MARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-511 |
2.09e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 154.85 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrql 355
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQNpFAsLDPRQRLFAIIEEPLKNfERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALI 435
Cdd:COG3839 74 DRNIAMVFQS-YA-LYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 436 LEPAILVLDEATSALD-------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAG 496
Cdd:COG3839 150 REPKVFLLDEPLSNLDaklrvemraeikrlhrrlgTTT-------------------IYVTHDQVEAMTLADRIAVMNDG 210
|
250
....*....|....*
gi 1031820327 497 QVVEHGDVNRLFAAP 511
Cdd:COG3839 211 RIQQVGTPEELYDRP 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
277-520 |
2.81e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 154.53 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG-HLS-REaqrq 354
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPpRE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 lrRKIQFVYQNpFAsldprqrLFaiieeplKN---FE---------RLSAATRRQRVESVAARVALApELLSRTPRELSG 422
Cdd:COG1118 75 --RRVGFVFQH-YA-------LF-------PHmtvAEniafglrvrPPSKAEIRARVEELLELVQLE-GLADRYPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....*...
gi 1031820327 503 DVNRLFAAPQQAYTRELI 520
Cdd:COG1118 217 TPDEVYDRPATPFVARFL 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
276-515 |
3.25e-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: 3.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrql 355
Cdd:cd03296 2 SIEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQN--PFASLDPRQRL-FAIIEEPLKnfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIAR 432
Cdd:cd03296 73 ERNVGFVFQHyaLFRHMTVFDNVaFGLRVKPRS--ERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
...
gi 1031820327 513 QAY 515
Cdd:cd03296 230 SPF 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-504 |
3.87e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 157.49 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS-REA 351
Cdd:COG1129 1 AEPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQlrrKIQFVYQ--NPFASLDPRQRLFaiIEEPLKNFERLSAATRRQRVESVAARVALapELLSRTP-RELSGGQRQRV 428
Cdd:COG1129 77 QAA---GIAIIHQelNLVPNLSVAENIF--LGREPRRGGLIDWRAMRRRARELLARLGL--DIDPDTPvGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 429 AIARALILEPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSV 490
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTereverlfriirrlkaqgVAI-------------------IYISHRLDEVFEIADRV 210
|
250
....*....|....
gi 1031820327 491 TVLRAGQVVEHGDV 504
Cdd:COG1129 211 TVLRDGRLVGTGPV 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-246 |
6.24e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 151.45 E-value: 6.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGvSISLVPQDPG 99
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL----KPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQFPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NslnpvktigQQVEE-ILR------LHQSLSAAERRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRVLIAIAIALQP 172
Cdd:TIGR04521 93 H---------QLFEEtVYKdiafgpKNLGLSEEEAEERVKEALELVGL--DEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 173 DLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQ 246
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-244 |
1.01e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.94 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDlrISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISD---W 78
Cdd:PRK13635 4 EIIRVEH--ISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL----LPEAGTITVGGMVLSEetvW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 79 SDKRlnrlrgvSISLVPQDPGNSLnpvktIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQLSGGM 158
Cdd:PRK13635 78 DVRR-------QVGMVFQNPDNQF-----VGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 159 KQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAeRADRIMVFRQGEIQEQGAT 238
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTP 224
|
....*.
gi 1031820327 239 ETIVQR 244
Cdd:PRK13635 225 EEIFKS 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
273-525 |
1.14e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 156.79 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAD-----AGQVTIDGIDAGHL 347
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 348 SREAQRQLR-RKIQFVYQNPFASLDPRQRlfaiIEEPLKNFERLSAATRRQ--RVESVAA--RVAL--APELLSRTPREL 420
Cdd:PRK15134 82 SEQTLRGVRgNKIAMIFQEPMVSLNPLHT----LEKQLYEVLSLHRGMRREaaRGEILNCldRVGIrqAAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 421 SGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVE 500
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|....*
gi 1031820327 501 HGDVNRLFAAPQQAYTRELIAAIPQ 525
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
277-512 |
2.85e-41 |
|
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: 148.25 E-value: 2.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKqalqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlR 356
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpfASLDPRQRLFAIIEEPLKNfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:cd03299 71 RDISYVPQN--YALFPHMTVYKNIAYGLKK-RKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
23-256 |
4.58e-41 |
|
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: 151.54 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDPGnsL 102
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTA----GQIFIDGENIMKQSPVELREVRRKKIGMVFQQFA--L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTS 182
Cdd:TIGR01186 83 FPHMTILQNTSLGPEL-LGWPEQERKEKALELLKLVGL---EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 183 ALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLLHD 256
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-241 |
6.81e-41 |
|
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: 146.94 E-value: 6.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADN-ARRDAGRIVLNGEVISDWSDKR 82
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGVSisLVPQDPgnslNPV-KTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLsHPEQRFDQYPHQLSGGMKQR 161
Cdd:cd03260 77 LELRRRVG--MVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL-WDEVKDRLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI 241
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
296-448 |
9.17e-41 |
|
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: 144.33 E-value: 9.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPFasLDPRQR 375
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 376 LFAIIEEPLkNFERLSAATRRQRVESVAARVAL---APELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATS 448
Cdd:pfam00005 76 VRENLRLGL-LLKGLSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
277-497 |
1.17e-40 |
|
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: 144.45 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqLR 356
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasldprqrlfaiieeplknferlsaatrrqrvesvaarvalapeLLSRTPRE--LSGGQRQRVAIARAL 434
Cdd:cd03228 76 KNIAYVPQDPF--------------------------------------------LFSGTIREniLSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 435 ILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLsyLFITHDLATVRRiADSVTVLRAGQ 497
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-232 |
1.51e-40 |
|
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: 145.48 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 5 SVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSdkrln 84
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI----KESSGSILLNGKPIKAKE----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 RLRgvSISLVPQDPGNSLnpvktIGQQVEEILRLHQSLsAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLI 164
Cdd:cd03226 69 RRK--SIGYVMQDVDYQL-----FTDSVREELLLGLKE-LDAGNEQAETVLKDLDLYALK---ERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 165 AIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
254-502 |
2.23e-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: 155.38 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 254 LHDLQDAPLGLTAARHRPLATPAIRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAD 333
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDIELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 334 AGQVTIDGIDAGHLSREAqrqLRRKIQFVYQNPFasldprqrLFA--IIE-----EPLKNFERLSAAtrrqrvesvaARV 406
Cdd:COG2274 529 SGRILIDGIDLRQIDPAS---LRRQIGVVLQDVF--------LFSgtIREnitlgDPDATDEEIIEA----------ARL 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 407 ALAPELLSRTP-----------RELSGGQRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLF 475
Cdd:COG2274 588 AGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALD--AETEAIILENLRRLLKGRTVII 665
|
250 260
....*....|....*....|....*..
gi 1031820327 476 ITHDLATVRRiADSVTVLRAGQVVEHG 502
Cdd:COG2274 666 IAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
277-502 |
2.94e-40 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 145.46 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlR 356
Cdd:cd03300 1 IELENVSKFY--GGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFAsLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:cd03300 72 RPVNTVFQN-YA-LFPHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-312 |
7.84e-40 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 146.77 E-value: 7.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 17 GEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEvisDWSDKRLNRLRGvSISLVPQ 96
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIE----PTSGRILIDGE---DIRDLDPVELRR-RIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 97 DPGnsLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLShPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLII 176
Cdd:COG1125 84 QIG--LFPHMTVAENIATVPRL-LGWDKERIRARVDELLELVGLD-PEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLL-H 255
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVgA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 256 DLQDAPLGLTAARHRPLATPAIRVEGISKRfslgkQALQALdsvsfeVRRGSTHALV 312
Cdd:COG1125 240 DRGLRRLSLLRVEDLMLPEPPTVSPDASLR-----EALSLM------LERGVDWLLV 285
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-249 |
1.32e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.14 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSD 80
Cdd:COG3839 1 MASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE----DPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRlnrlRGvsISLVPQDPGnsLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQ 160
Cdd:COG3839 73 KD----RN--IAMVFQSYA--LYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLED---LLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALD----VTVQKRILDLLdilrRESGTAVLFVTHD----LALaaerADRIMVFRQGEI 232
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLH----RRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRI 212
|
250
....*....|....*..
gi 1031820327 233 QEQGATETIVQRPQHPY 249
Cdd:COG3839 213 QQVGTPEELYDRPANLF 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
277-502 |
1.49e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.27 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:COG2884 2 IRFENVSKRYPGGREAL---SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFaSLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:COG2884 79 RRIGVVFQD-F-RLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 437 EPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:COG2884 155 RPELLLADEPTGNLDpetsweimelleeinrrgTTV-------------------LIATHDLELVDRMPKRVLELEDGRL 215
|
....
gi 1031820327 499 VEHG 502
Cdd:COG2884 216 VRDE 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
277-498 |
1.51e-39 |
|
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: 141.77 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGhlsrEAQRQLR 356
Cdd:cd03230 1 IEVRNLSKRY--GKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasldprqrlfaiieeplkNFERLSAAtrrqrvesvaarvalapELLsrtprELSGGQRQRVAIARALIL 436
Cdd:cd03230 73 RRIGYLPEEPS------------------LYENLTVR-----------------ENL-----KLSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 437 EPAILVLDEATSALDVtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:cd03230 113 DPELLILDEPTSGLDP-ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-232 |
1.83e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.04 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDK 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLV----EPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGvSISLVPQDPGNslnpvktIGQQ--VEEIL--RLHQ--------SLSAAERRQQVLNLLAKVGLS-HPEQRFD 148
Cdd:COG3638 74 ALRRLRR-RIGMIFQQFNL-------VPRLsvLTNVLagRLGRtstwrsllGLFPPEDRERALEALERVGLAdKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 149 QyphqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFR 228
Cdd:COG3638 146 Q----LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLR 221
|
....
gi 1031820327 229 QGEI 232
Cdd:COG3638 222 DGRV 225
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-254 |
1.86e-39 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 144.20 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVvhniSFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNA----RRDAGRIVLNGEVISDW 78
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDV----SFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHgtatYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 79 SDKRLNRlrgVSISLVPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLshPEQRFDQYPHQLSGGM 158
Cdd:TIGR02323 79 ERRRLMR---TEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEI--DPTRIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 159 KQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGAT 238
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLT 233
|
250
....*....|....*.
gi 1031820327 239 ETIVQRPQHPYTrQLL 254
Cdd:TIGR02323 234 DQVLDDPQHPYT-QLL 248
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
277-533 |
2.06e-39 |
|
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: 144.50 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghLSREAQRQLR 356
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNP---FASldprqrlfAIIEEP----LKNFeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVA 429
Cdd:TIGR04520 77 KKVGMVFQNPdnqFVG--------ATVEDDvafgLENL-GVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 430 IARALILEPAILVLDEATSALD-------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRRiADSV 490
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDpkgrkevletirklnkeegITV-------------------ISITHDMEEAVL-ADRV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1031820327 491 TVLRAGQVVEHGDVNRLFAapQQAYTRELIAAIPQVsSRLAQA 533
Cdd:TIGR04520 207 IVMNKGKIVAEGTPREIFS--QVELLKEIGLDVPFI-TELAKA 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-227 |
2.53e-39 |
|
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: 142.29 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 5 SVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKrln 84
Cdd:cd03235 1 EVEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL----KPTSGSIRVFGKPLEKERKR--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 rlrgvsISLVPQDPgnSLN---PVKtigqqVEEI--------LRLHQSLSAAERRQqVLNLLAKVGLSH-PEQRFDQyph 152
Cdd:cd03235 70 ------IGYVPQRR--SIDrdfPIS-----VRDVvlmglyghKGLFRRLSKADKAK-VDEALERVGLSElADRQIGE--- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 153 qLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVF 227
Cdd:cd03235 133 -LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-224 |
3.01e-39 |
|
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: 141.98 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 6 VEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLADnarRDAGRIVLNGEVISDWSDKRLNR 85
Cdd:TIGR03608 1 LKNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLN-IIGLLEK---FDSGQVYLNGQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 86 LRGVSISLVPQDPGNSLNpvktigQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRV 162
Cdd:TIGR03608 73 FRREKLGYLFQNFALIEN------ETVEENLDLglkYKKLSKKEKREKKKEALEKVGLNL---KLKQKIYELSGGEQQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALaAERADRI 224
Cdd:TIGR03608 144 ALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEV-AKQADRV 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
273-500 |
3.24e-39 |
|
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: 142.57 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ 352
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLR-RKIQFVYQNpfasldprqrlFAIIEE---------PLknfERLSAATRRQRVESVAARVALApELLSRTPRELSG 422
Cdd:COG4181 85 ARLRaRHVGFVFQS-----------FQLLPTltalenvmlPL---ELAGRRDARARARALLERVGLG-HRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVE 500
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
254-502 |
3.31e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.70 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 254 LHDLQDAPLGLTAARHRPLATPAIRVEGISkrFSLGKQAlQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAD 333
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVRGEIEFENVS--FSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 334 AGQVTIDGIDAGHLSREAqrqLRRKIQFVYQNPFasldprqrLFAI-IEEPLKnFERLSAAtrRQRVESvAARVALAPEL 412
Cdd:COG1132 394 SGRILIDGVDIRDLTLES---LRRQIGVVPQDTF--------LFSGtIRENIR-YGRPDAT--DEEVEE-AAKAAQAHEF 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 413 LSRTP-----------RELSGGQRQRVAIARALILEPAILVLDEATSALDV-----------------TVqaqilallqq 464
Cdd:COG1132 459 IEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTetealiqealerlmkgrTT---------- 528
|
250 260 270
....*....|....*....|....*....|....*...
gi 1031820327 465 lqqqlglsyLFITHDLATVRRiADSVTVLRAGQVVEHG 502
Cdd:COG1132 529 ---------IVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-452 |
4.17e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.41 E-value: 4.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRgvsISLVPQDPgnSLNP 104
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLY----QPDSGEILIDGKPVRIRSPRDAIALG---IGMVHQHF--MLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQQV----EEILRLHQSLSAAERRqqVLNLLAKVGLS-HPeqrfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:COG3845 94 NLTVAENIvlglEPTKGGRLDRKAARAR--IRELSERYGLDvDP----DAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 180 PTSALdvTVQKrILDLLDILRR--ESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIvqrpqhpyTRQLLHDL 257
Cdd:COG3845 168 PTAVL--TPQE-ADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET--------SEEELAEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 258 ---QDAPLGLTAARHRPlATPAIRVEGISKRfslGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA 334
Cdd:COG3845 237 mvgREVLLRVEKAPAEP-GEVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 335 GQVTIDGIDAGHLSREAQRqlRRKIQFVyqnpfasldP--RQRLFAIIEEP------LKNFERlSAATRRQRVESVAARv 406
Cdd:COG3845 313 GSIRLDGEDITGLSPRERR--RLGVAYI---------PedRLGRGLVPDMSvaenliLGRYRR-PPFSRGGFLDRKAIR- 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 407 ALAPELLS----RTP------RELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:COG3845 380 AFAEELIEefdvRTPgpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
277-497 |
4.56e-39 |
|
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: 140.40 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqRQLR 356
Cdd:cd03229 1 LELKNVSKRY--GQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL-PPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfasldprqRLFaiieePLKnferlsaatrrqrveSVAARVALApellsrtpreLSGGQRQRVAIARALIL 436
Cdd:cd03229 76 RRIGMVFQDF--------ALF-----PHL---------------TVLENIALG----------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQ 497
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
5.05e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 139.32 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRLNRlrgvSISLVPQDPgnSL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSH-PEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPT 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1031820327 182 S 182
Cdd:pfam00005 150 A 150
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
277-499 |
8.44e-39 |
|
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: 139.10 E-value: 8.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS-REAQrql 355
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQnpfasldprqrlfaiieeplknferlsaatrrqrvesvaarvalapellsrtpreLSGGQRQRVAIARALI 435
Cdd:cd03216 74 RAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 436 LEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:cd03216 99 RNARLLILDEPTAALTPA-EVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
277-507 |
1.13e-38 |
|
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: 141.16 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARIL-----LGFERADAGQVTIDGIDAGHLSREA 351
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRqLRRKIQFVYQ--NPFasldpRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRT-PRELSGGQRQRV 428
Cdd:cd03260 77 LE-LRRRVGMVFQkpNPF-----PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 429 AIARALILEPAILVLDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPI--STAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
275-499 |
1.93e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.96 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFSLGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQ 354
Cdd:COG3638 1 PMLELRNLSKRYPGGTPAL---DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVYQNPfaSLDPRQRLfaiieepLKN---------------FERLSAATRrQRVESVAARVALAPELLSRTpRE 419
Cdd:COG3638 78 LRRRIGMIFQQF--NLVPRLSV-------LTNvlagrlgrtstwrslLGLFPPEDR-ERALEALERVGLADKAYQRA-DQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 420 LSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
277-524 |
1.94e-38 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 141.63 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQALQALD----------------------SVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA 334
Cdd:cd03294 1 IKIKGLYKIF--GKNPQKAFKllakgkskeeilkktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 335 GQVTIDGIDAGHLSREAQRQLRRK-IQFVYQNpFAsLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALAPeLL 413
Cdd:cd03294 79 GKVLIDGQDIAAMSRKELRELRRKkISMVFQS-FA-LLPHRTVLENVAFGLE-VQGVPRAEREERAAEALELVGLEG-WE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 414 SRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:cd03294 155 HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM 234
|
250 260 270
....*....|....*....|....*....|.
gi 1031820327 494 RAGQVVEHGDVNRLFAAPQQAYTRELIAAIP 524
Cdd:cd03294 235 KDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
254-510 |
2.27e-38 |
|
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: 147.98 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 254 LHDLQDAPLGLTAARHRPL---ATPAIRVEGISKRFSLGKQALQaldSVSFEVRRGSTHALVGESGSGKTTLARILLGFE 330
Cdd:COG4988 311 IFALLDAPEPAAPAGTAPLpaaGPPSIELEDVSFSYPGGRPALD---GLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 331 RADAGQVTIDGIDAGHLSREaqrQLRRKIQFVYQNPFasldprqrLFAI-IEEPLknfeRLSA--ATRrQRVESVAARVA 407
Cdd:COG4988 388 PPYSGSILINGVDLSDLDPA---SWRRQIAWVPQNPY--------LFAGtIRENL----RLGRpdASD-EELEAALEAAG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 408 LApELLSRTP-----------RELSGGQRQRVAIARALILEPAILVLDEATSALDV-----------------TVqaqil 459
Cdd:COG4988 452 LD-EFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAeteaeilqalrrlakgrTV----- 525
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 460 allqqlqqqlglsyLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:COG4988 526 --------------ILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
279-526 |
2.50e-38 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 148.85 E-value: 2.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 279 VEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGI-------DAGHLSREA 351
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQLRR----KIQFVYQNPFASLDPrqrLFAIIEEPLKNFeRLSAATRRQRVESVA------ARVALAPELLSRTPRELS 421
Cdd:PRK10261 95 AAQMRHvrgaDMAMIFQEPMTSLNP---VFTVGEQIAESI-RLHQGASREEAMVEAkrmldqVRIPEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 422 GGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEH 501
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260
....*....|....*....|....*
gi 1031820327 502 GDVNRLFAAPQQAYTRELIAAIPQV 526
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVPQL 275
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-231 |
3.25e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 138.09 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRgvSISLVPQDPG 99
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLTDLEDELPPLRR--RIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nsLNPVKTIGQQVeeilrlhqslsaaerrqqvlnllakvglshpeqrfdQYPhqLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:cd03229 87 --LFPHLTVLENI------------------------------------ALG--LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 180 PTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
273-504 |
3.64e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.71 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG----IDAghlS 348
Cdd:COG3845 2 MPPALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrIRS---P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 349 REAqrqLRRKIQFVYQNPfaSLDPRqrlFAIIE------EPLKNFeRLSAATRRQRVESVAARVALAPElLSRTPRELSG 422
Cdd:COG3845 75 RDA---IALGIGMVHQHF--MLVPN---LTVAEnivlglEPTKGG-RLDRKAARARIRELSERYGLDVD-PDAKVEDLSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSAL------------------DVTVqaqilallqqlqqqlglsyLFITHDLATVR 484
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLtpqeadelfeilrrlaaeGKSI-------------------IFITHKLREVM 205
|
250 260
....*....|....*....|
gi 1031820327 485 RIADSVTVLRAGQVVEHGDV 504
Cdd:COG3845 206 AIADRVTVLRRGKVVGTVDT 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-277 |
5.01e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.29 E-value: 5.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLriSYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTaqaiIGLLADNARRDAGRIVLNGEVISDWSDK 81
Cdd:PRK13548 1 AMLEARNL--SVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSGELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGVsislVPQDpgNSLN-PVKtigqqVEEILRL---HQSLSAAERRQQVLNLLAKVGLSHPEQRFdqYPhQLSGG 157
Cdd:PRK13548 73 ELARRRAV----LPQH--SSLSfPFT-----VEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 158 MKQRVLIAIAIA------LQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:PRK13548 139 EQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1031820327 232 IQEQGAtetivqrPQHPYTRQLLHDLQDAPLGLTaaRHRPLATPAI 277
Cdd:PRK13548 219 LVADGT-------PAEVLTPETLRRVYGADVLVQ--PHPETGAPLV 255
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
276-523 |
5.62e-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: 140.18 E-value: 5.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReaqRQL 355
Cdd:COG1120 1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQNPFASLD------------PRQRLFAiieeplknfeRLSAATRrQRVESVAARVALApELLSRTPRELSGG 423
Cdd:COG1120 74 ARRIAYVPQEPPAPFGltvrelvalgryPHLGLFG----------RPSAEDR-EAVEEALERTGLE-HLADRPVDELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 424 QRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGd 503
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG- 220
|
250 260
....*....|....*....|
gi 1031820327 504 vnrlfaAPQQAYTRELIAAI 523
Cdd:COG1120 221 ------PPEEVLTPELLEEV 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-244 |
1.12e-37 |
|
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: 138.84 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKR 82
Cdd:COG4555 1 MIEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL----KPDSGSILIDGEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRlrgvsISLVPQDPGnsLNPVKTigqqVEEILRLH---QSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMK 159
Cdd:COG4555 73 RRQ-----IGVLPDERG--LYDRLT----VRENIRYFaelYGLFDEELKKRIEELIELLGLEEFL---DRRVGELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
....*
gi 1031820327 240 TIVQR 244
Cdd:COG4555 218 ELREE 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-275 |
1.42e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.10 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLriSYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:COG4559 2 LEAENL--SVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGEL----TPSSGEVRLNGRPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVsislVPQDpgNSLN-PVKtigqqVEEILRL---HQSLSAAERRQQVLNLLAKVGLSHPEQRFdqYPhQLSGGMK 159
Cdd:COG4559 74 ARRRAV----LPQH--SSLAfPFT-----VEEVVALgraPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIA-------LQPDLIIADEPTSALDVTVQkriLDLLDILRR--ESGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQ---HAVLRLARQlaRRGGGVVAVLHDLNLAAQYADRILLLHQG 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1031820327 231 EIQEQGATETIVqrpqhpyTRQLLHDLQDAPlgLTAARHRPLATP 275
Cdd:COG4559 217 RLVAQGTPEEVL-------TDELLERVYGAD--LRVLAHPEGGCP 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-280 |
1.64e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.48 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRLNRL 86
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL----ERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 RGvSISLVPQDpGNSLNPvKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAI 166
Cdd:PRK11153 81 RR-QIGMIFQH-FNLLSS-RTVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSD---KADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 167 AIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQ 246
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 1031820327 247 HPYTRQLLHDL--QDAPLGLTAARHRPLAT---PAIRVE 280
Cdd:PRK11153 234 HPLTREFIQSTlhLDLPEDYLARLQAEPTTgsgPLLRLE 272
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
279-531 |
2.04e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 140.65 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 279 VEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGF----ERADAGQVTIDGIDAGHLSREAQRQ 354
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 L-RRKIQFVYQNPFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALaPELLSRT---PRELSGGQRQRVAI 430
Cdd:PRK11022 86 LvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRLdvyPHQLSGGMSQRVMI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 431 ARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
250 260
....*....|....*....|....
gi 1031820327 511 PQQAYTRELIAAIPQVS---SRLA 531
Cdd:PRK11022 245 PRHPYTQALLRALPEFAqdkARLA 268
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
293-531 |
2.90e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 140.43 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 293 LQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERaDAGQVTID-----GIDAGHLSREAQRQL-RRKIQFVYQNP 366
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADrfrwnGIDLLKLSPRERRKIiGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FASLDP-----RQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALA--PELLSRTPRELSGGQRQRVAIARALILEPA 439
Cdd:COG4170 99 SSCLDPsakigDQLIEAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 440 ILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTREL 519
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKAL 258
|
250
....*....|..
gi 1031820327 520 IAAIPQVSSRLA 531
Cdd:COG4170 259 LRSMPDFRQPLP 270
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
277-498 |
3.18e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQalqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLR 356
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasldprqrLFA-----IIEEPLKNFERlsaATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIA 431
Cdd:COG4619 74 RQVAYVPQEPA--------LWGgtvrdNLPFPFQLRER---KFDRERALELLERLGLPPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 432 RALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-523 |
4.02e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISkrFSLGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlsreaq 352
Cdd:COG1121 3 MMPAIELENLT--VSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQNpfASLDPRqrlFAI-IEE--------PLKNFERLSAAtRRQRVESVAARVALApELLSRTPRELSGG 423
Cdd:COG1121 71 RRARRRIGYVPQR--AEVDWD---FPItVRDvvlmgrygRRGLFRRPSRA-DREAVDEALERVGLE-DLADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 424 QRQRVAIARALILEPAILVLDEATSALDV------------------TVqaqilallqqlqqqlglsyLFITHDLATVRR 485
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAateealyellrelrregkTI-------------------LVVTHDLGAVRE 204
|
250 260 270
....*....|....*....|....*....|....*...
gi 1031820327 486 IADSVTVLrAGQVVEHGDvnrlfaaPQQAYTRELIAAI 523
Cdd:COG1121 205 YFDRVLLL-NRGLVAHGP-------PEEVLTPENLSRA 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-232 |
4.24e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.10 E-value: 4.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSdkrL 83
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLD----PPTSGEIYLDGKPLSAMP---P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDPGnslnpvkTIGQQVEEILRLHQSLSAAE-RRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRV 162
Cdd:COG4619 70 PEWRR-QVAYVPQEPA-------LWGGTVRDNLPFPFQLRERKfDRERALELLERLGL--PPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
25-279 |
4.81e-37 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 140.17 E-value: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRlnrlRGVSIslVPQDpgNSLNP 104
Cdd:TIGR03265 22 DISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL----ERQTAGTIYQGGRDITRLPPQK----RDYGI--VFQS--YALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQQVEEILRlHQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSAL 184
Cdd:TIGR03265 90 NLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 185 DVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRP-------------QHPYTR 251
Cdd:TIGR03265 166 DARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPatpfvadfvgevnWLPGTR 245
|
250 260
....*....|....*....|....*...
gi 1031820327 252 QLLHDLQDAPLGLTAARHRPLATPAIRV 279
Cdd:TIGR03265 246 GGGSRARVGGLTLACAPGLAQPGASVRL 273
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-232 |
5.56e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 136.93 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP----TSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDPGNslnpvktIGQQ--VEEIL--RLHQ--------SLSAAERRQQVLNLLAKVGLS-HPEQRFDQy 150
Cdd:cd03256 74 RQLRR-QIGMIFQQFNL-------IERLsvLENVLsgRLGRrstwrslfGLFPKEEKQRALAALERVGLLdKAYQRADQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 151 phqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:cd03256 145 ---LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
..
gi 1031820327 231 EI 232
Cdd:cd03256 222 RI 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
271-503 |
7.34e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.43 E-value: 7.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 271 PLATPAIRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSRE 350
Cdd:PRK13632 2 KNKSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT---ISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 351 AQRQLRRKIQFVYQNPfasldPRQRLFAIIEEP----LKNfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQ 426
Cdd:PRK13632 77 NLKEIRKKIGIIFQNP-----DNQFIGATVEDDiafgLEN-KKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVrRIADSVTVLRAGQVVEHGD 503
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
277-502 |
7.48e-37 |
|
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: 135.96 E-value: 7.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqlR 356
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVyqnpFASLDPRQRLFAiiEEPLKNFERLSAATRRQ---RVESVAARVALApELLSRTPRELSGGQRQRVAIARA 433
Cdd:cd03266 78 RRLGFV----SDSTGLYDRLTA--RENLEYFAGLYGLKGDEltaRLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 434 LILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMA-TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-246 |
9.39e-37 |
|
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: 136.21 E-value: 9.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDW-SDKRlnrlrgvSISLVPQDpgN 100
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPTSGEILLDGKDITNLpPHKR-------PVNTVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 SLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLIIADEP 180
Cdd:cd03300 82 ALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 181 TSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQ 246
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
286-510 |
1.11e-36 |
|
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: 135.82 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 286 FSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQN 365
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 366 PFasldprqrLFA-IIEEPLKnFERLSAAtrRQRVESvAARVALAPELLSRTPR-----------ELSGGQRQRVAIARA 433
Cdd:cd03251 85 VF--------LFNdTVAENIA-YGRPGAT--REEVEE-AARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 434 LILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:cd03251 153 LLKDPPILILDEATSALD--TESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
277-522 |
3.40e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 134.74 E-value: 3.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLR 356
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED---IREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpfASLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALAP-ELLSRTPRELSGGQRQRVAIARALI 435
Cdd:cd03295 75 RKIGYVIQQ--IGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 436 LEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAY 515
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
....*..
gi 1031820327 516 TRELIAA 522
Cdd:cd03295 232 VAEFVGA 238
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
271-526 |
3.89e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 135.05 E-value: 3.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 271 PLATPAIRVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG----- 345
Cdd:PRK11701 1 MMDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdly 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 346 HLSrEAQRQ--LRRKIQFVYQNPFASLDPRQRLFAIIEEPL-----KNFERLsaatrRQRVESVAARVALAPELLSRTPR 418
Cdd:PRK11701 77 ALS-EAERRrlLRTEWGFVHQHPRDGLRMQVSAGGNIGERLmavgaRHYGDI-----RATAGDWLERVEIDAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 419 ELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250 260
....*....|....*....|....*...
gi 1031820327 499 VEHGDVNRLFAAPQQAYTRELIAAIPQV 526
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYTQLLVSSVLQV 258
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-502 |
5.89e-36 |
|
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: 133.15 E-value: 5.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlR 356
Cdd:cd03301 1 VELENVTKRF--GNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpFAsLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:cd03301 72 RDIAMVFQN-YA-LYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
295-526 |
6.51e-36 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 136.78 E-value: 6.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAD---AGQVTIDGIDAGHLSREAQRQLR-RKIQFVYQNPFASL 370
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRaEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 371 DPRQRLFAIIEEPLKNFERLSAATRRQrvESVAARVALA-PELLSRT---PRELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAEAFE--ESVRMLDAVKmPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 447 TSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAIPQV 526
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRL 268
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-235 |
8.34e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.22 E-value: 8.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSD 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAP----SSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRlnrlrGVsislVPQDpgNSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQ 160
Cdd:COG4525 77 DR-----GV----VFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVF--RQGEIQEQ 235
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-251 |
8.38e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.39 E-value: 8.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGL--LADNARRDaGRIVLNGEVISDwS 79
Cdd:COG1117 10 PKIEVRNLNVYY---GD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGARVE-GEILLDGEDIYD-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 DKRLNRLRgVSISLVPQDPgnslNPV-KTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGL-SHPEQRFDQYPHQLSGG 157
Cdd:COG1117 84 DVDVVELR-RRVGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDRLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 158 MKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
250
....*....|....
gi 1031820327 238 TETIVQRPQHPYTR 251
Cdd:COG1117 237 TEQIFTNPKDKRTE 250
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
276-520 |
1.04e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 133.72 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSlGKQALQALDsvsFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAGHLSREAQ- 352
Cdd:PRK11264 3 AIEVKNLVKKFH-GQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitIDTARSLSQQKg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 --RQLRRKIQFVYQNpFASLDPRQRLFAIIEEPL--KNFERLSAAtrrQRVESVAARVALAPELlSRTPRELSGGQRQRV 428
Cdd:PRK11264 79 liRQLRQHVGFVFQN-FNLFPHRTVLENIIEGPVivKGEPKEEAT---ARARELLAKVGLAGKE-TSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 429 AIARALILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLF 508
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPEL-VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|..
gi 1031820327 509 AAPQQAYTRELI 520
Cdd:PRK11264 233 ADPQQPRTRQFL 244
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-231 |
1.40e-35 |
|
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: 132.37 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGvSISLVPQDpg 99
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGAL----TPSRGQVRIAGEDVNRLRGRQLPLLRR-RIGVVFQD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:TIGR02673 88 FRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 180 PTSALDVTVQKRILDLLDILRReSGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-232 |
1.60e-35 |
|
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: 132.45 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnaRR-DAGRIVLNGEVISDWSDK 81
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGL-----RSvQEGSLKVLGQELHGASKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGvSISLVPQdpGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQR 161
Cdd:TIGR02982 76 QLVQLRR-RIGYIFQ--AHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALaAERADRIMVFRQGEI 232
Cdd:TIGR02982 150 VAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRI-LDVADRILQMEDGKL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
272-513 |
1.83e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 272 LATPAIRVEGISKRFSlgKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREA 351
Cdd:PRK13635 1 MKEEIIRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQLRRKIQFVYQNPfasldPRQRLFAIIEEP----LKN--------FERLSAATRRQRVEsvaarvalapELLSRTPRE 419
Cdd:PRK13635 76 VWDVRRQVGMVFQNP-----DNQFVGATVQDDvafgLENigvpreemVERVDQALRQVGME----------DFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 420 LSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVV 499
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
250
....*....|....
gi 1031820327 500 EHGDVNRLFAAPQQ 513
Cdd:PRK13635 220 EEGTPEEIFKSGHM 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
277-499 |
1.87e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 132.69 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:cd03256 1 IEVENLSKTYPNGKKAL---KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpfasldprqrlFAIIEE----------------PLKNFERLSAATRRQRVESVAARVALAPELLSRTpREL 420
Cdd:cd03256 78 RQIGMIFQQ-----------FNLIERlsvlenvlsgrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRA-DQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 421 SGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-241 |
2.34e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.42 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKR 82
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSS----GSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDpgNSLNPVKTIGQQVeeilrLHQSLSAA------------ERRQQVLNLLAKVGLSH-PEQRFDQ 149
Cdd:TIGR02315 74 LRKLRR-RIGMIFQH--YNLIERLTVLENV-----LHGRLGYKptwrsllgrfseEDKERALSALERVGLADkAYQRADQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 150 yphqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQ 229
Cdd:TIGR02315 146 ----LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKA 221
|
250
....*....|..
gi 1031820327 230 GEIQEQGATETI 241
Cdd:TIGR02315 222 GEIVFDGAPSEL 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-254 |
2.66e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.57 E-value: 2.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIiGLLAdnaRRDAGRIVLnGEVISDwSD 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLE---QPEAGTIRV-GDITID-TA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVsISLVPQDPG---NSLN--PVKTIGQQVEE---ILRLHQSLSAAERRQQvlnLLAKVGLSHPEqrfDQYPH 152
Cdd:PRK11264 71 RSLSQQKGL-IRQLRQHVGfvfQNFNlfPHRTVLENIIEgpvIVKGEPKEEATARARE---LLAKVGLAGKE---TSYPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRI 222
|
250 260
....*....|....*....|..
gi 1031820327 233 QEQGATETIVQRPQHPYTRQLL 254
Cdd:PRK11264 223 VEQGPAKALFADPQQPRTRQFL 244
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
277-451 |
3.42e-35 |
|
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: 131.11 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHlSREAQRQLR 356
Cdd:cd03262 1 IEIKNLHKSFG----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQ--NPFASLDPRQRlfaiIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRtPRELSGGQRQRVAIARAL 434
Cdd:cd03262 76 QKVGMVFQqfNLFPHLTVLEN----ITLAPIKVKGMSKAEAEERALELLEKVGLADKADAY-PAQLSGGQQQRVAIARAL 150
|
170
....*....|....*..
gi 1031820327 435 ILEPAILVLDEATSALD 451
Cdd:cd03262 151 AMNPKVMLFDEPTSALD 167
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-252 |
3.43e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 136.00 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDPGnsL 102
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI----EPTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQHFA--L 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVE---EIlrlhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:COG4175 117 LPHRTVLENVAfglEI----QGVPKAERRERAREALELVGL---AGWEDSYPDELSGGMQQRVGLARALATDPDILLMDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 180 PTSALDVTVQKRILD-LLDiLRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQ 252
Cdd:COG4175 190 AFSALDPLIRREMQDeLLE-LQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVAD 262
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
277-514 |
5.23e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.42 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQALQAldsvSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSrEAQRQLr 356
Cdd:COG3840 2 LRLDDLTYRY--GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 rKIQFVYQNPFASLDPRQRLFAIIEEPLknfeRLSAAtRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALIL 436
Cdd:COG3840 74 -SMLFQENNLFPHLTVAQNIGLGLRPGL----KLTAE-QRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 437 EPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQA 514
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
294-509 |
7.03e-35 |
|
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: 131.12 E-value: 7.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPFasldpr 373
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLRSQIGLVSQEPV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 qrLFAI-IEEPLknfeRLSAATRRQRVESVAARVALAPELLSRTPR-----------ELSGGQRQRVAIARALILEPAIL 441
Cdd:cd03249 88 --LFDGtIAENI----RYGKPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 442 VLDEATSALDVTVQAQILALLQQLQQQLGLsyLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-254 |
9.22e-35 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 130.92 E-value: 9.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRLNrlrgvsISLVPQDpgNSL 102
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL----ERPDSGTILFGGEDATDVPVQERN------VGFVFQH--YAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVE---EILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:cd03296 86 FRHMTVFDNVAfglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 180 PTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLL 254
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-231 |
1.04e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 128.27 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03228 1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY----DPTSGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvSISLVPQDPgnslnpvktigqqveeiLRLHQSLsaAErrqqvlNLlakvglshpeqrfdqyphqLSGGMKQRVL 163
Cdd:cd03228 75 RK----NIAYVPQDP-----------------FLFSGTI--RE------NI-------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALaAERADRIMVFRQGE 231
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
277-502 |
3.31e-34 |
|
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: 128.88 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISkrFSLGKQAlQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrQLR 356
Cdd:cd03254 3 IEFENVN--FSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK---SLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasldprqrLFA--IIEeplkNFeRLSAATRRQRVESVAARVALAPELLSRTPR-----------ELSGG 423
Cdd:cd03254 77 SMIGVVLQDTF--------LFSgtIME----NI-RLGRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 424 QRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHG 502
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNID--TETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
277-503 |
4.18e-34 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 128.71 E-value: 4.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS--REAQRQ 354
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPphEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVyqNPFASLDPRQ-----RLFAIIEEPLKNFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVA 429
Cdd:cd03219 77 IGRTFQIP--RLFPELTVLEnvmvaAQARTGSGLLLARARREEREARERAEELLERVGLA-DLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 430 IARALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGD 503
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPE-ETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-231 |
4.96e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 126.21 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 5 SVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLN 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 RLrgvsISLVPQdpgnslnpvktigqqveeilrlhqslsaaerrqqvlnllakvglshpeqrfdqyphqLSGGMKQRVLI 164
Cdd:cd00267 73 RR----IGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 165 AIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-236 |
8.11e-34 |
|
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: 127.40 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP----DSGEVLFDGKPLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrgvsislvPQDPGnsLNPVKTIGQQVEEILRLHqSLSAAERRQQVLNLLAKVGLS-HPEQRFDQyphqLSGGMKQRV 162
Cdd:cd03269 73 GYL--------PEERG--LYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSeYANKRVEE----LSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
8.97e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.96 E-value: 8.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDwsdKR 82
Cdd:PRK13632 7 MIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS----GEIKIDGITISK---EN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDPGNSLnpvktIGQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMK 159
Cdd:PRK13632 78 LKEIRK-KIGIIFQNPDNQF-----IGATVEDDIAFgleNKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGKPK 227
|
...
gi 1031820327 240 TIV 242
Cdd:PRK13632 228 EIL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
273-503 |
1.12e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 128.23 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS--RE 350
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 351 AQRQLRRKiqfvYQNP--FASLD------------PRQRLFAIIEEPLKNFERLSAAtrRQRVESVAARVALApELLSRT 416
Cdd:COG0411 77 ARLGIART----FQNPrlFPELTvlenvlvaaharLGRGLLAALLRLPRARREEREA--RERAEELLERVGLA-DRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 417 PRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAG 496
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
....*..
gi 1031820327 497 QVVEHGD 503
Cdd:COG0411 230 RVIAEGT 236
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
9-245 |
1.84e-33 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 130.20 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 9 LRISYRSRgEWREV-VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRlnrlR 87
Cdd:NF040840 2 IRIENLSK-DWKEFkLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPP----DSGKIYLDGKDITNLPPEK----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 88 GvsISLVPQDpgNSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIA 167
Cdd:NF040840 73 G--IAYVYQN--YMLFPHKTVFENIAFGLKL-RKVPKEEIERKVKEIMELLGISHLLHR---KPRTLSGGEQQRVALARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 168 IALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:NF040840 145 LIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRP 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-315 |
2.54e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.69 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKR 82
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP----DSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 lnrlrgvsISLVPQDPGnsLNPVKTIGQQVEEILRLHQsLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRV 162
Cdd:COG4152 73 --------IGYLPEERG--LYPKMKVGEQLVYLARLKG-LSKAEAKRRADEWLERLGLGD---RANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALD-VTVQKrildLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDpVNVEL----LKDVIRelAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 240 TIvqRPQHPYTRQLLHDLQDAPL-----GLTAARHRPLATpAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTH----A 310
Cdd:COG4152 215 EI--RRQFGRNTLRLEADGDAGWlralpGVTVVEEDGDGA-ELKLEDGADAQELLRALLARGPVREFEEVRPSLNeifiE 291
|
....*
gi 1031820327 311 LVGES 315
Cdd:COG4152 292 VVGEK 296
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
299-502 |
3.09e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 125.87 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 299 VSFEVRrGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIdaghLSREAQRQL-----RRKIQFVYQNpfASLDPR 373
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT----VLFDSRKKInlppqQRKIGLVFQQ--YALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 QRLFAIIEEPLKnfeRLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVT 453
Cdd:cd03297 90 LNVRENLAFGLK---RKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1031820327 454 VQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-244 |
3.21e-33 |
|
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: 133.34 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRL 83
Cdd:COG4988 337 IELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP----YSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrgvsISLVPQDP----GNslnpvktigqqVEEILRLHQSlSAAErrQQVLNLLAKVGLSHpeqrF-DQYPH------ 152
Cdd:COG4988 410 RRQ----IAWVPQNPylfaGT-----------IRENLRLGRP-DASD--EELEAALEAAGLDE----FvAALPDgldtpl 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 -----QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALAAeRADRIMVF 227
Cdd:COG4988 468 geggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVL 544
|
250
....*....|....*..
gi 1031820327 228 RQGEIQEQGATETIVQR 244
Cdd:COG4988 545 DDGRIVEQGTHEELLAK 561
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-245 |
5.16e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.05 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISdwsdkRLN-RLRGVSisLVPQDp 98
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS----GHIRFHGTDVS-----RLHaRDRKVG--FVFQH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 gNSLNPVKTIGQQVE---EILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLI 175
Cdd:PRK10851 83 -YALFRHMTVFDNIAfglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 176 IADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-236 |
5.59e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 125.10 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQrGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVisdWSDKRLNrlrgvsISLVPQDPG----- 99
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTV---LFDSRKK------INLPPQQRKiglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 --NSLNPVKTIGQQVEEILRLHqslSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLIIA 177
Cdd:cd03297 82 qqYALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 178 DEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-236 |
5.64e-33 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 125.31 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGevISDWSDKRL 83
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL----RPTSGTAYING--YSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgVSISLVPQDpgNSLNPVKTigqqVEEILRLH---QSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQ 160
Cdd:cd03263 73 AR---QSLGYCPQF--DALFDELT----VREHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKA---NKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESgtAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
294-502 |
6.48e-33 |
|
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: 125.81 E-value: 6.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPFasldpr 373
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAIGVVPQDTV------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 qrLF-AIIEEPLKnFERLSaATRRQRVEsvAARVALAPELLSRTPR-----------ELSGGQRQRVAIARALILEPAIL 441
Cdd:cd03253 86 --LFnDTIGYNIR-YGRPD-ATDEEVIE--AAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 442 VLDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHG 502
Cdd:cd03253 160 LLDEATSALDTH--TEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
276-512 |
9.10e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.51 E-value: 9.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKrfSLGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGID---AGHLSREAQ 352
Cdd:COG4161 2 SIQLKNINC--FYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQ--NPFASLDPRQRLfaiIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAI 430
Cdd:COG4161 78 RLLRQKVGMVFQqyNLWPHLTVMENL---IEAPCK-VLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 431 ARALILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNrLFAA 510
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEI-TAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQ 230
|
..
gi 1031820327 511 PQ 512
Cdd:COG4161 231 PQ 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
276-512 |
1.10e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.13 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISkrFSLGkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIdgidAGH---LSREAQ 352
Cdd:PRK11124 2 SIQLNGIN--CFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI----AGNhfdFSKTPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 ----RQLRRKIQFVYQ--NPFASLDPRQRLfaiIEEPLKNFErLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQ 426
Cdd:PRK11124 74 dkaiRELRRNVGMVFQqyNLWPHLTVQQNL---IEAPCRVLG-LSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDvNR 506
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEI-TAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-AS 226
|
....*.
gi 1031820327 507 LFAAPQ 512
Cdd:PRK11124 227 CFTQPQ 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
311-523 |
1.88e-32 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 126.84 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 311 LVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlRRKIQFVYQNpfASLDPRQRLFAIIEEPLKnFERL 390
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQS--YALFPHMTVEENVAFGLK-MRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 391 SAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLG 470
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 471 LSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAI 523
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
285-502 |
1.97e-32 |
|
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: 123.76 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 285 RFSLGKQALQaldsVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlRRKIQFVYQ 364
Cdd:cd03298 7 RFSYGEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 365 --NPFASLDPRQRLFAIIEEPLKnferlSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILV 442
Cdd:cd03298 78 enNLFAHLTVEQNVGLGLSPGLK-----LTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 443 LDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
265-510 |
2.61e-32 |
|
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: 130.61 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 265 TAARHRPLATPAIRVEGISKRFslGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDA 344
Cdd:TIGR02203 319 TGTRAIERARGDVEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 345 GHLSreaQRQLRRKIQFVYQNPFASLDPrqrLFAIIEeplknFERLSAATRrQRVESvAARVALAPELLSRTPR------ 418
Cdd:TIGR02203 397 ADYT---LASLRRQVALVSQDVVLFNDT---IANNIA-----YGRTEQADR-AEIER-ALAAAYAQDFVDKLPLgldtpi 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 419 -----ELSGGQRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVL 493
Cdd:TIGR02203 464 gengvLLSGGQRQRLAIARALLKDAPILILDEATSALD--NESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVM 540
|
250
....*....|....*..
gi 1031820327 494 RAGQVVEHGDVNRLFAA 510
Cdd:TIGR02203 541 DDGRIVERGTHNELLAR 557
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
21-254 |
2.62e-32 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 124.14 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEvisdwsDKRLNRLRGVSISLVPQDpgN 100
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL----EQPDSGRIRLNGQ------DATRVHARDRKIGFVFQH--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 SLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEP 180
Cdd:TIGR00968 82 ALFKHLTVRDNIAFGLEI-RKHPKAKIKARVEELLELVQLEGLG---DRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 181 TSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLL 254
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-249 |
2.81e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 131.49 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWreVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSdkrL 83
Cdd:COG2274 474 IELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP----TSGRILIDGIDLRQID---P 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDP----GNslnpvktigqqVEEILRL-HQSLSaaerRQQVLNLLAKVGL-----SHPeqrfDQYPHQ 153
Cdd:COG2274 545 ASLRR-QIGVVLQDVflfsGT-----------IRENITLgDPDAT----DEEIIEAARLAGLhdfieALP----MGYDTV 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 154 -------LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDilRRESGTAVLFVTHDLALAAeRADRIMV 226
Cdd:COG2274 605 vgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR--RLLKGRTVIIIAHRLSTIR-LADRIIV 681
|
250 260
....*....|....*....|...
gi 1031820327 227 FRQGEIQEQGATETIVQRPQHPY 249
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-236 |
3.66e-32 |
|
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: 122.75 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRLNrlrgvsISLVPQDpg 99
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL----EEPTSGRIYIGGRDVTDLPPKDRD------IAMVFQN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQVEEILRLHQSlSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQIEH---LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 180 PTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-224 |
4.72e-32 |
|
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: 122.20 E-value: 4.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISyrsRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKR 82
Cdd:COG4133 2 MLEAENLSCR---RGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL----PPSAGEVLWNGEPIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLrgvsiSLVPQDPGnsLNPVKTigqqVEEILRLHQSLSAAER-RQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQR 161
Cdd:COG4133 74 RRRL-----AYLGHADG--LKPELT----VRENLRFWAALYGLRAdREAIDEALEAVGLAG---LADLPVRQLSAGQKRR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDIlRRESGTAVLFVTHDlALAAERADRI 224
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ-PLELAAARVL 200
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
295-511 |
5.31e-32 |
|
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: 126.37 E-value: 5.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDsVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG-----IDAGH-LSREaqrqlRRKIQFVYQNP-- 366
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdSARGIfLPPH-----RRRIGYVFQEArl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FASLDPRQRL-FAIieeplknfERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:COG4148 89 FPHLSVRGNLlYGR--------KRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 446 ATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
277-499 |
6.47e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 123.18 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQAldsVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKN---INLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpfASLDPRQrlfAIIEEPL------KNFER--LSAATRRQRVESVAA--RVALAPELLSRTpRELSGGQRQ 426
Cdd:TIGR02315 79 RRIGMIFQH--YNLIERL---TVLENVLhgrlgyKPTWRslLGRFSEEDKERALSAleRVGLADKAYQRA-DQLSGGQQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-451 |
7.98e-32 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 130.63 E-value: 7.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLAdNARR-DAGRI-VLNGevisDWSD 80
Cdd:NF033858 1 VARLEGVSHRYGKT----VALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIA-GARKiQQGRVeVLGG----DMAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVPQDPGNSLNPVKTigqqVEEILRLHQSL---SAAERRQQVLNLLAKVGLShpeqRFDQYPH-QLSG 156
Cdd:NF033858 68 ARHRRAVCPRIAYMPQGLGKNLYPTLS----VFENLDFFGRLfgqDAAERRRRIDELLRATGLA----PFADRPAgKLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 157 GMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRES-GTAVLFVThdlalA----AERADRIMVFRQGE 231
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT-----AymeeAERFDWLVAMDAGR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 232 IQEQGATETIVQRPQHPytrqllhDLQDAPLGL--TAAR--HRPLATP----------AIRVEGISKRFSlgkqALQALD 297
Cdd:NF033858 215 VLATGTPAELLARTGAD-------TLEAAFIALlpEEKRrgHQPVVIPprpaddddepAIEARGLTMRFG----DFTAVD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 298 SVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAGHLSreaqrqLRRKIQF------------VY 363
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIA------TRRRVGYmsqafslygeltVR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 364 QNpfasLDPRQRLFaiieeplknfeRLSAATRRQRVESVAARVALAPELLSRtPRELSGGQRQRVAIARALILEPAILVL 443
Cdd:NF033858 358 QN----LELHARLF-----------HLPAAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
....*...
gi 1031820327 444 DEATSALD 451
Cdd:NF033858 422 DEPTSGVD 429
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
297-522 |
8.95e-32 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 122.89 E-value: 8.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 297 DSVSFEVRRGSTHALVGESGSGKTTLARILLGF----ERADAGQVTIDGIDAghlsreAQRQLR-RKIQFVYQNPFASLD 371
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPV------APCALRgRKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 PRQRLFAIIEEPLKNFERLSA-ATRRQRVESVAarVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPADdATLTAALEAVG--LENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 451 DVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAA 522
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-232 |
1.53e-31 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 121.36 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 24 HNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRLNRLRGvSISLVPQDpgNSLN 103
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKST----LLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 104 PVKTIGQQVEEILRLHQSlSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSA 183
Cdd:cd03292 91 PDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1031820327 184 LDVTVQKRILDLLDILRReSGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:cd03292 167 LDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-254 |
1.85e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNG-EVISDWSDKRLNRLRGVSI----SLVP 95
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL----EEITSGDLIVDGlKVNDPKVDERLIRQEAGMVfqqfYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 96 QDPG--N-SLNPVKTIGQqveeilrlhqslSAAERRQQVLNLLAKVGLShpeQRFDQYPHQLSGGMKQRVLIAIAIALQP 172
Cdd:PRK09493 91 HLTAleNvMFGPLRVRGA------------SKEEAEKQARELLAKVGLA---ERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 173 DLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQ 252
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
..
gi 1031820327 253 LL 254
Cdd:PRK09493 235 FL 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-254 |
2.48e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.02 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRsrgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWS-DKR 82
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP----DSGRILWNGQDLTALPpAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 lnrlrgvSISLVPQDpgNSLNPVKTIGQQVEeiLRLHQS--LSAAERrQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQ 160
Cdd:COG3840 72 -------PVSMLFQE--NNLFPHLTVAQNIG--LGLRPGlkLTAEQR-AQVEQALERVGLAGLLDR---LPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET 240
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
250
....*....|....
gi 1031820327 241 IVQRPQHPYTRQLL 254
Cdd:COG3840 217 LLDGEPPPALAAYL 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-505 |
3.80e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAGHLSR---- 349
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPEDRRRigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 350 --EaqRQLRRKI----QFVYqnpFASldprqrlfaiieepLKNferLSAATRRQRVESVAARVALApELLSRTPRELSGG 423
Cdd:COG4152 77 peE--RGLYPKMkvgeQLVY---LAR--------------LKG---LSKAEAKRRADEWLERLGLG-DRANKKVEELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 424 QRQRVAIARALILEPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHDLATVRR 485
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDpvnvellkdvirelaakgTTV-------------------IFSSHQMELVEE 194
|
250 260
....*....|....*....|
gi 1031820327 486 IADSVTVLRAGQVVEHGDVN 505
Cdd:COG4152 195 LCDRIVIINKGRKVLSGSVD 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-232 |
4.08e-31 |
|
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: 119.07 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRsrgewrevVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDK 81
Cdd:cd03215 3 PVLEVRGLSVKGA--------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR----PPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRgvsISLVPQDPgnslnpvKTIGqqveeilrLHQSLSAAErrqqvlNLLAkvglshpeqrfdqyPHQLSGGMKQR 161
Cdd:cd03215 71 DAIRAG---IAYVPEDR-------KREG--------LVLDLSVAE------NIAL--------------SSLLSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-241 |
5.54e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 119.85 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03224 1 LEVENLNAGYGKS----QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL----PPRSGSIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlRGvsISLVPQdpGNSLNPVKTigqqVEEILRL----HQSLSAAERRQQVLNLLAKVglshpEQRFDQYPHQLSGGMK 159
Cdd:cd03224 73 AR-AG--IGYVPE--GRRIFPELT----VEENLLLgayaRRRAKRKARLERVYELFPRL-----KERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
..
gi 1031820327 240 TI 241
Cdd:cd03224 218 EL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-235 |
5.66e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.31 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKRLNRLRGVSISLVPQdpGN 100
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS----GDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 SLNPVKTIGQQVEEILrLHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEP 180
Cdd:PRK11629 97 HLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 181 TSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALaAERADRIMVFRQGEIQEQ 235
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL-AKRMSRQLEMRDGRLTAE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-245 |
6.42e-31 |
|
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: 123.29 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDwSDKRLNR---LRgvSISLVPQDPgnS 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLE----RPDSGRIRLGGEVLQD-SARGIFLpphRR--RIGYVFQEA--R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPVKTigqqVEEILRLHQSLSAAERRQ----QVLNLLakvGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIA 177
Cdd:COG4148 88 LFPHLS----VRGNLLYGRKRAPRAERRisfdEVVELL---GIGH---LLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 178 DEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-234 |
6.79e-31 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 120.62 E-value: 6.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRl 83
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGF----QNATSGEILVNGNEVTKPGPDR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlrgvsiSLVPQDpgNSLNPVKTIGQQVEEILRlHQSLSAAERRQQVLNLLAkvgLSHPEQRFDQYPHQLSGGMKQRVL 163
Cdd:NF040729 77 --------GFVFQN--YALFPWMTVKENIEYPMK-QQKMPKQEREKRLNELLE---MAQLTGKENLYPHQISGGMKQRTA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVF--RQGEIQE 234
Cdd:NF040729 143 VIRALACKPEVLLMDEPLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-255 |
9.23e-31 |
|
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: 126.03 E-value: 9.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRL 83
Cdd:COG4987 334 LELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP----QSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrgvsISLVPQDPgnslnPVktIGQQVEEILRLhqslsAAER--RQQVLNLLAKVGLSHpeqRFDQYPH--------- 152
Cdd:COG4987 408 RRR----IAVVPQRP-----HL--FDTTLRENLRL-----ARPDatDEELWAALERVGLGD---WLAALPDgldtwlgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 --QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDllDILRRESGTAVLFVTHDLAlAAERADRIMVFRQG 230
Cdd:COG4987 469 grRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA--DLLEALAGRTVLLITHRLA-GLERMDRILVLEDG 545
|
250 260
....*....|....*....|....*
gi 1031820327 231 EIQEQGATETIVQrpQHPYTRQLLH 255
Cdd:COG4987 546 RIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
267-520 |
1.23e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 267 ARHRPLATPAIRVEGISkrFSLGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARIL-----L--GFeRADaGQVTI 339
Cdd:COG1117 2 TAPASTLEPKIEVRNLN--VYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLipGA-RVE-GEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 340 DGIDAghLSREA-QRQLRRKIQFVYQ--NPFA-SldprqrlfaiIEE----PLKNFERLSAATRRQRVESVAARVALAPE 411
Cdd:COG1117 76 DGEDI--YDPDVdVVELRRRVGMVFQkpNPFPkS----------IYDnvayGLRLHGIKSKSELDEIVEESLRKAALWDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 412 L---LSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALD-----------------VTVqaqilallqqlqqqlgl 471
Cdd:COG1117 144 VkdrLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakieelilelkkdYTI----------------- 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1031820327 472 syLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELI 520
Cdd:COG1117 207 --VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
276-527 |
1.54e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.11 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS-REaqrq 354
Cdd:PRK10851 2 SIEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHaRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 lrRKIQFVYQNpfASLDPRQRLFAIIEEPLKNF---ERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIA 431
Cdd:PRK10851 74 --RKVGFVFQH--YALFRHMTVFDNIAFGLTVLprrERPNAAAIKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 432 RALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
250
....*....|....*.
gi 1031820327 512 QQAYTRELIAAIPQVS 527
Cdd:PRK10851 229 ATRFVLEFMGEVNRLQ 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
284-502 |
1.78e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.15 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 284 KRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReaqRQLRRKIQFVY 363
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP---KELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 364 QnpfasldprqrlfaiieeplknferlsaatrrqrvesVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVL 443
Cdd:cd03214 80 Q-------------------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 444 DEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
266-523 |
2.58e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.87 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 266 AARHRPLATPAIRVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG 345
Cdd:PRK11607 9 QAKTRKALTPLLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 346 HLSreaqrQLRRKIQFVYQNpfASLDPRQRLFAIIEEPLKNfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQR 425
Cdd:PRK11607 85 HVP-----PYQRPINMMFQS--YALFPHMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 426 QRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVN 505
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
250
....*....|....*...
gi 1031820327 506 RLFAAPQQAYTRELIAAI 523
Cdd:PRK11607 236 EIYEHPTTRYSAEFIGSV 253
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
278-497 |
2.63e-30 |
|
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: 115.80 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 278 RVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRR 357
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD---IAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 358 KIQFVYQnpfasldprqrlfaiieeplknferlsaatrrqrvesvaarvalapellsrtpreLSGGQRQRVAIARALILE 437
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 438 PAILVLDEATSALDVtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQ 497
Cdd:cd00267 99 PDLLLLDEPTSGLDP-ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
285-510 |
4.28e-30 |
|
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: 117.97 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 285 RFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqLRRKIQFVYQ 364
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 365 NpfasldprQRLF--AIIEeplkNFERLSAATRRQRVESvAARVALAPELLSRTPR-----------ELSGGQRQRVAIA 431
Cdd:cd03252 84 E--------NVLFnrSIRD----NIALADPGMSMERVIE-AAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 432 RALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:cd03252 151 RALIHNPRILIFDEATSALD--YESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
277-502 |
5.38e-30 |
|
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: 116.55 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreaqrqlr 356
Cdd:cd03268 1 LKTNDLTKTY--GKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 rkiqfvyqnpfaslDPRQRLFAIIEEP--------LKNFERLSAAT--RRQRVESVAARVALAPELLSRTpRELSGGQRQ 426
Cdd:cd03268 69 --------------EALRRIGALIEAPgfypnltaRENLRLLARLLgiRKKRIDEVLDVVGLKDSAKKKV-KGFSLGMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLD-PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
266-509 |
6.47e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 123.92 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 266 AARHRPLATPAIRVEGISK----RFSLGKQAlQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG 341
Cdd:PRK13657 318 DVRDPPGAIDLGRVKGAVEfddvSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 342 IDAGHLSREAqrqLRRKIQFVYQNPFasldprqrLFA-IIEEPLK-------NFERLSAATRRQRVESVAARVALAPELL 413
Cdd:PRK13657 397 TDIRTVTRAS---LRRNIAVVFQDAG--------LFNrSIEDNIRvgrpdatDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 414 SRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVL 493
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET--EAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVF 542
|
250
....*....|....*.
gi 1031820327 494 RAGQVVEHGDVNRLFA 509
Cdd:PRK13657 543 DNGRVVESGSFDELVA 558
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-246 |
9.55e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 9.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLA----DNARRDAGRIVLNGEVISDW 78
Cdd:PRK13640 5 IVEFKHVSFTYPDSK--KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpddnPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 79 SDKrlnrlrgvsISLVPQDPGNSLnpvktIGQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLShpeQRFDQYPHQLS 155
Cdd:PRK13640 83 REK---------VGIVFQNPDNQF-----VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGML---DYIDSEPANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQ 235
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQ 224
|
250
....*....|.
gi 1031820327 236 GATETIVQRPQ 246
Cdd:PRK13640 225 GSPVEIFSKVE 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
1.04e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIsDWSDKR 82
Cdd:PRK13639 1 ILETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL----KPTSGEVLIKGEPI-KYDKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDPGNSLnpvktIGQQVEEILR---LHQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMK 159
Cdd:PRK13639 73 LLEVRK-TVGIVFQNPDDQL-----FAPTVEEDVAfgpLNLGLSKEEVEKRVKEALKAVGMEGFENK---PPHHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
..
gi 1031820327 240 TI 241
Cdd:PRK13639 223 EV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-245 |
1.40e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLlaDNArrDAGRIVLNGEVISDWS- 79
Cdd:PRK09452 12 SPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ETP--DSGRIMLDGQDITHVPa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 DKRlnrlrgvSISLVPQDpgNSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMK 159
Cdd:PRK09452 84 ENR-------HVNTVFQS--YALFPHMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQL---EEFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
....*.
gi 1031820327 240 TIVQRP 245
Cdd:PRK09452 231 EIYEEP 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-254 |
1.60e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.99 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVIS------- 76
Cdd:PRK10619 6 LNVIDLHKRY---GE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL----EKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 77 --DWSDKRLNRLRGVSISLVPQDpgNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQrfDQYPHQL 154
Cdd:PRK10619 78 qlKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLALAAERADRIMVFRQGEIQE 234
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEE 232
|
250 260
....*....|....*....|
gi 1031820327 235 QGATETIVQRPQHPYTRQLL 254
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQFL 252
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-246 |
2.43e-29 |
|
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: 115.61 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrGEWReVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03219 1 LEVRGLTKRF---GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL----RPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlRGVS-----ISLVPqdpgnSLnpvkTI---------GQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHpeqRFDQ 149
Cdd:cd03219 73 AR-LGIGrtfqiPRLFP-----EL----TVlenvmvaaqARTGSGLLLARARREEREARERAEELLERVGLAD---LADR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 150 YPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQ 229
Cdd:cd03219 140 PAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQ 218
|
250
....*....|....*..
gi 1031820327 230 GEIQEQGATETIVQRPQ 246
Cdd:cd03219 219 GRVIAEGTPDEVRNNPR 235
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
276-511 |
3.13e-29 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 122.37 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqL 355
Cdd:TIGR03797 451 AIEVDRVT--FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA---V 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQNpfasldprQRLFaiieePLKNFERLSAATR--RQRVESVAARVALAPE----------LLSRTPRELSGG 423
Cdd:TIGR03797 526 RRQLGVVLQN--------GRLM-----SGSIFENIAGGAPltLDEAWEAARMAGLAEDirampmgmhtVISEGGGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 424 QRQRVAIARALILEPAILVLDEATSALDvtvqAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGD 503
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
....*...
gi 1031820327 504 VNRLFAAP 511
Cdd:TIGR03797 668 YDELMARE 675
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
295-502 |
4.24e-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: 114.17 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlsreaqRQLRRKIQFVYQnpFASLDprq 374
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQ--RRSID--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAI-IEE--------PLKNFERLSAAtRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:cd03235 81 RDFPIsVRDvvlmglygHKGLFRRLSKA-DKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 446 ATSALDVtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLrAGQVVEHG 502
Cdd:cd03235 159 PFAGVDP-KTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
274-498 |
5.54e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.13 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSlGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqr 353
Cdd:PRK09452 12 SPLVELRGISKSFD-GKEVI---SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 qlRRKIQFVYQNpFAsLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARA 433
Cdd:PRK09452 85 --NRHVNTVFQS-YA-LFPHMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 434 LILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-245 |
5.89e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKrlNRlrgvSISLVPQDpgNS 101
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL----EKPTEGQIFIDGEDVTHRSIQ--QR----DICMVFQS--YA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPT 181
Cdd:PRK11432 89 LFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 182 SALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
274-451 |
7.27e-29 |
|
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: 114.07 E-value: 7.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSL---GKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTID----GIDagh 346
Cdd:COG4778 2 TTLLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 347 LSREAQRQ---LRRK-IQFVYQnpFASLDPRQRLFAIIEEPLknFER-LSAATRRQRVESVAARVALAPELLSRTPRELS 421
Cdd:COG4778 79 LAQASPREilaLRRRtIGYVSQ--FLRVIPRVSALDVVAEPL--LERgVDREEARARARELLARLNLPERLWDLPPATFS 154
|
170 180 190
....*....|....*....|....*....|
gi 1031820327 422 GGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
296-509 |
8.67e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 8.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaGHLSREAQRQLRRKIQFVYQNPfasldPRQR 375
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIRHKIGMVFQNP-----DNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 376 LFAIIEEP----LKNfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:PRK13650 95 VGATVEDDvafgLEN-KGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 452 VTVQAQILALLQQLQQQLGLSYLFITHDLATVrRIADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-239 |
8.69e-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: 113.62 E-value: 8.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTaqaiIGLLADNARRDAGRIVLNG-EVISDWSDKRlnrlrgVSISLVPQDPg 99
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTT----IKMLTTLLKPTSGRATVAGhDVVREPREVR------RRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLShpEQRfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:cd03265 83 -SVDDELTGWENLYIHARL-YGVPGAERRERIDELLDFVGLL--EAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 180 PTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
258-515 |
1.04e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 119.87 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 258 QDAPLGLTAARHRPLATPAIRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQV 337
Cdd:COG4987 315 APPAVTEPAEPAPAPGGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 338 TIDGIDAGHLSREAqrqLRRKIQFVYQNPFasldprqrLFAI-IEEPLknfeRLSA--ATRRQrVESVAARVALAPeLLS 414
Cdd:COG4987 393 TLGGVDLRDLDEDD---LRRRIAVVPQRPH--------LFDTtLRENL----RLARpdATDEE-LWAALERVGLGD-WLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 415 RTP-----------RELSGGQRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATV 483
Cdd:COG4987 456 ALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLD--AATEQALLADLLEALAGRTVLLITHRLAGL 533
|
250 260 270
....*....|....*....|....*....|..
gi 1031820327 484 RRiADSVTVLRAGQVVEHGDVNRLFAAPQQAY 515
Cdd:COG4987 534 ER-MDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-267 |
1.10e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISD--- 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQE-KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE----AESGQIIIDGDLLTEenv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 78 WSDKRLnrlrgvsISLVPQDPGNSLnpvktIGQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQL 154
Cdd:PRK13650 77 WDIRHK-------IGMVFQNPDNQF-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQDFKER---EPARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAeRADRIMVFRQGEIQE 234
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVES 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1031820327 235 QGATETIVQRPQH--------PYTRQLLHDLQDAPLGLTAA 267
Cdd:PRK13650 221 TSTPRELFSRGNDllqlgldiPFTTSLVQSLRQNGYDLPEG 261
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-241 |
1.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 115.57 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLngeVISDWS-DKRLNRLRGVSISLVPQDP-G 99
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLP----DTGTIEW---IFKDEKnKKKTKEKEKVLEKLVIQKTrF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQV-----------------EEILRLHQSL--SAAERRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQ 160
Cdd:PRK13651 95 KKIKKIKEIRRRVgvvfqfaeyqlfeqtieKDIIFGPVSMgvSKEEAKKRAAKYIELVGL--DESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET 240
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
.
gi 1031820327 241 I 241
Cdd:PRK13651 252 I 252
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-249 |
1.72e-28 |
|
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: 115.67 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 39 VGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDwsdkRLNRLRGvsISLVPQDpgNSLNPVKTIGQQVEEILRL 118
Cdd:TIGR01187 2 LGPSGCGKTT----LLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRH--INMVFQS--YALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 119 hQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDI 198
Cdd:TIGR01187 70 -RKVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 199 LRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPY 249
Cdd:TIGR01187 146 IQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-241 |
1.93e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.08 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 11 ISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDwsdKRLNRLRGvS 90
Cdd:PRK13648 13 VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKS----GEIFYNNQAITD---DNFEKLRK-H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 91 ISLVPQDPGNslnpvktigQQVEEILRL-------HQSLSAAERRQQVLNLLAKVGLShpeQRFDQYPHQLSGGMKQRVL 163
Cdd:PRK13648 85 IGIVFQNPDN---------QFVGSIVKYdvafgleNHAVPYDEMHRRVSEALKQVDML---ERADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAErADRIMVFRQGEIQEQGATETI 241
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
277-502 |
2.30e-28 |
|
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: 112.29 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGsTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlsREAQRQLR 356
Cdd:cd03264 1 LQLENLTKRY--GKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfaSLDPRQRlfaiIEEPLKNFERL---SAATRRQRVESVAARVALAPELlSRTPRELSGGQRQRVAIARA 433
Cdd:cd03264 72 RRIGYLPQEF--GVYPNFT----VREFLDYIAWLkgiPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 434 LILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03264 145 LVGDPSILIVDEPTAGLD--PEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-236 |
2.32e-28 |
|
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: 111.93 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKrL 83
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSYQKNIEA-L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrGVSISlvpqDPGnsLNPVKTigqqVEEILRLHQSLsAAERRQQVLNLLAKVGLSH-PEQRFDQYphqlSGGMKQRV 162
Cdd:cd03268 72 RRI-GALIE----APG--FYPNLT----ARENLRLLARL-LGIRKKRIDEVLDVVGLKDsAKKKVKGF----SLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDvtvQKRILDLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLD---PDGIKELRELILslRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
278-499 |
2.54e-28 |
|
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: 111.97 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 278 RVEGISkrFSLGKQALqALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlsreAQRQLRR 357
Cdd:cd03226 1 RIENIS--FSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 358 KIQFVYQnpfaslDPRQRLF--AIIEEPLKNFERLSAatRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALI 435
Cdd:cd03226 72 SIGYVMQ------DVDYQLFtdSVREELLLGLKELDA--GNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 436 LEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYK-NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-246 |
2.81e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWS- 79
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGRIFLDGEDITHLPm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 DKRlnRLRGvsISLVPQDPgnS----LNpvktigqqVEE----ILRLHQsLSAAERRQQVLNLLAKVGLSHpeqRFDQYP 151
Cdd:COG1137 73 HKR--ARLG--IGYLPQEA--SifrkLT--------VEDnilaVLELRK-LSKKEREERLEELLEEFGITH---LRKSKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALD-VTV---QKRILDLldilrRESGTAVLFVTHD----LALaaerADR 223
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVadiQKIIRHL-----KERGIGVLITDHNvretLGI----CDR 205
|
250 260
....*....|....*....|...
gi 1031820327 224 IMVFRQGEIQEQGATETIVQRPQ 246
Cdd:COG1137 206 AYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-507 |
2.90e-28 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 112.08 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlSREAqRQLR 356
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREP-REVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfaSLDPRQRLFaiieEPLKNFERL---SAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARA 433
Cdd:cd03265 73 RRIGIVFQDL--SVDDELTGW----ENLYIHARLygvPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 434 LILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-236 |
3.90e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.64 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSRGEWRE--VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDwsDKRLN 84
Cdd:PRK13633 8 KNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE----GKVYVDGLDTSD--EENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 RLRGvSISLVPQDPGNSLnpVKTIgqqVEEILRL---HQSLSAAERRQQVLNLLAKVGLShpEQRfDQYPHQLSGGMKQR 161
Cdd:PRK13633 82 DIRN-KAGMVFQNPDNQI--VATI---VEEDVAFgpeNLGIPPEEIRERVDESLKKVGMY--EYR-RHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAErADRIMVFRQGEIQEQG 236
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
256-502 |
4.82e-28 |
|
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: 118.38 E-value: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 256 DLQDAPlgltAARHRPLATPAIRVEGISkrFSLGKQAlQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAG 335
Cdd:COG5265 341 EVADAP----DAPPLVVGGGEVRFENVS--FGYDPER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSG 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 336 QVTIDGIDAGHLSreaQRQLRRKIQFVYQNPFasldprqrLF-AIIEEplkN--FERLSAaTRRQRVEsvAARVALAPEL 412
Cdd:COG5265 414 RILIDGQDIRDVT---QASLRAAIGIVPQDTV--------LFnDTIAY---NiaYGRPDA-SEEEVEA--AARAAQIHDF 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 413 LSRTPR-----------ELSGGQRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLA 481
Cdd:COG5265 477 IESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALD--SRTERAIQAALREVARGRTTLVIAHRLS 554
|
250 260
....*....|....*....|.
gi 1031820327 482 TVRRiADSVTVLRAGQVVEHG 502
Cdd:COG5265 555 TIVD-ADEILVLEAGRIVERG 574
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-236 |
5.59e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.22 E-value: 5.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKrLNRLRGvSISLVPQDPGNSLNP 104
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS----GKIIIDGVDITDKKVK-LSDIRK-KVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 vKTIGQQVEEILRlHQSLSAAERRQQVLNLLAKVGLSHpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSAL 184
Cdd:PRK13637 99 -ETIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDY-EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 185 DVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-232 |
7.40e-28 |
|
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: 109.06 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISDWSDKRLNRLRgvsISLVpqdpgn 100
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK----PDSGEILVDGKEVSFASPRDARRAG---IAMV------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 slnpvktigqqveeilrlhqslsaaerrqqvlnllakvglshpeqrfdqypHQLSGGMKQRVLIAIAIALQPDLIIADEP 180
Cdd:cd03216 81 ---------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 181 TSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
293-511 |
7.54e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.29 E-value: 7.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 293 LQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPFasldp 372
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDHHYLHRQVALVGQEPV----- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 373 rqrLFAIIEEplknfERLSAATRRQRVESV--AARVALAPELLSRTPR-----------ELSGGQRQRVAIARALILEPA 439
Cdd:TIGR00958 566 ---LFSGSVR-----ENIAYGLTDTPDEEImaAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 440 ILVLDEATSALDVTVqaqiLALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:TIGR00958 638 VLILDEATSALDAEC----EQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
30-235 |
8.92e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.02 E-value: 8.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 30 IQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRLNRLRGVSISLVPQD----PgnSLNPV 105
Cdd:PRK10584 33 VKRGETIALIGESGSGKST----LLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSfmliP--TLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 106 KTIgqQVEEILRlhqSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALD 185
Cdd:PRK10584 107 ENV--ELPALLR---GESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1031820327 186 VTVQKRILDLLDILRRESGTAVLFVTHDLALAAeRADRIMVFRQGEIQEQ 235
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQLQEE 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-502 |
9.31e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.45 E-value: 9.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqrqlr 356
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFASLdPRQR-LF--AIIEEPLKNFERLSAATRRQ---RVESVAARVALAPELLSRTpRELSGGQRQRVAI 430
Cdd:cd03269 62 KPLDIAARNRIGYL-PEERgLYpkMKVIDQLVYLAQLKGLKKEEarrRIDEWLERLELSEYANKRV-EELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 431 ARALILEPAILVLDEATSALDVtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
285-502 |
9.37e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 110.76 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 285 RFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReaqRQLRRKIQFVYQ 364
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP---ADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 365 NP---FASLDPRQRLFAiieePLKNFERLSAATRRQRVESVAARVALAPEL-LSRTPRELSGGQRQRVAIARALILEPAI 440
Cdd:cd03245 86 DVtlfYGTLRDNITLGA----PLADDERILRAAELAGVTDFVNKHPNGLDLqIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 441 LVLDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLAtVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03245 162 LLLDEPTSAMDMN--SEERLKERLRQLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
282-511 |
1.02e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 282 ISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrqlRRKIQF 361
Cdd:PRK11432 12 ITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 362 VYQNpfASLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAIL 441
Cdd:PRK11432 83 VFQS--YALFPHMSLGENVGYGLK-MLGVPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 442 VLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
6-254 |
1.52e-27 |
|
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: 113.94 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 6 VEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadNARRDAGRIVLNGEVISDWSDKRLNr 85
Cdd:TIGR03258 8 IDHLRVAYGAN----TVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFV--KAAGLTGRIAIADRDLTHAPPHKRG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 86 lrgvsISLVPQDpgNSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIA 165
Cdd:TIGR03258 81 -----LALLFQN--YALFPHLKVEDNVAFGLRA-QKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 166 IAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRE-SGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQR 244
Cdd:TIGR03258 150 RAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDA 229
|
250
....*....|
gi 1031820327 245 PQHPYTRQLL 254
Cdd:TIGR03258 230 PADGFAAEFL 239
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
275-530 |
2.61e-27 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 112.59 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFE----RADAGQVTIDGIDAGHLS-R 349
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSpR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 350 EAQRQLRRKIQFVYQNPFASLDP-----RQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALA--PELLSRTPRELSG 422
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKdhKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260
....*....|....*....|....*...
gi 1031820327 503 DVNRLFAAPQQAYTRELIAAIPQVSSRL 530
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIPDFGSAM 269
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
275-452 |
2.70e-27 |
|
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: 109.11 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlsREAQRQ 354
Cdd:COG4133 1 MMLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVYQNP--FASLDPRqrlfaiieEPLKNFERLS-AATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIA 431
Cdd:COG4133 73 YRRRLAYLGHADglKPELTVR--------ENLRFWAALYgLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALA 143
|
170 180
....*....|....*....|.
gi 1031820327 432 RALILEPAILVLDEATSALDV 452
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDA 164
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
23-309 |
2.84e-27 |
|
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: 111.71 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNG-EVISDWSDKRLnrlrgvSISLVPQDPgnS 101
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL----RPTSGTARVAGyDVVREPRKVRR------SIGIVPQYA--S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPT 181
Cdd:TIGR01188 77 VDEDLTGRENLEMMGRL-YGLPKDEAEERAEELLELFELGEAA---DRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 182 SALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE---------TIVQRPQHPYTRQ 252
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEelkrrlgkdTLESRPRDIQSLK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 253 LLHDLQDAPLGLT----AARHRPLATPAIRVEGISKrfsLGKQALQALDSVSFEVRRGSTH 309
Cdd:TIGR01188 232 VEVSMLIAELGETglglLAVTVDSDRIKILVPDGDE---TVPEIVEAAIRNGIRIRSISTE 289
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-224 |
3.12e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.11 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDaGRIVLNGEvisdwsdkRL 83
Cdd:COG4136 2 LSLENLTITLGGR----PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAS-GEVLLNGR--------RL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRL----RGVSIslVPQDPgnSLNPVKTIGQQVeeILRLHQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMK 159
Cdd:COG4136 69 TALpaeqRRIGI--LFQDD--LLFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGLAG---FADRDPATLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLAlAAERADRI 224
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE-DAPAAGRV 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-246 |
4.04e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 109.30 E-value: 4.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSD 80
Cdd:COG0410 1 MPMLEVENLHAGY---GG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL----PPRSGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRlRGvsISLVPQD----PGNSlnpvktigqqVEEILRL-----HQSLSAAERRQQVLNL---LAkvglshpeQRFD 148
Cdd:COG0410 73 HRIAR-LG--IGYVPEGrrifPSLT----------VEENLLLgayarRDRAEVRADLERVYELfprLK--------ERRR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 149 QYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFR 228
Cdd:COG0410 132 QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLE 210
|
250
....*....|....*...
gi 1031820327 229 QGEIQEQGATETIVQRPQ 246
Cdd:COG0410 211 RGRIVLEGTAAELLADPE 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-249 |
4.77e-27 |
|
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: 112.13 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 26 ISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDPgnSLNPV 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT----RPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEA--RLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 106 KTIGQQVEEILRLHQSLSAAERRQQVLNLLakvGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALD 185
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 186 VTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPY 249
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-260 |
5.59e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.21 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLaDNArrDAGRIVLNGEVISDWSDKRL 83
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL-DKP--TSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSISLVPQDpgNSLNPVKTIGQQVEeILRLHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVL 163
Cdd:PRK10535 81 AQLRREHFGFIFQR--YHLLSHLTAAQNVE-VPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAErADRIMVFRQGEI--------QEQ 235
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqeKVN 232
|
250 260
....*....|....*....|....*
gi 1031820327 236 GATETIVQRPQHPYTRQLLHDLQDA 260
Cdd:PRK10535 233 VAGGTEPVVNTASGWRQFVSGFREA 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-258 |
6.95e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVvHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKR 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFE----GKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRlrgvSISLVPQDPGNSLnpvktIGQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMK 159
Cdd:PRK13642 79 LRR----KIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAErADRIMVFRQGEIQEQGATE 239
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
250 260
....*....|....*....|....*..
gi 1031820327 240 TIVQRPQH--------PYTRQLLHDLQ 258
Cdd:PRK13642 226 ELFATSEDmveigldvPFSSNLMKDLR 252
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
282-511 |
8.02e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 111.36 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 282 ISKRFSlGKQALQALDsVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghLSREAQRQL---RRK 358
Cdd:TIGR02142 1 LSARFS-KRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL--FDSRKGIFLppeKRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 359 IQFVYQNpfASLDPRqrlFAIIEEPLKNFERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEP 438
Cdd:TIGR02142 77 IGYVFQE--ARLFPH---LSVRGNLRYGMKRARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 439 AILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-236 |
1.38e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.72 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLAdnarR----DAGRIVLNGEVISDWS 79
Cdd:COG1132 340 IEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKST----LVNLLL----RfydpTSGRILIDGVDIRDLT 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 dkrLNRLRGvSISLVPQDP----GnslnpvkTIG------------QQVEEILRLhqsLSAAERrqqVLNLlakvglshp 143
Cdd:COG1132 409 ---LESLRR-QIGVVPQDTflfsG-------TIRenirygrpdatdEEVEEAAKA---AQAHEF---IEAL--------- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 144 EQRFDQY----PHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLAlAAE 219
Cdd:COG1132 463 PDGYDTVvgerGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIR 539
|
250
....*....|....*..
gi 1031820327 220 RADRIMVFRQGEIQEQG 236
Cdd:COG1132 540 NADRILVLDDGRIVEQG 556
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-251 |
1.41e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGevisdwsdkrlnrlrgVSISLVP--QDPG 99
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGFEQPTAGQIMLDG----------------VDLSHVPpyQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 N------SLNPVKTIGQQVEEILRlHQSLSAAERRQQVLNLLakvGLSHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPD 173
Cdd:PRK11607 94 NmmfqsyALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEML---GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 174 LIIADEPTSALDVTVQKRI-LDLLDILRRESGTAVLfVTHDLALAAERADRIMVFRQGEIQEQGATETIVqrpQHPYTR 251
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVM-VTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-246 |
1.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIS-DWSDKRLNRLRGvSISLVPQDP 98
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL----QPTSGTVTIGERVITaGKKNKKLKPLRK-KVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 GNSLnpvktigqqVEE-ILR------LHQSLSAAERRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRVLIAIAIALQ 171
Cdd:PRK13634 95 EHQL---------FEEtVEKdicfgpMNFGVSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 172 PDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQ 246
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-247 |
1.64e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 107.55 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRLnrlrgvsisLVPQDpgNSLNP 104
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGL----AQPTSGGVILEGKQITEPGPDRM---------VVFQN--YSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQQVE-EILRLHQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSA 183
Cdd:TIGR01184 68 WLTVRENIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 184 LDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI-VQRPQH 247
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
276-512 |
1.66e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.15 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSLGKQ-ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAgHLSREAQ 352
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITP-ETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQNPFASLDPRQRLFAIIEEPlKNFERLSAATRRQRVESVAaRVALAPELLSRTPRELSGGQRQRVAIAR 432
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQLFENTVLKDVEFGP-KNFGFSEDEAKEKALKWLK-KVGLSEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLD-PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-254 |
2.33e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.89 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLADNARrdaGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDpgNSL 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLIEPTR---GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTS 182
Cdd:PRK10070 118 MPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 183 ALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQLL 254
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
300-503 |
2.61e-26 |
|
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: 106.48 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 300 SFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreaqrQLRRKIQFVYQ--NPFASLDPRQRLF 377
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQenNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 378 AIIEEPLKnferlSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQ 457
Cdd:TIGR01277 93 LGLHPGLK-----LNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1031820327 458 ILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGD 503
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
294-498 |
3.26e-26 |
|
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: 106.79 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaGHLSREAQRQLRRKIQFVYQNPfasldpr 373
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYEHKYLHSKVSLVGQEP------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 qRLFA-IIEE------PLKNFERLSAATRRQRVESVAARVALAP-ELLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:cd03248 98 -VLFArSLQDniayglQSCSFECVKEAAQKAHAHSFISELASGYdTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 446 ATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQV 498
Cdd:cd03248 177 ATSALD--AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
295-512 |
3.35e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.18 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTI--DGIDAGhlSREAQ-RQLRRKIQFVYQnpFasld 371
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgeRVITAG--KKNKKlKPLRKKVGIVFQ--F---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 PRQRLFaiiEEPL--------KNFErLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVL 443
Cdd:PRK13634 94 PEHQLF---EETVekdicfgpMNFG-VSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 444 DEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-236 |
3.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIsDWSDK 81
Cdd:PRK13636 4 YILKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGKPI-DYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGvSISLVPQDPGNSLNPVkTIGQQVEeILRLHQSLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQR 161
Cdd:PRK13636 76 GLMKLRE-SVGMVFQDPDNQLFSA-SVYQDVS-FGAVNLKLPEDEVRKRVDNALKRTGIEHLK---DKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-498 |
3.71e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 111.68 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISDWSDKRLNRLrgvSISLVPQDPgn 100
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP----PDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 SLNPVKTIGQQVeeILRLHQSLSAAERRQQvlnLLAKVGLShpeqrFDqyPHQLSGGM----KQRVLIAIAIALQPDLII 176
Cdd:PRK15439 96 LLFPNLSVKENI--LFGLPKRQASMQKMKQ---LLAALGCQ-----LD--LDSSAGSLevadRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATET-----IVQRPQHPYTR 251
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADlstddIIQAITPAARE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 252 QLLHDLQDAPLGLTAARHR-PLATPAIRVEGISKrfslgkqalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFE 330
Cdd:PRK15439 243 KSLSASQKLWLELPGNRRQqAAGAPVLTVEDLTG---------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 331 RADAGQVTIDGIDAGHLSrEAQRqLRRKIQFVYQNpfasldpRQRLFAIIEEPLK------NFERLSAATRRQRVESVAA 404
Cdd:PRK15439 314 PARGGRIMLNGKEINALS-TAQR-LARGLVYLPED-------RQSSGLYLDAPLAwnvcalTHNRRGFWIKPARENAVLE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 405 RV--ALAPEL--LSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDL 480
Cdd:PRK15439 385 RYrrALNIKFnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS-ARNDIYQLIRSIAAQNVAVLFISSDL 463
|
490
....*....|....*...
gi 1031820327 481 ATVRRIADSVTVLRAGQV 498
Cdd:PRK15439 464 EEIEQMADRVLVMHQGEI 481
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
274-501 |
6.41e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.05 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQR 353
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 QLR-RKIQFVYQnpFASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAArVALAPELLSRtPRELSGGQRQRVAIAR 432
Cdd:PRK11629 83 ELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAA-VGLEHRANHR-PSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 433 ALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTvLRAGQVVEH 501
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-236 |
7.19e-26 |
|
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: 105.35 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGeMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKrl 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP----SSGTIRIDGQDVLKQPQK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrLRGVsISLVPQDPGnsLNPVKTIGQQVEEILRLHqSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVL 163
Cdd:cd03264 70 --LRRR-IGYLPQEFG--VYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNL---GDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrrESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
262-514 |
8.10e-26 |
|
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: 111.38 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 262 LGLTAARHRPLATPA----IRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQV 337
Cdd:COG4618 312 LAAVPAEPERMPLPRpkgrLSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 338 TIDGIDAGHLSREaqrQLRRKIQFVYQNPfasldprqRLFAI-IEEplkNFERLSAATRRQRVEsvAARVALAPELLSRT 416
Cdd:COG4618 390 RLDGADLSQWDRE---ELGRHIGYLPQDV--------ELFDGtIAE---NIARFGDADPEKVVA--AAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 417 P-----------RELSGGQRQRVAIARALILEPAILVLDEATSALD------------------VTVqaqilallqqlqq 467
Cdd:COG4618 454 PdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalaaairalkargATV------------- 520
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1031820327 468 qlglsyLFITHDLATVrRIADSVTVLRAGQVVEHG---DVNRLFAAPQQA 514
Cdd:COG4618 521 ------VVITHRPSLL-AAVDKLLVLRDGRVQAFGprdEVLARLARPAAA 563
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
277-498 |
1.07e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 103.45 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLR 356
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD---ISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPfasldprqrlfaiieeplknferlsaatrrqrvesvaarvalapELLSRTPRE--LSGGQRQRVAIARAL 434
Cdd:cd03246 76 DHVGYLPQDD--------------------------------------------ELFSGSIAEniLSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 435 ILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQV 498
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVE-GERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
295-509 |
1.29e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNpfasldprQ 374
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQVALVSQN--------V 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFaiiEEPLKN---FERLSAATRRQRVEsvAARVALAPELLSRTPR-----------ELSGGQRQRVAIARALILEPAI 440
Cdd:PRK11176 427 HLF---NDTIANniaYARTEQYSREQIEE--AARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 441 LVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:PRK11176 502 LILDEATSALD--TESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-245 |
1.30e-25 |
|
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: 104.93 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDITKLPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrgvSISLVPQDPgnSLNPVKTIGQQVEEILRLHQsLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVL 163
Cdd:cd03218 73 ARL---GIGYLPQEA--SIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLR---KSKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
..
gi 1031820327 244 RP 245
Cdd:cd03218 223 NE 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
277-528 |
1.84e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.29 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQ-ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHlSREAQRQL 355
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQNPFASLDpRQRLFAIIEEPLKNFErLSAATRRQRVESVAARVALAPE-LLSRTPRELSGGQRQRVAIARAL 434
Cdd:PRK13637 82 RKKVGLVFQYPEYQLF-EETIEKDIAFGPINLG-LSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 435 ILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFaapQQA 514
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF---KEV 236
|
250
....*....|....*
gi 1031820327 515 YTRELIA-AIPQVSS 528
Cdd:PRK13637 237 ETLESIGlAVPQVTY 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
272-504 |
1.88e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.87 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 272 LATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREA 351
Cdd:PRK09700 1 MATPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQLrrKIQFVYQ------------NPFASLDPRQRLFAIieePLKNFERLsaatrRQRVESVAARVALAPELLSRTPrE 419
Cdd:PRK09700 77 AAQL--GIGIIYQelsvideltvleNLYIGRHLTKKVCGV---NIIDWREM-----RVRAAMMLLRVGLKVDLDEKVA-N 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 420 LSGGQRQRVAIARALILEPAILVLDEATSALdVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
....*
gi 1031820327 500 EHGDV 504
Cdd:PRK09700 225 CSGMV 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-284 |
1.99e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVI-SDWSDKRLNRLRGvSISLVPQDPGNSLN 103
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHItPETGNKNLKKLRK-KVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 104 PvKTIGQQVEeILRLHQSLSAAERRQQVLNLLAKVGLShpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSA 183
Cdd:PRK13641 100 E-NTVLKDVE-FGPKNFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 184 LDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQ--------HPYTRQLLH 255
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSRFAS 254
|
250 260
....*....|....*....|....*....
gi 1031820327 256 DLQDAPLGLtaaRHRPLATPAIrVEGISK 284
Cdd:PRK13641 255 KLEKGGFKF---SEMPLTIDEL-VDGIKN 279
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-232 |
2.01e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRisyrsrgeWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIsdwsdk 81
Cdd:COG1129 255 VVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD----PADSGEIRLDGKPV------ 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 rlnRLRGVS------ISLVPQD-PGNSLNPVKTIGQ-----QVEEILRLHQsLSAAERRQQVLNLLAKVGL--SHPEQRF 147
Cdd:COG1129 317 ---RIRSPRdairagIAYVPEDrKGEGLVLDLSIREnitlaSLDRLSRGGL-LDRRRERALAEEYIKRLRIktPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 148 DQyphqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVF 227
Cdd:COG1129 393 GN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVM 467
|
....*
gi 1031820327 228 RQGEI 232
Cdd:COG1129 468 REGRI 472
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
280-523 |
2.65e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.81 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 280 EGISKRFSLGKQALQ-ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRRK 358
Cdd:PRK10070 27 QGLSKEQILEKTGLSlGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 359 -IQFVYQNpFAsLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILE 437
Cdd:PRK10070 107 kIAMVFQS-FA-LMPHMTVLDNTAFGME-LAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 438 PAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTR 517
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
....*.
gi 1031820327 518 ELIAAI 523
Cdd:PRK10070 263 TFFRGV 268
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
294-526 |
2.70e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ-RQLRRKIQFVYQNPFASL-- 370
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKRIGMVFQFPESQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 371 DPRQRlfAIIEEPlKNFeRLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:PRK13646 101 DTVER--EIIFGP-KNF-KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 451 DVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAapQQAYTRELIAAIPQV 526
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADWHIGLPEI 250
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
300-507 |
3.99e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.89 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 300 SFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSrEAQRQLrrKIQFVYQNPFASLDPRQRLFAI 379
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-PSRRPV--SMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 380 IEEPLKnferLSAATRRQrVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQIL 459
Cdd:PRK10771 96 LNPGLK----LNAAQREK-LHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1031820327 460 ALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
296-512 |
4.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaGHLSREAQRQLRRKIQFVYQNPfasldPRQR 375
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRKIGMVFQNP-----DNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 376 LFAIIEEPLKnFERLSAATRRQRVESVAARVALAPELL---SRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK13642 95 VGATVEDDVA-FGMENQGIPREEMIKRVDEALLAVNMLdfkTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 453 TVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
4.47e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSD 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGvsisLVPQDPGNSL-NPvkTIGQQVEeILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMK 159
Cdd:PRK13652 74 REVRKFVG----LVFQNPDDQIfSP--TVEQDIA-FGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
....*.
gi 1031820327 240 TIVQRP 245
Cdd:PRK13652 224 EIFLQP 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
295-512 |
4.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGF---ERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPfasld 371
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGIT---LTAKTVWDIREKVGIVFQNP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 PRQRLFAIIEEPLKnFERLSAATRRQR----VESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:PRK13640 94 DNQFVGATVGDDVA-FGLENRAVPRPEmikiVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 448 SALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVrRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-232 |
4.57e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISyRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDK 81
Cdd:COG3845 256 VVLEVENLSVR-DDRG--VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLR----PPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRgvsISLVPQDP-GNSLNPVKTIGQQVeeILRLHQS--------LSAAERRQQVLNLLAK--VGLSHPEQRFDQy 150
Cdd:COG3845 329 ERRRLG---VAYIPEDRlGRGLVPDMSVAENL--ILGRYRRppfsrggfLDRKAIRAFAEELIEEfdVRTPGPDTPARS- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 151 phqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDV----TVQKRILDLldilrRESGTAVLFVTHDL----ALaaerAD 222
Cdd:COG3845 403 ---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLEL-----RDAGAAVLLISEDLdeilAL----SD 470
|
250
....*....|
gi 1031820327 223 RIMVFRQGEI 232
Cdd:COG3845 471 RIAVMYEGRI 480
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-246 |
4.58e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 104.04 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIvlngevisdwsd 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAP----DEGVI------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRgvsISLVPQdpgnSLNPVKTIGQQVEEILRLHQSLsaaeRRQQVLNLLAKVGLSHpeqrFDQYPHQ-LSGGMK 159
Cdd:PRK09544 62 KRNGKLR---IGYVPQ----KLYLDTTLPLTVNRFLRLRPGT----KKEDILPALKRVQAGH----LIDAPMQkLSGGET 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQgEIQEQGATE 239
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPE 205
|
....*..
gi 1031820327 240 TIVQRPQ 246
Cdd:PRK09544 206 VVSLHPE 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-232 |
5.64e-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: 101.52 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDlrISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdAGRIVLNGEVISDWSDKRL 83
Cdd:cd03246 1 LEVEN--VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT----SGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlrGVSISLVPQD----PGnslnpvkTIGQQVeeilrlhqslsaaerrqqvlnllakvglshpeqrfdqyphqLSGGMK 159
Cdd:cd03246 75 ----GDHVGYLPQDdelfSG-------SIAENI-----------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLALAAeRADRIMVFRQGEI 232
Cdd:cd03246 103 QRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIV-IAHRPETLA-SADRILVLEDGRV 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-510 |
5.95e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 5.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreAQRQ 354
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LrrkiqfVYQNpfASLDPRQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARAL 434
Cdd:COG4525 80 V------VFQK--DALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 435 ILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL--RAGQVVE--HGDVNRLFAA 510
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVErlELDFSRRFLA 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-244 |
5.98e-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: 103.46 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSdkrLNRL 86
Cdd:cd03253 4 ENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLFRFYDVSSGSILIDGQDIREVT---LDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 RGvSISLVPQDPgnslnpV---KTIGQQVEeilrlHQSLSAAErrQQVLNLlAKVGLSHPE-QRF-DQYPHQ-------L 154
Cdd:cd03253 74 RR-AIGVVPQDT------VlfnDTIGYNIR-----YGRPDATD--EEVIEA-AKAAQIHDKiMRFpDGYDTIvgerglkL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALAAErADRIMVFRQGEIQE 234
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
250
....*....|
gi 1031820327 235 QGATETIVQR 244
Cdd:cd03253 216 RGTHEELLAK 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-236 |
6.40e-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: 103.39 E-value: 6.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIiglladnaRR----DAGRIVLNGEVISDWSdkr 82
Cdd:cd03249 4 KNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--------ERfydpTSGEILLDGVDIRDLN--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDPGNSLNPVKtigqqvEEILrlhqsLSAAERRQQVLNLLAKVGLSH------PEQrFD----QYPH 152
Cdd:cd03249 72 LRWLRS-QIGLVSQEPVLFDGTIA------ENIR-----YGKPDATDEEVEEAAKKANIHdfimslPDG-YDtlvgERGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLAlAAERADRIMVFRQGEI 232
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
....
gi 1031820327 233 QEQG 236
Cdd:cd03249 216 VEQG 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-243 |
6.42e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 103.38 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 26 ISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrdAGRIVLNGEVISDWSDKRLNRLRGVsisLVPQDPGNSLNPV 105
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-----QGEILLNGRPLSDWSAAELARHRAY---LSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 106 KtigqqveEILRLHQ--SLSAAERRQQVLNLLAKVGLShpeqrfDQYP---HQLSGGMKQRVLIAiAIALQ------PD- 173
Cdd:COG4138 87 F-------QYLALHQpaGASSEAVEQLLAQLAEALGLE------DKLSrplTQLSGGEWQRVRLA-AVLLQvwptinPEg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 174 -LIIADEPTSALDVTvQKRILDLLdiLRR--ESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:COG4138 153 qLLLLDEPMNSLDVA-QQAALDRL--LRElcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-273 |
6.61e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 103.62 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 5 SVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLN 84
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLL----PPDSGEVLVDGLDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 85 RlrgvSISLVPQDpgNSLNPVKTigqqVEEILRL-----HQSLSAAERRQQVLNLLAKVGLSHPEQRF-DQyphqLSGGM 158
Cdd:COG4604 75 K----RLAILRQE--NHINSRLT----VRELVAFgrfpySKGRLTAEDREIIDEAIAYLDLEDLADRYlDE----LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 159 KQRVLIAIAIALQPDLIIADEPTSALDVtvqKRILDLLDILRR---ESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDM---KHSVQMMKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1031820327 236 GATETIVqrpqhpyTRQLLHDLQDAPLGLTAARHRPLA 273
Cdd:COG4604 218 GTPEEII-------TPEVLSDIYDTDIEVEEIDGKRIC 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
277-515 |
8.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.91 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQaldSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReaQRQLR 356
Cdd:PRK13644 2 IRLENVSYSYPDGTPALE---NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFASLDPRQrlfaiIEEPL----KNFeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIAR 432
Cdd:PRK13644 77 KLVGIVFQNPETQFVGRT-----VEEDLafgpENL-CLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVrRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
...
gi 1031820327 513 QAY 515
Cdd:PRK13644 228 LQT 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-265 |
1.01e-24 |
|
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: 102.86 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLL-ADNARRDAGRIVLNGEVISDWS 79
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKST----LLSLItGDLPPTYGNDVRLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 dkrLNRLRGvSISLVPQDPGNSLNPvktiGQQVEEI--------LRLHQSLSAAERrQQVLNLLAKVGLSHpeqRFDQYP 151
Cdd:COG1119 73 ---VWELRK-RIGLVSPALQLRFPR----DETVLDVvlsgffdsIGLYREPTDEQR-ERARELLELLGLAH---LADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
250 260 270
....*....|....*....|....*....|....
gi 1031820327 232 IQEQGATETIVqrpqhpyTRQLLHDLQDAPLGLT 265
Cdd:COG1119 221 VVAAGPKEEVL-------TSENLSEAFGLPVEVE 247
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-452 |
1.23e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 107.01 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISdWSDKRLNRLRGVSI-----SLVPQdpg 99
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIY----TRDAGSILYLGKEVT-FNGPKSSQEAGIGIihqelNLIPQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nslnpvKTIGQQV---EEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQRVLIAIAIALQPDLII 176
Cdd:PRK10762 94 ------LTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKL---VGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRrESGTAVLFVTHDLALAAERADRIMVFRQG---------EIQEQGATETIVQR--- 244
Cdd:PRK10762 165 MDEPTDALTDTETESLFRVIRELK-SQGRGIVYISHRLKEIFEICDDVTVFRDGqfiaerevaDLTEDSLIEMMVGRkle 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 245 PQHPYTrqllhdlqDAPLGLTAARHRPLATPAIrvegiskrfslgkqalqalDSVSFEVRRGSTHALVGESGSGKTTLAR 324
Cdd:PRK10762 244 DQYPRL--------DKAPGEVRLKVDNLSGPGV-------------------NDVSFTLRKGEILGVSGLMGAGRTELMK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 325 ILLGFERADAGQVTIDGIDAghLSREAQRQLRRKIQFVyqnpfaSLDpRQR----LFAIIEE-----PLKNFERLSAATR 395
Cdd:PRK10762 297 VLYGALPRTSGYVTLDGHEV--VTRSPQDGLANGIVYI------SED-RKRdglvLGMSVKEnmsltALRYFSRAGGSLK 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 396 RQRvESVAarVALAPELLS-RTP------RELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK10762 368 HAD-EQQA--VSDFIRLFNiKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-243 |
1.42e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.78 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYrsrGEWReVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDK 81
Cdd:PRK11231 1 MTLRTENLTVGY---GTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS----GTVFLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRlrgvSISLVPQDPgnsLNPVktiGQQVEEILRLHQS--LS-----AAERRQQVLNLLAKVGLSH-PEQRFDQyphq 153
Cdd:PRK11231 73 QLAR----RLALLPQHH---LTPE---GITVRELVAYGRSpwLSlwgrlSAEDNARVNQAMEQTRINHlADRRLTD---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 154 LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQ 233
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
250
....*....|
gi 1031820327 234 EQGATETIVQ 243
Cdd:PRK11231 218 AQGTPEEVMT 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-214 |
1.96e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRlnrlrGVsislVPQDPG 99
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV----VFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nsLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:PRK11248 81 --LLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRY---IWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1031820327 180 PTSALDVTVQKRILDLLDILRRESGTAVLFVTHDL 214
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
292-507 |
2.27e-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: 101.36 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 292 ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreAQRQLRRKIQFVYQNpfasld 371
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP--PHERARAGIGYVPEG------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 prQRLFA--IIEEPLK-NFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATS 448
Cdd:cd03224 84 --RRIFPelTVEENLLlGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 449 AL------------------DVTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:cd03224 162 GLapkiveeifeairelrdeGVTI-------------------LLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
259-521 |
2.41e-24 |
|
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: 107.34 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 259 DAPLGLTAARHRPLaTPAIRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVT 338
Cdd:TIGR03796 461 PEGSAATSEPPRRL-SGYVELRNITFGYSPLEPPL--IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEIL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 339 IDGIDAGHLSREAqrqLRRKIQFVYQNPFasldprqrLFA-IIEEPLK------NFERLSAATRRQRV-ESVAARVALAP 410
Cdd:TIGR03796 538 FDGIPREEIPREV---LANSVAMVDQDIF--------LFEgTVRDNLTlwdptiPDADLVRACKDAAIhDVITSRPGGYD 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 411 ELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVqaqiLALLQQLQQQLGLSYLFITHDLATVRRiADSV 490
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPET----EKIIDDNLRRRGCTCIIVAHRLSTIRD-CDEI 681
|
250 260 270
....*....|....*....|....*....|.
gi 1031820327 491 TVLRAGQVVEHGDVNRLFAAPqQAYTReLIA 521
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVG-GAYAR-LIR 710
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-243 |
2.86e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.17 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLriSYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDK 81
Cdd:PRK10575 10 TTFALRNV--SFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKST----LLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGVSISLVPQDPGNSLNPVKTIGQqveeiLRLHQSLS--AAERRQQVLNLLAKVGLSHPEQRFDQyphQLSGGMK 159
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGMTVRELVAIGR-----YPWHGALGrfGAADREKVEEAISLVGLKPLAHRLVD---SLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
....
gi 1031820327 240 TIVQ 243
Cdd:PRK10575 234 ELMR 237
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-259 |
3.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTaqaiigLLADNARRDA--GRIVLNGEVISDWSD 80
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTL------LLHLNGIYLPqrGRVKVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGvsisLVPQDPGNSLnpvktIGQQVEEILR---LHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGG 157
Cdd:PRK13647 75 KWVRSKVG----LVFQDPDDQV-----FSSTVWDDVAfgpVNMGLDKDEVERRVEEALKAVRM---WDFRDKPPYHLSYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 158 MKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
250 260
....*....|....*....|....*....
gi 1031820327 238 TETIVQRP-------QHPYTRQLLHDLQD 259
Cdd:PRK13647 222 KSLLTDEDiveqaglRLPLVAQIFEDLPE 250
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
295-451 |
3.36e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 100.56 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNpfASLDPRQ 374
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAIIEEPLknfeRLSAATRR---QRVESVAARVALAPEllSRT-PRELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:cd03292 94 NVYENVAFAL----EVTGVPPReirKRVPAALELVGLSHK--HRAlPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
.
gi 1031820327 451 D 451
Cdd:cd03292 168 D 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
277-499 |
4.04e-24 |
|
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: 100.66 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQAlqALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghlsREAQRQLR 356
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNP--FASLDPRQ--RLFAIieepLKNferLSAATRRQRVESVAARVALAPELLSRTpRELSGGQRQRVAIAR 432
Cdd:cd03263 75 QSLGYCPQFDalFDELTVREhlRFYAR----LKG---LPKSEIKEEVELLLRVLGLTDKANKRA-RTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 433 ALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLD--PASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-244 |
4.96e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.86 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRS---------------RGEWREV--VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDA 65
Cdd:COG4586 1 IIEVENLSKTYRVyekepglkgalkglfRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGIL----VPTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 66 GRIVLNGEVIsdWSDKRLNRLRgvsISLVpqdpgnslnpvktIGQ--Q------VEEILRLHQ---SLSAAERRQQvLNL 134
Cdd:COG4586 77 GEVRVLGYVP--FKRRKEFARR---IGVV-------------FGQrsQlwwdlpAIDSFRLLKaiyRIPDAEYKKR-LDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 135 LAKV-GLSHpeqrFDQYP-HQLSGGmkQRVLIAIAIAL--QPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFV 210
Cdd:COG4586 138 LVELlDLGE----LLDTPvRQLSLG--QRMRCELAAALlhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLT 211
|
250 260 270
....*....|....*....|....*....|....
gi 1031820327 211 THDLALAAERADRIMVFRQGEIQEQGATETIVQR 244
Cdd:COG4586 212 SHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-245 |
5.07e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSdkRLNRLRGVsISLVPQDPGNSLnp 104
Cdd:PRK13644 20 NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGIDTGDFS--KLQGIRKL-VGIVFQNPETQF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 vktIGQQVEEILRL---HQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLIIADEPT 181
Cdd:PRK13644 91 ---VGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 182 SALDVTVQKRILDLLDILRREsGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-236 |
6.84e-24 |
|
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: 100.48 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 6 VEDLRISYRS---------------RGEWREV--VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRI 68
Cdd:cd03267 3 VSNLSKSYRVyskepgligslkslfKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL----QPTSGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 69 VLNGEVISDWSDKRLNRlrgvsISLVpqdpgnslnpvktIGQQ--------VEEILRLHQS---LSAAERRQQVLNLLAK 137
Cdd:cd03267 79 RVAGLVPWKRRKKFLRR-----IGVV-------------FGQKtqlwwdlpVIDSFYLLAAiydLPPARFKKRLDELSEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 138 VGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALA 217
Cdd:cd03267 141 LDL---EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDI 217
|
250
....*....|....*....
gi 1031820327 218 AERADRIMVFRQGEIQEQG 236
Cdd:cd03267 218 EALARRVLVIDKGRLLYDG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-257 |
7.38e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwrEVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRL 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvSISLVPQDpgnslnpVKTIGQQVEEILRLHQSLSAAERRQQVLNllaKVGLSH---PEQRFDQY----PHQLSG 156
Cdd:PRK11160 413 RQ----AISVVSQR-------VHLFSATLRDNLLLAAPNASDEALIEVLQ---QVGLEKlleDDKGLNAWlgegGRQLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 157 GMKQRvlIAIAIALQPD--LIIADEPTSALDVTVQKRILDLLdiLRRESGTAVLFVTHDLaLAAERADRIMVFRQGEIQE 234
Cdd:PRK11160 479 GEQRR--LGIARALLHDapLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRL-TGLEQFDRICVMDNGQIIE 553
|
250 260
....*....|....*....|...
gi 1031820327 235 QGATETIVQrpQHPYTRQLLHDL 257
Cdd:PRK11160 554 QGTHQELLA--QQGRYYQLKQRL 574
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
277-520 |
7.48e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.17 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHlSREAQRQLR 356
Cdd:PRK09493 2 IEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQ--NPFASLDPrqrLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARAL 434
Cdd:PRK09493 77 QEAGMVFQqfYLFPHLTA---LENVMFGPLR-VRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 435 ILEPAILVLDEATSALD-------VTVqaqilallQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDpelrhevLKV--------MQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
250
....*....|...
gi 1031820327 508 FAAPQQAYTRELI 520
Cdd:PRK09493 224 IKNPPSQRLQEFL 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-244 |
1.14e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MT-VLSVEDLRISYR------------------SRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadna 61
Cdd:COG1134 1 MSsMIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 62 RRDAGRIVLNGEVISdwsdkrlnrlrgvsislvPQDPGNSLNPvktigqqveeilrlhqSLSAAE-----------RRQQ 130
Cdd:COG1134 77 EPTSGRVEVNGRVSA------------------LLELGAGFHP----------------ELTGREniylngrllglSRKE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 131 VLNLLAKV----GLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRrESGTA 206
Cdd:COG1134 123 IDEKFDEIvefaEL---GDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRT 198
|
250 260 270
....*....|....*....|....*....|....*...
gi 1031820327 207 VLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQR 244
Cdd:COG1134 199 VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-255 |
1.30e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 105.21 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:TIGR01193 474 IVINDVSYSY---GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF----QARSGEILLNGFSLKDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvSISLVPQDP----GNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDqyphqLSGGMK 159
Cdd:TIGR01193 547 RQ----FINYLPQEPyifsGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS-----ISGGQK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESgtaVLFVTHDLALaAERADRIMVFRQGEIQEQGATE 239
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSV-AKQSDKIIVLDHGKIIEQGSHD 693
|
250
....*....|....*.
gi 1031820327 240 TIVQrpQHPYTRQLLH 255
Cdd:TIGR01193 694 ELLD--RNGFYASLIH 707
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
277-511 |
1.96e-23 |
|
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: 98.77 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLsrEAQRQLR 356
Cdd:cd03218 1 LRAENLSKRY--GKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNP--FASLDPRQRLFAIIEeplknFERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARAL 434
Cdd:cd03218 75 LGIGYLPQEAsiFRKLTVEENILAVLE-----IRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 435 ILEPAILVLDEATSALD-VTVQAQILALLQQLQQQLGlsyLFIT-HDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDpIAVQDIQKIIKILKDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-243 |
2.37e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 27 SFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRlnrlRGVSISLvpQDpgNSLNPVK 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP----ASGSLTLNGQDHTTTPPSR----RPVSMLF--QE--NNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 107 TIGQQVEeiLRLHQSLS-AAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALD 185
Cdd:PRK10771 87 TVAQNIG--LGLNPGLKlNAAQREKLHAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 186 VTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-236 |
3.28e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.07 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRLNRl 86
Cdd:cd03254 6 ENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTT----LINLLMRFYDPQKGQILIDGIDIRDISRKSLRS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 rgvSISLVPQDPGnsLNPvKTIgqqVEEILrlhqsLSAAERRQQVLNLLAKVGLSHPEQRF--DQYPHQ-------LSGG 157
Cdd:cd03254 78 ---MIGVVLQDTF--LFS-GTI---MENIR-----LGRPNATDEEVIEAAKEAGAHDFIMKlpNGYDTVlgenggnLSQG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 158 MKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQG 236
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEG 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
295-508 |
3.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDAGHLsreaqRQLRRKIQFVYQNPfasldP 372
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNF-----EKLRKHIGIVFQNP-----D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 373 RQRLFAIIEEP----LKNFerlsaATRRQRVESVAARVALAPELLSRT---PRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:PRK13648 94 NQFVGSIVKYDvafgLENH-----AVPYDEMHRRVSEALKQVDMLERAdyePNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 446 ATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLaTVRRIADSVTVLRAGQVVEHGDVNRLF 508
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
290-511 |
3.62e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 290 KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaGHLSREAQRQLRRKIQFVYQNPfas 369
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---EPITKENIREVRKFVGLVFQNP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 370 ldpRQRLFAIIEEPLKNFER----LSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:PRK13652 88 ---DDQIFSPTVEQDIAFGPinlgLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 446 ATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
295-508 |
3.76e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ-RQLRRKIQFVYQnpFasldPR 373
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDiKQIRKKVGLVFQ--F----PE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 QRLFAiiEEPLK-------NFErLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:PRK13649 96 SQLFE--ETVLKdvafgpqNFG-VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 447 TSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLF 508
Cdd:PRK13649 173 TAGLD-PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
294-451 |
3.79e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.69 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS-REaqrqlrRKIQFVYQNpFAsLDP 372
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEpAD------RDIAMVFQN-YA-LYP 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 373 RQRLFAIIEEPLKNfERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:PRK11650 90 HMSVRENMAYGLKI-RGMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
292-508 |
4.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 292 ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ-RQLRRKIQFVYQNPFASL 370
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEiKPVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 371 DPRQRLFAIIEEPlKNFerlsaATRRQRVESVAAR----VALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:PRK13643 98 FEETVLKDVAFGP-QNF-----GIPKEKAEKIAAEklemVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 447 TSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLF 508
Cdd:PRK13643 172 TAGLDPKA-RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
270-508 |
4.44e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 270 RPLATPAI-RVEGISKRFSlGKQA--LQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG- 345
Cdd:PRK13631 14 NPLSDDIIlRVKNLYCVFD-EKQEneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 346 ----------HLSREAQR--QLRRKIQFVYQNP----FASLDPRQRLFAIIEEPLKNFERlsaatrRQRVESVAARVALA 409
Cdd:PRK13631 93 kknnhelitnPYSKKIKNfkELRRRVSMVFQFPeyqlFKDTIEKDIMFGPVALGVKKSEA------KKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 410 PELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADS 489
Cdd:PRK13631 167 DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD-PKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADE 245
|
250
....*....|....*....
gi 1031820327 490 VTVLRAGQVVEHGDVNRLF 508
Cdd:PRK13631 246 VIVMDKGKILKTGTPYEIF 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-531 |
4.69e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 102.30 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISdWSDKRLNRLRGVSI-----SLVPQdpg 99
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKST----LLKILSGNYQPDAGSILIDGQEMR-FASTTAALAAGVAIiyqelHLVPE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nslnpvktigQQVEEILRLHQ------SLSAAERRQQVLNLLAKVGLS-HPEQRFdqypHQLSGGMKQRVLIAIAIALQP 172
Cdd:PRK11288 94 ----------MTVAENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDiDPDTPL----KYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 173 DLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQgatetivqrpqHPYTRQ 252
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT-----------FDDMAQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 253 LLHD-LQDAPLGLTAA-----RHRPLATPAIRVEGISKRfslgkqALQAldSVSFEVRRGSTHALVGESGSGKTTLARIL 326
Cdd:PRK11288 228 VDRDqLVQAMVGREIGdiygyRPRPLGEVRLRLDGLKGP------GLRE--PISFSVRAGEIVGLFGLVGAGRSELMKLL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 327 LGFERADAGQVTIDG-----------IDAG-HLSREaqrqlRRK------IQFVYQNPFASLDPRQRLFAIIEEPLKnfE 388
Cdd:PRK11288 300 YGATRRTAGQVYLDGkpidirsprdaIRAGiMLCPE-----DRKaegiipVHSVADNINISARRHHLRAGCLINNRW--E 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 389 RLSAATRRQRvesvaarvalapeLLSRTP------RELSGGQRQRVAIARALILEPAILVLDEATSALDVTvQAQILALL 462
Cdd:PRK11288 373 AENADRFIRS-------------LNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG-AKHEIYNV 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 463 QQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVehGDVNRLFAAPQQAytreLIAAIPQVSSRLA 531
Cdd:PRK11288 439 IYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAREQATERQA----LSLALPRTSAAVA 501
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-236 |
4.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNG-EVISDWSDKRLNRLRGvSISLVPQDPG 99
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDiTITHKTKDKYIRPVRK-RIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSL-----------NPvKTIGQQVEEIlrlhqslsaaerRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRVLIAIAI 168
Cdd:PRK13646 96 SQLfedtvereiifGP-KNFKMNLDEV------------KNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 169 ALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-451 |
5.91e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 271 PLATPAIRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIdgidAGHLSRE 350
Cdd:PRK13537 2 PMSVAPIDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL----CGEPVPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 351 AQRQLRRKIQFVYQnpFASLDPRqrlFAIIEEpLKNFER---LSAATRRQRVESVAARVALAPELLSRTpRELSGGQRQR 427
Cdd:PRK13537 74 RARHARQRVGVVPQ--FDNLDPD---FTVREN-LLVFGRyfgLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRR 146
|
170 180
....*....|....*....|....
gi 1031820327 428 VAIARALILEPAILVLDEATSALD 451
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-262 |
6.87e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 98.30 E-value: 6.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 8 DLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLR 87
Cdd:PRK11831 9 DMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQI----APDHGEILFDGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 88 GvSISLVPQDpgNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQRVLIAIA 167
Cdd:PRK11831 84 K-RMSMLFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 168 IALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIvQRPQH 247
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPD 236
|
250
....*....|....*
gi 1031820327 248 PYTRQLLHDLQDAPL 262
Cdd:PRK11831 237 PRVRQFLDGIADGPV 251
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-520 |
1.13e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 102.13 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqalDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrQLR 356
Cdd:TIGR01193 474 IVINDVSYSYGYGSNIL---SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH---TLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasldprqrLFA-IIEEPLknferLSAATRRQRVESVAARVALApEL--------------LSRTPRELS 421
Cdd:TIGR01193 548 QFINYLPQEPY--------IFSgSILENL-----LLGAKENVSQDEIWAACEIA-EIkddienmplgyqteLSEEGSSIS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 422 GGQRQRVAIARALILEPAILVLDEATSALDVTVqaqILALLQQLQQQLGLSYLFITHDLaTVRRIADSVTVLRAGQVVEH 501
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTIT---EKKIVNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKIIEQ 689
|
250
....*....|....*....
gi 1031820327 502 GDVNRLFAapQQAYTRELI 520
Cdd:TIGR01193 690 GSHDELLD--RNGFYASLI 706
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-522 |
1.17e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADaGQVTIDG-IDAGHLSREAQR 353
Cdd:PRK14258 6 PAIKVNNLS--FYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 ----QLRRKIQFVYqnpfasldPRQRLFaiieePLKNFERLSAATR----RQR------VESVAARVALAPEL---LSRT 416
Cdd:PRK14258 81 vnlnRLRRQVSMVH--------PKPNLF-----PMSVYDNVAYGVKivgwRPKleiddiVESALKDADLWDEIkhkIHKS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 417 PRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL--- 493
Cdd:PRK14258 148 ALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgn 227
|
250 260 270
....*....|....*....|....*....|.
gi 1031820327 494 --RAGQVVEHGDVNRLFAAPQQAYTRELIAA 522
Cdd:PRK14258 228 enRIGQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
276-509 |
1.28e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 101.74 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGIskRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreaQRQL 355
Cdd:TIGR01846 455 AITFENI--RFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAD---PAWL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQNPFasldprqrLF--AIIE-----EPLKNFERLSAAtrrqrvesvaARVALAPELLSRTPR---------- 418
Cdd:TIGR01846 530 RRQMGVVLQENV--------LFsrSIRDnialcNPGAPFEHVIHA----------AKLAGAHDFISELPQgyntevgekg 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 419 -ELSGGQRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQ 497
Cdd:TIGR01846 592 aNLSGGQRQRIAIARALVGNPRILIFDEATSALD--YESEALIMRNMREICRGRTVIIIAHRLSTVRA-CDRIIVLEKGQ 668
|
250
....*....|..
gi 1031820327 498 VVEHGDVNRLFA 509
Cdd:TIGR01846 669 IAESGRHEELLA 680
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-236 |
1.57e-22 |
|
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: 95.64 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 19 WREVVHNISFSIQ--RGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGE--VISDWSDKrlnrlrgvSISLV 94
Cdd:cd03298 8 FSYGEQPMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETP----QSGRVLINGVdvTAAPPADR--------PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 95 PQDpgNSLNPVKTIGQQVEeiLRLHQSLS-AAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQRVLIAIAIALQPD 173
Cdd:cd03298 76 FQE--NNLFAHLTVEQNVG--LGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 174 LIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
277-509 |
1.92e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.23 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVsfeVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDG--IDaghLSREAQRQ 354
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININ---IKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpID---YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVYQnpfaslDPRQRLF-AIIEEPLK----NFeRLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVA 429
Cdd:PRK13636 80 LRESVGMVFQ------DPDNQLFsASVYQDVSfgavNL-KLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 430 IARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-246 |
2.22e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISDWSD 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP----RDAGNIIIDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRlRGvsISLVPQDPgnSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQyphQLSGGMKQ 160
Cdd:PRK10895 73 HARAR-RG--IGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALD---VTVQKRILDLLdilrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHL----RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
....*....
gi 1031820327 238 TETIVQRPQ 246
Cdd:PRK10895 221 PTEILQDEH 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
277-445 |
2.48e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.87 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS--REAqrq 354
Cdd:COG1137 4 LEAENLVKSY--GKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 lRRKIQFVYQNP--FASLDPRQRLFAIIEeplknFERLSAATRRQRVESvaarvaLAPEL----LSRTP-RELSGGQRQR 427
Cdd:COG1137 77 -RLGIGYLPQEAsiFRKLTVEDNILAVLE-----LRKLSKKEREERLEE------LLEEFgithLRKSKaYSLSGGERRR 144
|
170
....*....|....*...
gi 1031820327 428 VAIARALILEPAILVLDE 445
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-236 |
2.50e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 95.76 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWreVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSdkrL 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKST----LVNLIPRFYDVDSGRILIDGHDVRDYT---L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDP----GNSLNPVK--TIGQQVEEILRlhqSLSAAERRQQVLNLlakvglshPE---QRFDQYPHQL 154
Cdd:cd03251 72 ASLRR-QIGLVSQDVflfnDTVAENIAygRPGATREEVEE---AARAANAHEFIMEL--------PEgydTVIGERGVKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLAlAAERADRIMVFRQGEIQE 234
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVE 216
|
..
gi 1031820327 235 QG 236
Cdd:cd03251 217 RG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-244 |
2.56e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISdwSDKR 82
Cdd:PRK13537 7 PIDFRNVEKRY---GD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL----THPDAGSISLCGEPVP--SRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRgvsISLVPQdpGNSLNPVKTigqqVEEILRL---HQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMK 159
Cdd:PRK13537 77 HARQR---VGVVPQ--FDNLDPDFT----VRENLLVfgrYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH 223
|
....*
gi 1031820327 240 TIVQR 244
Cdd:PRK13537 224 ALIES 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-247 |
2.66e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.42 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTaqaiIGLLADNARRDAGRIVLNGEVISDWSDKRLNRlrgvSISLVPQDPG 99
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRVFDPQSGRILIDGTDIRTVTRASLRR----NIAVVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nslnpvkTIGQQVEEILRL------HQSLSAAERRQQVLNLLAKvglshPEQRFD----QYPHQLSGGMKQRVLIAIAIA 169
Cdd:PRK13657 420 -------LFNRSIEDNIRVgrpdatDEEMRAAAERAQAHDFIER-----KPDGYDtvvgERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 170 LQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVlfVTHDLALAAErADRIMVFRQGEIQEQGATETIVQRPQH 247
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGR 562
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
294-521 |
2.71e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.19 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDA-------GHLS---REAQRQLRRKIQFVY 363
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 364 QNpFASLDPRQRLFAIIEEPLKNFErLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVL 443
Cdd:PRK10619 99 QH-FNLWSHMTVLENVMEAPIQVLG-LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 444 DEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIA 521
Cdd:PRK10619 177 DEPTSALDPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-452 |
2.79e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.24 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKRLNRLrgvSISLVPQDpgnslnp 104
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK----GTITINNINYNKLDHKLAAQL---GIGIIYQE------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQ-QVEEILRLHQSLSA----------AERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPD 173
Cdd:PRK09700 89 LSVIDElTVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 174 LIIADEPTSALdvtVQKRILDLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQG---------EIQEQGATETIV 242
Cdd:PRK09700 166 VIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsgmvsDVSNDDIVRLMV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 243 QRpqhpytrqllhDLQDAPLGLTAARHRPLATPAIRVEGISKRfSLGKqalqaLDSVSFEVRRGSTHALVGESGSGKTTL 322
Cdd:PRK09700 243 GR-----------ELQNRFNAMKENVSNLAHETVFEVRNVTSR-DRKK-----VRDISFSVCRGEILGFAGLVGSGRTEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 323 ARILLGFERADAGQVTIDGIDAGhlSREAQRQLRRKIQFVYQNP-----FASLDPRQRLfaIIEEPLKN------FERLS 391
Cdd:PRK09700 306 MNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYITESRrdngfFPNFSIAQNM--AISRSLKDggykgaMGLFH 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 392 AATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK09700 382 EVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
277-522 |
2.90e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.34 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReaqRQLR 356
Cdd:COG4559 2 LEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSP---WELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RK---------IQFvyqnPFASLDprqrlfaIIE---EPLknfeRLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQ 424
Cdd:COG4559 75 RRravlpqhssLAF----PFTVEE-------VVAlgrAPH----GSSAAQDRQIVREALALVGLAH-LAGRSYQTLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 425 RQRVAIARALI-------LEPAILVLDEATSALD------------------VTVqaqilallqqlqqqlglsyLFITHD 479
Cdd:COG4559 139 QQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDlahqhavlrlarqlarrgGGV-------------------VAVLHD 199
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1031820327 480 LATVRRIADSVTVLRAGQVVEHGdvnrlfaAPQQAYTRELIAA 522
Cdd:COG4559 200 LNLAAQYADRILLLHQGRLVAQG-------TPEEVLTDELLER 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-452 |
3.63e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRdaGRIVLNGEVISDWSDKRLNRlRGVSI-----SLVPQd 97
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYE--GEIIFEGEELQASNIRDTER-AGIAIihqelALVKE- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 pgnslnpvKTIGQQV---EEILRlHQSLSAAERRQQVLNLLAKVGLS-HPEQRFDQYphqlSGGMKQRVLIAIAIALQPD 173
Cdd:PRK13549 97 --------LSVLENIflgNEITP-GGIMDYDAMYLRAQKLLAQLKLDiNPATPVGNL----GLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 174 LIIADEPTSALdvtVQKRILDLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQGE-IQEQGATET--------IV 242
Cdd:PRK13549 164 LLILDEPTASL---TESETAVLLDIIRdlKAHGIACIYISHKLNEVKAISDTICVIRDGRhIGTRPAAGMteddiitmMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 243 QR------PQHPytrqllHDLQDAPLgltAARHRPLATPAIRveGIsKRfslgkqalqaLDSVSFEVRRGSTHALVGESG 316
Cdd:PRK13549 241 GReltalyPREP------HTIGEVIL---EVRNLTAWDPVNP--HI-KR----------VDDVSFSLRRGEILGIAGLVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 317 SGKTTLARILLG-FERADAGQVTIDG-----------IDAG--HLSREAQRQLRRKIQFVYQN-PFASLDpRQRLFAIIE 381
Cdd:PRK13549 299 AGRTELVQCLFGaYPGRWEGEIFIDGkpvkirnpqqaIAQGiaMVPEDRKRDGIVPVMGVGKNiTLAALD-RFTGGSRID 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 382 EPLKnFERLSAATRRQRVESVAARVALApellsrtprELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK13549 378 DAAE-LKTILESIQRLKVKTASPELAIA---------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-263 |
3.92e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.32 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIiGLLAD--NARRDAGRIVLNGEVISDWSDKRLNRLRgvsISLVPQD 97
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNDkvSGYRYSGDVLLGGRSIFNYRDVLEFRRR---VGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 PgnslNPVK-TIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGL-SHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLI 175
Cdd:PRK14271 110 P----NPFPmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 176 IADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHP----YTR 251
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVA 263
|
250
....*....|..
gi 1031820327 252 QLLHDLQDAPLG 263
Cdd:PRK14271 264 GLSGDVKDAKRG 275
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
277-451 |
4.20e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.94 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDsvsFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVT---FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFASLDprQRLFAIIEEPLKnFERLSAATRRQRVESVAARVALAPELLSrTPRELSGGQRQRVAIARALIL 436
Cdd:PRK10908 79 RQIGMIFQDHHLLMD--RTVYDNVAIPLI-IAGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVN 154
|
170
....*....|....*
gi 1031820327 437 EPAILVLDEATSALD 451
Cdd:PRK10908 155 KPAVLLADEPTGNLD 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-236 |
4.36e-22 |
|
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: 94.74 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNG-EVISDWSDKR 82
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL----EPDAGFATVDGfDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNrlrgvsISLVPQDPGnsLNPVKTIGQQVEEILRLHqSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRV 162
Cdd:cd03266 78 RR------LGFVSDSTG--LYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGM---EELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
286-502 |
5.78e-22 |
|
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: 93.15 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 286 FSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidagHLSREAQRQLRRKIQFVYQN 365
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG----VPVSDLEKALSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 366 PFasldprqrLFAiieeplknferlsaATRRQRVEsvaarvalapellsrtpRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:cd03247 84 PY--------LFD--------------TTLRNNLG-----------------RRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 446 ATSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHG 502
Cdd:cd03247 125 PTVGLDPIT--ERQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-232 |
7.94e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.17 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKRLNRLRGvSISLVPQDpg 99
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI----ERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQVEEILRLHQSlSAAERRQQVLNLLAKVGLShpeQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLL---DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 180 PTSALDVTVQKRILDLLDILRReSGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-224 |
9.27e-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: 94.04 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYR--SRGEWR-EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGlladNARRDAGRIVL---NGEV- 74
Cdd:COG4778 3 TLLEVENLSKTFTlhLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG----NYLPDSGSILVrhdGGWVd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 75 ISDWSDKRLNRLRGVSISLVPQdpgnSLN--PVKTIGQQVEEILrLHQSLSAAERRQQVLNLLAKVGLshPEQRFDQYPH 152
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQ----FLRviPRVSALDVVAEPL-LERGVDREEARARARELLARLNL--PERLWDLPPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRI 224
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
9.88e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.51 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRL 83
Cdd:TIGR02857 322 LEFSGVSVAYPGR---RPALRPVSFTVPPGERVALVGPSGAGKST----LLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvSISLVPQDPGnslnpvkTIGQQVEEILRLHQS------LSAAERRQQVLNLLAKVGLSHpEQRFDQYPHQLSGG 157
Cdd:TIGR02857 395 RD----QIAWVPQHPF-------LFAGTIAENIRLARPdasdaeIREALERAGLDEFVAALPQGL-DTPIGEGGAGLSGG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 158 MKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALaAERADRIMV 226
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVV 528
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-242 |
1.08e-21 |
|
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: 98.34 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRS--RGEWReVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdAGRI-VLNGEvisDWS 79
Cdd:TIGR03269 279 IIKVRNVSKRYISvdRGVVK-AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT----SGEVnVRVGD---EWV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 D--KRLNRLRGVS---ISLVPQDpgNSLNPVKTIGQQVEEILRLHQSLSAAERRqqVLNLLAKVGLSHPEQR--FDQYPH 152
Cdd:TIGR03269 351 DmtKPGPDGRGRAkryIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMK--AVITLKMVGFDEEKAEeiLDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALD----VTVQKRILDlldiLRRESGTAVLFVTHDLALAAERADRIMVFR 228
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILK----AREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|....
gi 1031820327 229 QGEIQEQGATETIV 242
Cdd:TIGR03269 503 DGKIVKIGDPEEIV 516
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-258 |
1.09e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.09 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 10 RISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRLNRLRGV 89
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP----ENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 90 --------------SISLVpqDPGNSLnpvktigQQVEEILRL---HQSLSaaERRQQVLNLLAKVGLShpeqrfdqyph 152
Cdd:cd03252 81 vlqenvlfnrsirdNIALA--DPGMSM-------ERVIEAAKLagaHDFIS--ELPEGYDTIVGEQGAG----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 qLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRIL-DLLDILrreSGTAVLFVTHDLAlAAERADRIMVFRQGE 231
Cdd:cd03252 139 -LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMrNMHDIC---AGRTVIIIAHRLS-TVKNADRIIVMEKGR 213
|
250 260
....*....|....*....|....*..
gi 1031820327 232 IQEQGATETIVQRPQHPYTrqlLHDLQ 258
Cdd:cd03252 214 IVEQGSHDELLAENGLYAY---LYQLQ 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
294-520 |
1.11e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.21 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARIL-----LGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQ--NP 366
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQD---IFKMDVIELRRRVQMVFQipNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FASLDprqrLFAIIEEPLKnFERL--SAATRRQRVESVAARVALAPELLSR---TPRELSGGQRQRVAIARALILEPAIL 441
Cdd:PRK14247 94 IPNLS----IFENVALGLK-LNRLvkSKKELQERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 442 VLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELI 520
Cdd:PRK14247 169 LADEPTANLD--PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-502 |
1.11e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 93.71 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFSLGKQAlqALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrQ 354
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH---D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVYQNPF-------ASLDPrqrlfaiieeplknFERLSAATRRQRVESVA--ARVALAPELLSRTPRE----LS 421
Cdd:cd03244 76 LRSRISIIPQDPVlfsgtirSNLDP--------------FGEYSDEELWQALERVGlkEFVESLPGGLDTVVEEggenLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 422 GGQRQRVAIARALILEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATvrrIADS--VTVLRAGQVV 499
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVD--PETDALIQKTIREAFKDCTVLTIAHRLDT---IIDSdrILVLDKGRVV 216
|
...
gi 1031820327 500 EHG 502
Cdd:cd03244 217 EFD 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
277-502 |
1.13e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 93.25 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqLR 356
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNPFasldprqrLFA-IIEEPLKNFERLSAATRRQrvesvAARValapellSRTPRELSGGQRQRVAIARALI 435
Cdd:cd03369 82 SSLTIIPQDPT--------LFSgTIRSNLDPFDEYSDEEIYG-----ALRV-------SEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 436 LEPAILVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIaDSVTVLRAGQVVEHG 502
Cdd:cd03369 142 KRPRVLVLDEATASID--YATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-236 |
1.31e-21 |
|
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: 93.37 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 10 RISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISdwsdkrlnrlrgv 89
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIY----PPDSGTVTVRGRVSS------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 90 sislvPQDPGNSLNPVKTIGQQVEEILRLHqSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIA 169
Cdd:cd03220 88 -----LLGLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSEL---GDFIDLPVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 170 LQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
277-503 |
1.33e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLG-KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ--- 352
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 ------------------RQLRRKIQFVYQnpFASLdprqRLF-AIIEEPLKnFERLSAATRRQRVESVAAR----VALA 409
Cdd:PRK13651 83 vleklviqktrfkkikkiKEIRRRVGVVFQ--FAEY----QLFeQTIEKDII-FGPVSMGVSKEEAKKRAAKyielVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 410 PELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADS 489
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD-PQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKR 234
|
250
....*....|....
gi 1031820327 490 VTVLRAGQVVEHGD 503
Cdd:PRK13651 235 TIFFKDGKIIKDGD 248
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-245 |
1.36e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISyrsRGEWReVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSD 80
Cdd:PRK09536 1 MPMIDVSDLSVE---FGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLrgvsISLVPQDPGNSLNpvkTIGQQVEEILRL-HQS----LSAAERRQqVLNLLAKVGLShpeQRFDQYPHQLS 155
Cdd:PRK09536 73 RAASRR----VASVPQDTSLSFE---FDVRQVVEMGRTpHRSrfdtWTETDRAA-VERAMERTGVA---QFADRPVTSLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
|
250
....*....|
gi 1031820327 236 GATETIVQRP 245
Cdd:PRK09536 221 GPPADVLTAD 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
275-493 |
1.39e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.13 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFslgKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREaqrQ 354
Cdd:TIGR02857 320 SSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---S 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVYQNPF---ASLDPRQRLF------AIIEEplknferlsAATRRQRVESVAARVALAPELLSRTPRELSGGQR 425
Cdd:TIGR02857 394 WRDQIAWVPQHPFlfaGTIAENIRLArpdasdAEIRE---------ALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 426 QRVAIARALILEPAILVLDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVL 493
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAE--TEAEVLEALRALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
273-501 |
1.67e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsrEAQ 352
Cdd:PRK11288 1 SSPYLSFDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG--------QEM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RqlrrkiqfvYQNPFASLDPRqrlFAIIEEPLKNFERLSAA---------------TRRQRVESVAARVA-LAPELLSRT 416
Cdd:PRK11288 69 R---------FASTTAALAAG---VAIIYQELHLVPEMTVAenlylgqlphkggivNRRLLNYEAREQLEhLGVDIDPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 417 P-RELSGGQRQRVAIARALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRA 495
Cdd:PRK11288 137 PlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR-EIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKD 215
|
....*.
gi 1031820327 496 GQVVEH 501
Cdd:PRK11288 216 GRYVAT 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-252 |
1.97e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.82 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNAR-RDAGRIVLNGEVISDWS 79
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV----EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEaRVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 DKRLNRlrgvSISLVPQDPgnslNPVKT--IGQQVEEILRLHQSL-SAAERRQQVLNLLAKVGL-SHPEQRFDQYPHQLS 155
Cdd:PRK14247 77 VIELRR----RVQMVFQIP----NPIPNlsIFENVALGLKLNRLVkSKKELQERVRWALEKAQLwDEVKDRLDAPAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
250
....*....|....*..
gi 1031820327 236 GATETIVQRPQHPYTRQ 252
Cdd:PRK14247 227 GPTREVFTNPRHELTEK 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
292-515 |
2.29e-21 |
|
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: 93.12 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 292 ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreAQRQLRRKIQFVYQNpfasld 371
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP--PHRIARLGIGYVPEG------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 prQRLFAI--IEEPLknfeRLSAATRRQR--VESVAARV-ALAPELLSRTPR---ELSGGQRQRVAIARALILEPAILVL 443
Cdd:COG0410 87 --RRIFPSltVEENL----LLGAYARRDRaeVRADLERVyELFPRLKERRRQragTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 444 DEATSAL------------------DVTVqaqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAGQVVEHGDVN 505
Cdd:COG0410 161 DEPSLGLapliveeifeiirrlnreGVTI-------------------LLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
250
....*....|..
gi 1031820327 506 RLFAAP--QQAY 515
Cdd:COG0410 222 ELLADPevREAY 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
296-520 |
2.69e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.57 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGiDAGHLSREAQR----QLRRKIQFVYQ--NPFas 369
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG-KVLYFGKDIFQidaiKLRKEVGMVFQqpNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 370 ldPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSR--TP-RELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnSPaSQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 447 TSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELI 520
Cdd:PRK14246 181 TSMIDIV--NSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
287-451 |
2.74e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.16 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 287 SLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA---GQVTIDGIDAGHLSREaqrqlRRKIQFVY 363
Cdd:COG4136 10 TLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE-----QRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 364 QNP--FASLDPRQRL-FAIieePlknfERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAI 440
Cdd:COG4136 83 QDDllFPHLSVGENLaFAL---P----PTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170
....*....|.
gi 1031820327 441 LVLDEATSALD 451
Cdd:COG4136 155 LLLDEPFSKLD 165
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-234 |
3.23e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLnGEvisdwsdk 81
Cdd:COG0488 314 KVLELEGLSKSY---GD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP----DSGTVKL-GE-------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 rlnrlrGVSISLVPQDpGNSLNPVKTIgqqVEEIlrlhQSLSAAERRQQVLNLLAKVGLSHPEQRfdQYPHQLSGGMKQR 161
Cdd:COG0488 377 ------TVKIGYFDQH-QEELDPDKTV---LDEL----RDGAPGGTEQEVRGYLGRFLFSGDDAF--KPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDV-TVQKrildLLDILRRESGTaVLFVTHDLALAAERADRIMVFRQGEIQE 234
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPGT-VLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-254 |
4.16e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNAR-RDAGRIVLNGEVI--SD 77
Cdd:PRK14267 2 KFAIETVNLRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEaRVEGEVRLFGRNIysPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 78 WSDKRLNRlrgvSISLVPQDPgnslNPVK--TIGQQVEEILRLHQSL-SAAERRQQVLNLLAKVGL-SHPEQRFDQYPHQ 153
Cdd:PRK14267 78 VDPIEVRR----EVGMVFQYP----NPFPhlTIYDNVAIGVKLNGLVkSKKELDERVEWALKKAALwDEVKDRLNDYPSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 154 LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFRQGEIQ 233
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
250 260
....*....|....*....|.
gi 1031820327 234 EQGATETIVQRPQHPYTRQLL 254
Cdd:PRK14267 228 EVGPTRKVFENPEHELTEKYV 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-498 |
4.33e-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: 96.43 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARrdAGRIVLNGEVISDwSDKRLNRLRGVSI-----SLVPQD 97
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW--DGEIYWSGSPLKA-SNIRDTERAGIVIihqelTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 P-------GNSLNPVKTIGQQVEEILRLHQSLsaAERRQQVLNLLAKVGlshpeqrfdqyphQLSGGMKQRVLIAIAIAL 170
Cdd:TIGR02633 94 SvaeniflGNEITLPGGRMAYNAMYLRAKNLL--RELQLDADNVTRPVG-------------DYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 171 QPDLIIADEPTSALdvtVQKRILDLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQGE---------IQEQGATE 239
Cdd:TIGR02633 159 QARLLILDEPSSSL---TEKETEILLDIIRdlKAHGVACVYISHKLNEVKAVCDTICVIRDGQhvatkdmstMSEDDIIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 240 TIVQR------PQHPytrqllHDLQDAPL---GLTAarHRPLATPAIRVegiskrfslgkqalqalDSVSFEVRRGSTHA 310
Cdd:TIGR02633 236 MMVGReitslyPHEP------HEIGDVILearNLTC--WDVINPHRKRV-----------------DDVSFSLRRGEILG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 311 LVGESGSGKTTLARILLG-FERADAGQVTIDG--IDaghlSREAQRQLRRKIQFVYQNpfaslDPRQRLFAIIE------ 381
Cdd:TIGR02633 291 VAGLVGAGRTELVQALFGaYPGKFEGNVFINGkpVD----IRNPAQAIRAGIAMVPED-----RKRHGIVPILGvgknit 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 382 -EPLKNFE---RLSAATRRQRVESVAARVAL---APEL-LSRtpreLSGGQRQRVAIARALILEPAILVLDEATSALDVT 453
Cdd:TIGR02633 362 lSVLKSFCfkmRIDAAAELQIIGSAIQRLKVktaSPFLpIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1031820327 454 vQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:TIGR02633 438 -AKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
276-507 |
4.62e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFslgKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQL 355
Cdd:PRK13647 4 IIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE---VNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 RRKIQFVYQnpfaslDPRQRLFAIIEEPLKNF----ERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIA 431
Cdd:PRK13647 78 RSKVGLVFQ------DPDDQVFSSTVWDDVAFgpvnMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 432 RALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPR-GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-232 |
5.56e-21 |
|
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: 91.76 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQaiigLLADNARRDAGRIVLNGEVISDWSDKRLNRl 86
Cdd:cd03248 15 QNVTFAYPTRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVA----LLENFYQPQGGQVLLDGKPISQYEHKYLHS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 rgvSISLVPQDP---GNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLakvglSHPEQRFDQYPHQLSGGMKQRVL 163
Cdd:cd03248 89 ---KVSLVGQEPvlfARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELA-----SGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLL-DILRRESgtaVLFVTHDLALaAERADRIMVFRQGEI 232
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALyDWPERRT---VLVIAHRLST-VERADQILVLDGGRI 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
294-521 |
5.65e-21 |
|
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: 91.82 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreAQRQLRRKIQFVYQNP--FASLD 371
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP--PHERARAGIAYVPQGReiFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 prqrlfaiIEEPLKnferLSAATRRQRVESVAARV-ALAP---ELLSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:TIGR03410 92 --------VEENLL----TGLAALPRRSRKIPDEIyELFPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 448 SALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLfaapQQAYTRELIA 521
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-232 |
6.02e-21 |
|
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: 90.69 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSR--GEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGlladnaRRDAGRIvlNGEVISDWSD 80
Cdd:cd03213 3 TLSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG------RRTGLGV--SGEVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGvSISLVPQDpgNSLNPVKTigqqVEEILRLhqslsAAERRqqvlnllakvglshpeqrfdqyphQLSGGMKQ 160
Cdd:cd03213 75 LDKRSFRK-IIGYVPQD--DILHPTLT----VRETLMF-----AAKLR------------------------GLSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTvqkRILDLLDILRRES--GTAVLFVTHDL-ALAAERADRIMVFRQGEI 232
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSS---SALQVMSLLRRLAdtGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-252 |
6.17e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGL--LADNARRDaGRIVLNGEVISDWS 79
Cdd:PRK14243 9 TVLRTENLNVYYGSF----LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRVE-GKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 80 -DKRLNRLRgvsISLVPQDPgnslNPV-KTI-----------GQQVEEILRLHQSLSAAERRQQVLNLLAKVGLShpeqr 146
Cdd:PRK14243 84 vDPVEVRRR---IGMVFQKP----NPFpKSIydniaygarinGYKGDMDELVERSLRQAALWDEVKDKLKQSGLS----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 147 fdqyphqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMV 226
Cdd:PRK14243 152 -------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAF 222
|
250 260 270
....*....|....*....|....*....|....*
gi 1031820327 227 F---------RQGEIQEQGATETIVQRPQHPYTRQ 252
Cdd:PRK14243 223 FnveltegggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-236 |
6.98e-21 |
|
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: 91.11 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 11 ISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDW--SDKRLNrlrg 88
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLdpADLRRN---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 89 vsISLVPQDPG---NSLNPVKTIGQQV---EEILRlhqslsaAERRQQVLNLLAKvglsHP---EQRFDQYPHQLSGGMK 159
Cdd:cd03245 80 --IGYVPQDVTlfyGTLRDNITLGAPLaddERILR-------AAELAGVTDFVNK----HPnglDLQIGERGRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALaAERADRIMVFRQGEIQEQG 236
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-250 |
7.30e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAI--IGLLADNARRdAGRIVLNGEVI---- 75
Cdd:PRK14239 4 PILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTI-TGSIVYNGHNIyspr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 76 SDWSDKRlnrlrgVSISLVPQDPgnslNPVK-TIGQQVEEILRLhqslsAAERRQQVLNLLAKVGL------SHPEQRFD 148
Cdd:PRK14239 79 TDTVDLR------KEIGMVFQQP----NPFPmSIYENVVYGLRL-----KGIKDKQVLDEAVEKSLkgasiwDEVKDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 149 QYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFR 228
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|..
gi 1031820327 229 QGEIQEQGATETIVQRPQHPYT 250
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKET 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-244 |
7.89e-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: 95.97 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEdlRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:COG4618 331 LSVE--NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW----PPTAGSVRLDGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlrGVSISLVPQD----PGnslnpvkTIGqqvEEILRLhqslsAAERRQQVLNLLAKVG-----LSHP---EQRFDQYP 151
Cdd:COG4618 405 ----GRHIGYLPQDvelfDG-------TIA---ENIARF-----GDADPEKVVAAAKLAGvhemiLRLPdgyDTRIGEGG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAErADRIMVFRQGE 231
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGR 543
|
250
....*....|...
gi 1031820327 232 IQEQGATETIVQR 244
Cdd:COG4618 544 VQAFGPRDEVLAR 556
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-452 |
8.77e-21 |
|
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: 96.01 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 31 QRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIvlNGEVisDWsDKRLNRLRGVSIslvpQDPGNSL--NPVKTI 108
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNL----GDY--DEEP--SW-DEVLKRFRGTEL----QDYFKKLanGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 109 --GQQVEEILRLH-----QSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPT 181
Cdd:COG1245 164 hkPQYVDLIPKVFkgtvrELLEKVDERGKLDELAEKLGLEN---ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 182 SALDV----TVQKRILDLLdilrrESGTAVLFVTHDLALAAERADRIMVFrQGEIQEQGatetIVQRPQHP------YTR 251
Cdd:COG1245 241 SYLDIyqrlNVARLIRELA-----EEGKYVLVVEHDLAILDYLADYVHIL-YGEPGVYG----VVSKPKSVrvginqYLD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 252 QLLHD----LQDAPLGLTAARHRPLATPAIRVE--GISKRFSLGKqalqaLDSVSFEVRRGSTHALVGESGSGKTTLARI 325
Cdd:COG1245 311 GYLPEenvrIRDEPIEFEVHAPRREKEEETLVEypDLTKSYGGFS-----LEVEGGEIREGEVLGIVGPNGIGKTTFAKI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 326 LLGFERADAGQVTIDgIDaghLSREAQrqlrrkiqfvYQNPFASLDPRQRLFAIIEEPLKN--FErlsaatrrqrvESVA 403
Cdd:COG1245 386 LAGVLKPDEGEVDED-LK---ISYKPQ----------YISPDYDGTVEEFLRSANTDDFGSsyYK-----------TEII 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1031820327 404 ARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:COG1245 441 KPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-244 |
9.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVI-SDWSDKRLNRLRGvSISLVPQDPGNSL- 102
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ----GSVRVDDTLItSTSKNKDIKQIRK-KVGLVFQFPESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 --NPVKTI--GQQveeilrlHQSLSAAERRQQVLNLLAKVGLShpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIAD 178
Cdd:PRK13649 100 eeTVLKDVafGPQ-------NFGVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 179 EPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQR 244
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
256-528 |
1.00e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.56 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 256 DLQDAPLGLTAARHRPLATPAIRVEGISKRFSLGKQALQaldSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAG 335
Cdd:PRK10790 320 ELMDGPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQ---NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 336 QVTIDGIDAGHLSREAqrqLRRKIQFVYQNPFASLDPrqrLFAIIeeplknfeRLSAATRRQRVESVAARVALAPelLSR 415
Cdd:PRK10790 397 EIRLDGRPLSSLSHSV---LRQGVAMVQQDPVVLADT---FLANV--------TLGRDISEEQVWQALETVQLAE--LAR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 416 TPRE------------LSGGQRQRVAIARALILEPAILVLDEATSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATV 483
Cdd:PRK10790 461 SLPDglytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGT--EQAIQQALAAVREHTTLVVIAHRLSTI 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 484 RRiADSVTVLRAGQVVEHGDVNRLFAAP---------QQAyTRELIAAIPQVSS 528
Cdd:PRK10790 539 VE-ADTILVLHRGQAVEQGTHQQLLAAQgrywqmyqlQLA-GEELAASVREEES 590
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-245 |
1.11e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 8 DLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRLNRlr 87
Cdd:TIGR00958 483 DVSFSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKST----VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR-- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 88 gvSISLVPQDPgnslnpVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFD----QYPHQLSGGMKQRVL 163
Cdd:TIGR00958 556 --QVALVGQEP------VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKrildLLDILRRESGTAVLFVTHDLALaAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLST-VERADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 1031820327 244 RP 245
Cdd:TIGR00958 703 DQ 704
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
274-504 |
1.15e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSLG-------KQAL-----------QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAG 335
Cdd:COG1134 2 SSMIEVENVSKSYRLYhepsrslKELLlrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 336 QVTIDGIDA----------GHLS-RE-----------AQRQLRRKIQFVYQnpFASLDPrqrlFaiIEEPLKNFerlsaa 393
Cdd:COG1134 82 RVEVNGRVSallelgagfhPELTgREniylngrllglSRKEIDEKFDEIVE--FAELGD----F--IDQPVKTY------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 394 trrqrvesvaarvalapellsrtprelSGGQRQRVAIARALILEPAILVLDEATSALDV------------------TVq 455
Cdd:COG1134 148 ---------------------------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkkclarirelresgrTV- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1031820327 456 aqilallqqlqqqlglsyLFITHDLATVRRIADSVTVLRAGQVVEHGDV 504
Cdd:COG1134 200 ------------------IFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
293-509 |
1.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.38 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 293 LQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQvTIDG---IDAGHLSREAQRQLRRKIQFVYQNPfas 369
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaIPANLKKIKEVKRLRKEIGLVFQFP--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 370 ldpRQRLFAIIEEPLKNFERLSAATRRQ----RVESVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:PRK13645 100 ---EYQLFQETIEKDIAFGPVNLGENKQeaykKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 446 ATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-237 |
1.43e-20 |
|
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: 90.25 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWreVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEvisDWSDKRL 83
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV----ELSSGSILIDGV---DISKIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDP----G---NSLNPvktIGQQVEEilRLHQSLSAAERRQQVLNLLAkvGLSHPEQRFDQyphQLSG 156
Cdd:cd03244 74 HDLRS-RISIIPQDPvlfsGtirSNLDP---FGEYSDE--ELWQALERVGLKEFVESLPG--GLDTVVEEGGE---NLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 157 GMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLldiLRRE-SGTAVLFVTHDLALAAErADRIMVFRQGEIQEQ 235
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEF 218
|
..
gi 1031820327 236 GA 237
Cdd:cd03244 219 DS 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-242 |
1.75e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKRLNRlrgvSISLVPQD---P 98
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH----GHVWLDGEHIQHYASKEVAR----RIGLLAQNattP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 GNSlnpvkTIGQQVEEILRLHQSLSAAERRQQ---VLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDLI 175
Cdd:PRK10253 94 GDI-----TVQELVARGRYPHQPLFTRWRKEDeeaVTKAMQATGITHLA---DQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 176 IADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIV 242
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
295-527 |
3.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAghLSREAQRQLRRKIQFVYQNPfasldPRQ 374
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT--SDEENLWDIRNKAGMVFQNP-----DNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAIIEEPLKnF--ERLSAATR--RQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:PRK13633 98 IVATIVEEDVA-FgpENLGIPPEeiRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 451 DVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFaaPQQAYTRELIAAIPQVS 527
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEMMKKIGLDVPQVT 249
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
275-520 |
3.40e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.22 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRFSLGKqalqALDSVSFEVRRGSTHALVGESGSGKTTLARIL-----LGFERADAGQVTIDGIDAgHLSR 349
Cdd:PRK14239 4 PILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNI-YSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 350 EAQRQLRRKIQFVYQ--NPFASLDPRQRLFAIIEEPLKNFERLSAAtrrqrVESVAARVALAPELLSR---TPRELSGGQ 424
Cdd:PRK14239 79 TDTVDLRKEIGMVFQqpNPFPMSIYENVVYGLRLKGIKDKQVLDEA-----VEKSLKGASIWDEVKDRlhdSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 425 RQRVAIARALILEPAILVLDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDV 504
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
250
....*....|....*.
gi 1031820327 505 NRLFAAPQQAYTRELI 520
Cdd:PRK14239 232 KQMFMNPKHKETEDYI 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
275-522 |
3.54e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.22 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSReAQRQ 354
Cdd:PRK13548 1 AMLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRR-------KIQFvyqnPFASLDprqrlfaIIE---EPLknfeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQ 424
Cdd:PRK13548 76 RRRavlpqhsSLSF----PFTVEE-------VVAmgrAPH----GLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 425 RQRVAIARALI------LEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250 260
....*....|....*....|....
gi 1031820327 499 VEHGdvnrlfaAPQQAYTRELIAA 522
Cdd:PRK13548 220 VADG-------TPAEVLTPETLRR 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
299-512 |
3.79e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.01 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 299 VSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaQRQ-----LRRKIQFVYQNpfASLDPR 373
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE----------KRMndvppAERGVGMVFQS--YALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 QRLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVT 453
Cdd:PRK11000 90 LSVAENMSFGLK-LAGAKKEEINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 454 VQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-236 |
3.97e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 89.00 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGeviSDWSDKRL 83
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL----RPTSGEIIFDG---HPWTRKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlrgvsislvpqdpgnslnpvKTIGQQVEEIlRLHQSLSAAER-----------RQQVLNLLAKVGLSHPEQRfdqYPH 152
Cdd:TIGR03740 70 ----------------------HKIGSLIESP-PLYENLTARENlkvhttllglpDSRIDEVLNIVDLTNTGKK---KAK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTvqkRILDLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:TIGR03740 124 QFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPI---GIQELRELIRsfPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
....*.
gi 1031820327 231 EIQEQG 236
Cdd:TIGR03740 201 VLGYQG 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
241-454 |
4.96e-20 |
|
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: 93.19 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 241 IVQRPQHPYTRQLLHDLQDAPLG-----LTAARHRPLATPAIRVEGISKRFSlgkQALQALDSVSFEVRRGSTHALVGES 315
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPvaegsAPAAGAVGLGKPTLELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 316 GSGKTTLARILLGFERADAGQVTIDGIDAGHLSreaQRQLRRKIQFVYQNP--FASlDPRQRLfaIIEEPLKNFERLSAA 393
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD---QDEVRRRVSVCAQDAhlFDT-TVRENL--RLARPDATDEELWAA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 394 TRRQRVES-VAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTV 454
Cdd:TIGR02868 445 LERVGLADwLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
263-523 |
5.54e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.16 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 263 GLTAARHRPLATPAIrvegISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGI 342
Cdd:PRK14271 8 GQSGAADVDAAAPAM----AAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 343 DAGHLSREAQR---QLRRKIQFVYQ--NPFAsLDPRQRLFAIIEE----PLKNFERLSAAtrrqRVESVAARVALApELL 413
Cdd:PRK14271 84 LLGGRSIFNYRdvlEFRRRVGMLFQrpNPFP-MSIMDNVLAGVRAhklvPRKEFRGVAQA----RLTEVGLWDAVK-DRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 414 SRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:PRK14271 158 SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTT--TEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALF 235
|
250 260 270
....*....|....*....|....*....|
gi 1031820327 494 RAGQVVEHGDVNRLFAAPQQAYTRELIAAI 523
Cdd:PRK14271 236 FDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
290-502 |
5.65e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 88.93 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 290 KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGhlsrEAQRQLRRKIQFVY---QNP 366
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW----KRRKKFLRRIGVVFgqkTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FASLDPRQRLfaiieEPLKNFERLSAATRRQRVESVAARVALAPELlsRTP-RELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:cd03267 107 WWDLPVIDSF-----YLLAAIYDLPPARFKKRLDELSELLDLEELL--DTPvRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 446 ATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-236 |
5.84e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.36 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLlaDNARRDAGRIVLNGEVISDWS-DKR 82
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSILLDGEDILELSpDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRlrGVSISLvpQdpgnslNPVKTIGQQVEEILRL------HQSLSAAERRQQVLNLLAKVGLShpeqrfDQYPHQ--- 153
Cdd:COG0396 75 ARA--GIFLAF--Q------YPVEIPGVSVSNFLRTalnarrGEELSAREFLKLLKEKMKELGLD------EDFLDRyvn 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 154 --LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLA-LAAERADRIMVFRQG 230
Cdd:COG0396 139 egFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRiLDYIKPDFVHVLVDG 217
|
....*.
gi 1031820327 231 EIQEQG 236
Cdd:COG0396 218 RIVKSG 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
267-502 |
6.18e-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: 93.18 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 267 ARHRPLATPA----IRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGI 342
Cdd:TIGR01842 303 SRDPAMPLPEpeghLSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 343 DaghLSREAQRQLRRKIQFVYQNpfasldprQRLFA-IIEEPLKNFERlsAATRRQRVEsvAARVALAPELLSRTPR--- 418
Cdd:TIGR01842 381 D---LKQWDRETFGKHIGYLPQD--------VELFPgTVAENIARFGE--NADPEKIIE--AAKLAGVHELILRLPDgyd 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 419 --------ELSGGQRQRVAIARALILEPAILVLDEATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLAtVRRIADSV 490
Cdd:TIGR01842 446 tvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLD-EEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKI 523
|
250
....*....|..
gi 1031820327 491 TVLRAGQVVEHG 502
Cdd:TIGR01842 524 LVLQDGRIARFG 535
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
296-503 |
7.49e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 7.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFE--RADAGQVTIDGIDAGHLSREaQRQlRRKIQFVYQNPfasldpr 373
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPD-ERA-RAGIFLAFQYP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 qrlfaiIEEP---LKNFERLSAATRRQ----------RVESVAARVALAPELLSRTPRE-LSGGQRQRVAIARALILEPA 439
Cdd:COG0396 87 ------VEIPgvsVSNFLRTALNARRGeelsareflkLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 440 ILVLDEATSALDV----TVqaqilALLQQLQQQLGLSYLFITHdlatVRRI-----ADSVTVLRAGQVVEHGD 503
Cdd:COG0396 161 LAILDETDSGLDIdalrIV-----AEGVNKLRSPDRGILIITH----YQRIldyikPDFVHVLVDGRIVKSGG 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
277-451 |
8.52e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.30 E-value: 8.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 -RKIQFVYQNpfasldprqrlFAIIE--EPLKNFErLSAATR-------RQRVESVAARVALApELLSRTPRELSGGQRQ 426
Cdd:PRK10584 87 aKHVGFVFQS-----------FMLIPtlNALENVE-LPALLRgessrqsRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQ 153
|
170 180
....*....|....*....|....*
gi 1031820327 427 RVAIARALILEPAILVLDEATSALD 451
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
273-527 |
1.05e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQ 352
Cdd:PRK15439 8 APPLLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLrrKIQFVYQNP--FASLDPRQRLFAIIEEPLKNFERLSAATRrqrvesvAARVALAPELLSRTpreLSGGQRQRVAI 430
Cdd:PRK15439 84 HQL--GIYLVPQEPllFPNLSVKENILFGLPKRQASMQKMKQLLA-------ALGCQLDLDSSAGS---LEVADRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 431 ARALILEPAILVLDEATSALdVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVehgdvnrLFAA 510
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASL-TPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA-------LSGK 223
|
250
....*....|....*..
gi 1031820327 511 PQQAYTRELIAAIPQVS 527
Cdd:PRK15439 224 TADLSTDDIIQAITPAA 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
275-502 |
1.05e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreaQRQ 354
Cdd:PRK09536 2 PMIDVSDLS--VEFGDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS---ARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIQFVYQNPFASLDPRQRlfAIIE---EP-LKNFERLSAATRRQrVESVAARVALApELLSRTPRELSGGQRQRVAI 430
Cdd:PRK09536 75 ASRRVASVPQDTSLSFEFDVR--QVVEmgrTPhRSRFDTWTETDRAA-VERAMERTGVA-QFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 431 ARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFItHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
294-512 |
1.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.98 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHlSREAQRQLRRKIQFVYQNPfasldpR 373
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLLEVRKTVGIVFQNP------D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 QRLFA-IIEE-----PLkNFeRLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:PRK13639 89 DQLFApTVEEdvafgPL-NL-GLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 448 SALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK13639 166 SGLD-PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-232 |
1.46e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYrsrGEwREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDk 81
Cdd:PRK11247 11 TPLLLNAVSKRY---GE-RTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLAGLETPSAGELLAGTAPLAEARE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 rlnrlrgvSISLVPQDPgnSLNPVKTIGQQVEEILRLHQslsaaerRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQR 161
Cdd:PRK11247 82 --------DTRLMFQDA--RLLPWKKVIDNVGLGLKGQW-------RDAALQALAAVGL---ADRANEWPAALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-224 |
2.13e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVlngevisdwsdkrlnRLRGVSISLVPQ--D 97
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL----RPTSGTVR---------------RAGGARVAYVPQrsE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 PGNSLnPVkTIGQQVEEILRLHQSLS---AAERRQQVLNLLAKVGLshpeQRFDQYP-HQLSGGMKQRVLIAIAIALQPD 173
Cdd:NF040873 66 VPDSL-PL-TVRDLVAMGRWARRGLWrrlTRDDRAAVDDALERVGL----ADLAGRQlGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 174 LIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAeRADRI 224
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPC 188
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
2.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWR-EVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADN----ARRD---AGRIVLNGEV 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtiQVGDiyiGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 75 ISDWSDK--RLNRLRGVsISLVPQDPGNSL-----------NPVkTIGQQVEEilrlhqslsAAERRQQVLNllaKVGLS 141
Cdd:PRK13631 101 TNPYSKKikNFKELRRR-VSMVFQFPEYQLfkdtiekdimfGPV-ALGVKKSE---------AKKLAKFYLN---KMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 142 HPeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLdILRRESGTAVLFVTHDLALAAERA 221
Cdd:PRK13631 167 DS--YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVA 243
|
250
....*....|....*
gi 1031820327 222 DRIMVFRQGEIQEQG 236
Cdd:PRK13631 244 DEVIVMDKGKILKTG 258
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-451 |
2.53e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 90.84 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 27 SFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnarrdagrIVLNGEVISDW------SDKRLNRLrgvsISLVPQDPGN 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGEL----------PLLSGERQSQFshitrlSFEQLQKL----VSDEWQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 SLNPVKT--IGQQVEEILRLHqsLSAAERRQQvlnLLAKVGLSHP-EQRFDQyphqLSGGMKQRVLIAIAIALQPDLIIA 177
Cdd:PRK10938 89 DMLSPGEddTGRTTAEIIQDE--VKDPARCEQ---LAQQFGITALlDRRFKY----LSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 178 DEPTSALDVTVQKRILDLLDILRRESGTAVLFVT--HDLalaAERADRIMVFRQGEIQEQGATETIVQRpqhPYTRQLLH 255
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGITLVLVLNrfDEI---PDFVQFAGVLADCTLAETGEREEILQQ---ALVAQLAH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 256 --DLQDAPLGLTAArhrPLATPAIrVEGISkRFSLGKQALQ-----ALDSVSFEVRRGSTHALVGESGSGKTTLARILLG 328
Cdd:PRK10938 234 seQLEGVQLPEPDE---PSARHAL-PANEP-RIVLNNGVVSyndrpILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 329 -FERADAGQVTIDGIDAGhlSREAQRQLRRKIQFVYQNpfASLDPR---QRLFAIIEEPLKNFERLSAATRRQRVES--- 401
Cdd:PRK10938 309 dHPQGYSNDLTLFGRRRG--SGETIWDIKKHIGYVSSS--LHLDYRvstSVRNVILSGFFDSIGIYQAVSDRQQKLAqqw 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 402 -----VAARVALAPEllsrtpRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:PRK10938 385 ldilgIDKRTADAPF------HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-257 |
2.87e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLAdnaRRDAGRIVLNGEVI---SDWSDKRLNRLRGvSISLVPQD 97
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLE---MPRSGTLNIAGNHFdfsKTPSDKAIRELRR-NVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 pgNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIA 177
Cdd:PRK11124 91 --YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRL---KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 178 DEPTSALD--VTVQkrildLLDILRRESGTAV--LFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQrpqhPYTRQL 253
Cdd:PRK11124 166 DEPTAALDpeITAQ-----IVSIIRELAETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ----PQTEAF 236
|
....
gi 1031820327 254 LHDL 257
Cdd:PRK11124 237 KNYL 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-257 |
3.55e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLaDNArrDAGRIVLNGEVIS---DWSDKRLNRLRGvSISLVPQD 97
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLL-ETP--DSGQLNIAGHQFDfsqKPSEKAIRLLRQ-KVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 pgNSLNPVKTIGQQ-VEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQRVLIAIAIALQPDLII 176
Cdd:COG4161 91 --YNLWPHLTVMENlIEAPCKV-LGLSKEQAREKAMKLLARLRLTDKADRF---PLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 177 ADEPTSALDVTVQKRIldlLDILRRESGTAV--LFVTHDLALAAERADRIMVFRQGEIQEQGATETIvqrpQHPYTRQLL 254
Cdd:COG4161 165 FDEPTAALDPEITAQV---VEIIRELSQTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEAFA 237
|
...
gi 1031820327 255 HDL 257
Cdd:COG4161 238 HYL 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
289-511 |
5.12e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 289 GKQALQALdsvSFEVRRGSTHALVGESGSGKTTLARILLGFeRADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPfa 368
Cdd:PRK11174 362 GKTLAGPL---NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIE---LRELDPESWRKHLSWVGQNP-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 369 sldprqRLFA--IIEEPLKNFERLSAATRRQRVES--VAARVALAPELLSRTPRE----LSGGQRQRVAIARALILEPAI 440
Cdd:PRK11174 433 ------QLPHgtLRDNVLLGNPDASDEQLQQALENawVSEFLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 441 LVLDEATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIaDSVTVLRAGQVVEHGDVNRLFAAP 511
Cdd:PRK11174 507 LLLDEPTASLD--AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-241 |
5.28e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.53 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 26 ISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarrDAGRIVLNGEVISDWSDKRLNRLRGVsisLVPQDPGNSLNPV 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRAY---LSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 106 KtigqqveEILRLHQSLSAAER-RQQVLNLLA-KVGLShpeqrfDQYP---HQLSGGMKQRVLIAiAIALQ--PD----- 173
Cdd:PRK03695 87 F-------QYLTLHQPDKTRTEaVASALNEVAeALGLD------DKLGrsvNQLSGGEWQRVRLA-AVVLQvwPDinpag 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 174 -LIIADEPTSALDVTvQKRILDLLdiLRR--ESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI 241
Cdd:PRK03695 153 qLLLLDEPMNSLDVA-QQAALDRL--LSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-236 |
5.73e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.67 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWreVVHNISFSIQRGEMLAFVGESGSGKTTTAQaiigLLADNARRDAGRIVLNGEVISDWSDKRL 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQ----LLTGDLKPQQGEITLDGVPVSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NrlrgvSISLVPQDPgnslnpvktigqqveeilrlhqSLSAAerrqqvlNLLAKVGLshpeqrfdqyphQLSGGMKQRVL 163
Cdd:cd03247 75 S-----LISVLNQRP----------------------YLFDT-------TLRNNLGR------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLL-DILRresGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQG 236
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVLK---DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-252 |
7.29e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLA--DNARRDAGRIVLNGEVISDWSDKRLNRlrgvSISLVPQD 97
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 PgnslNPVK--TIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGL-SHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDL 174
Cdd:PRK14246 99 P----NPFPhlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 175 IIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQRPQHPYTRQ 252
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
277-507 |
1.00e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.36 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLR 356
Cdd:PRK11831 8 VDMRGVS--FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 357 RKIQFVYQNpfASLDPRQRLFAIIEEPLKNFERLSAATRRQRV----ESVAARVAlaPELLsrtPRELSGGQRQRVAIAR 432
Cdd:PRK11831 84 KRMSMLFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVmmklEAVGLRGA--AKLM---PSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 433 ALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRL 507
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-236 |
1.01e-18 |
|
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: 84.50 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISyrsRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLlaDNARRDAGRIVLNGEVISDWS-DKR 82
Cdd:cd03217 1 LEIKDLHVS---VGG-KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPpEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LnrLRGvsISLVPQdpgnslNPVKTIGQQVEEILRlhqslsaaerrqqVLNllakVGLShpeqrfdqyphqlsGGMKQRV 162
Cdd:cd03217 75 A--RLG--IFLAFQ------YPPEIPGVKNADFLR-------------YVN----EGFS--------------GGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAE-RADRIMVFRQGEIQEQG 236
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYiKPDRVHVLYDGRIVKSG 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-241 |
1.19e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.62 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 37 AFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDwSDKRLN-----RlrgvSISLVPQDpgNSLNPVKTigqq 111
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGL----TRPQKGRIVLNGRVLFD-AEKGIClppekR----RIGYVFQD--ARLFPHYK---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 112 VEEILRLHQSLSAAERRQQVLNLLakvGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKR 191
Cdd:PRK11144 93 VRGNLRYGMAKSMVAQFDKIVALL---GIEP---LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1031820327 192 ILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETI 241
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
274-508 |
1.22e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 85.52 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQ-VTIDGIDAGhlsREAQ 352
Cdd:COG1119 1 DPLLELRNVT--VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRG---GEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQNPFASLDPRQRLFAIIeeplknferLSAAT------------RRQRVESVAARVALApELLSRTPREL 420
Cdd:COG1119 74 WELRKRIGLVSPALQLRFPRDETVLDVV---------LSGFFdsiglyreptdeQRERARELLELLGLA-HLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 421 SGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLAtvrRIADSVT---VLRAGQ 497
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE---EIPPGIThvlLLKDGR 220
|
250
....*....|.
gi 1031820327 498 VVEHGDVNRLF 508
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-218 |
1.23e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRIsYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIiglladnarrdAGrivlngevISDWSDKRL 83
Cdd:COG4178 363 LALEDLTL-RTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-----------AG--------LWPYGSGRI 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSISLVPQDP----GNslnpvktigqqveeilrLHQSLS---AAER--RQQVLNLLAKVGLSHPEQRFDQ---YP 151
Cdd:COG4178 421 ARPAGARVLFLPQRPylplGT-----------------LREALLypaTAEAfsDAELREALEAVGLGHLAERLDEeadWD 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLdiLRRESGTAVLFVTHDLALAA 218
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAA 548
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-236 |
1.60e-18 |
|
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: 88.72 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLAdnarR----DAGRIVLNGEVISDWSDKR 82
Cdd:COG5265 361 ENVSFGYDPE---RPILKGVSFEVPAGKTVAIVGPSGAGKST----LARLLF----RfydvTSGRILIDGQDIRDVTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRlrgvSISLVPQDPgnslnpV---KTIGQQV---------EEILrlhqslsAAERRQQVLNLLAKV-----------G 139
Cdd:COG5265 430 LRA----AIGIVPQDT------VlfnDTIAYNIaygrpdaseEEVE-------AAARAAQIHDFIESLpdgydtrvgerG 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 140 LshpeqrfdqyphQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALAAe 219
Cdd:COG5265 493 L------------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIV- 557
|
250
....*....|....*..
gi 1031820327 220 RADRIMVFRQGEIQEQG 236
Cdd:COG5265 558 DADEILVLEAGRIVERG 574
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
287-536 |
1.79e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 287 SLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTL----ARILLGFeradAGQVTIDGIDAGHLSreaQRQLRRKIQFV 362
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLlkcfARLLTPQ----SGTVFLGDKPISMLS---SRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 363 YQNPfasLDPR----QRLFAIIEEP-LKNFERLSAATRrQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILE 437
Cdd:PRK11231 82 PQHH---LTPEgitvRELVAYGRSPwLSLWGRLSAEDN-ARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 438 PAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGdvnrlfaAPQQAYTR 517
Cdd:PRK11231 157 TPVVLLDEPTTYLDIN-HQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTP 228
|
250
....*....|....*....
gi 1031820327 518 ELIAaipQVSSRLAQAHTE 536
Cdd:PRK11231 229 GLLR---TVFDVEAEIHPE 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
266-502 |
2.05e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 266 AARHRPLATPAIRVEGISKrfSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG 345
Cdd:PRK13536 31 ASIPGSMSTVAIDLAGVSK--SYGDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 346 HLSREAqrqlRRKIQFVYQnpFASLDPRqrlfAIIEEPLKNFERLSAATRRQ------------RVESVA-ARVAlapel 412
Cdd:PRK13536 107 ARARLA----RARIGVVPQ--FDNLDLE----FTVRENLLVFGRYFGMSTREieavipsllefaRLESKAdARVS----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 413 lsrtprELSGGQRQRVAIARALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTV 492
Cdd:PRK13536 172 ------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCV 244
|
250
....*....|
gi 1031820327 493 LRAGQVVEHG 502
Cdd:PRK13536 245 LEAGRKIAEG 254
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
296-496 |
3.64e-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: 83.67 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsREAQRQLRRKIqFVYQNpfASLDP--- 372
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRM-VVFQN--YSLLPwlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 373 -RQRLFAIIEEPLKNferLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:TIGR01184 71 vRENIALAVDRVLPD---LSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1031820327 452 VTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAG 496
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
274-451 |
4.75e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQR 353
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 QLRRK-IQFVYQ--NPFASLDPRQRlfaiIEEPlKNFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAI 430
Cdd:PRK10535 82 QLRREhFGFIFQryHLLSHLTAAQN----VEVP-AVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSI 155
|
170 180
....*....|....*....|.
gi 1031820327 431 ARALILEPAILVLDEATSALD 451
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALD 176
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-452 |
4.75e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.17 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 30 IQRGEMLAFVGESGSGKTTTAQAIiglladnarrdAGRIVLN-GEVIS--DWsDKRLNRLRGVSIslvpQD-----PGNS 101
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-----------SGELIPNlGDYEEepSW-DEVLKRFRGTEL----QNyfkklYNGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPVKTIgQQVEEILRL-----HQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLII 176
Cdd:PRK13409 160 IKVVHKP-QYVDLIPKVfkgkvRELLKKVDERGKLDEVVERLGLEN---ILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 177 ADEPTSALDV----TVQKRILDLLDilrresGTAVLFVTHDLALAAERADRIMVFrQGEIQEQGatetIVQRPQHP---- 248
Cdd:PRK13409 236 FDEPTSYLDIrqrlNVARLIRELAE------GKYVLVVEHDLAVLDYLADNVHIA-YGEPGAYG----VVSKPKGVrvgi 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 249 --YTRQLLHD----LQDAPLGLTAARHRPLATPAIRVE--GISKR---FSlgkqalqaLDSVSFEVRRGSTHALVGESGS 317
Cdd:PRK13409 305 neYLKGYLPEenmrIRPEPIEFEERPPRDESERETLVEypDLTKKlgdFS--------LEVEGGEIYEGEVIGIVGPNGI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 318 GKTTLARILLGFERADAGQVTIDgidaghlsreaqrqlrRKIqfvyqnpfaSLDPrQRLFAIIEEPLKNFerLSAATRR- 396
Cdd:PRK13409 377 GKTTFAKLLAGVLKPDEGEVDPE----------------LKI---------SYKP-QYIKPDYDGTVEDL--LRSITDDl 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 397 ----QRVEsVAARVALaPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK13409 429 gssyYKSE-IIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-234 |
5.19e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGllADnaRRDAGRIVLNGEVISDWSDkrLNRLRGvSISLVPQD-- 97
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VD--KRAGGEIRLNGKDISPRSP--LDAVKK-GMAYITESrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 -----PGNSLNPVKTIGQQVEE--------ILRLHQSLSAAERRQQVLNLLAkvglshpeQRFDQYPHQLSGGMKQRVLI 164
Cdd:PRK09700 349 dngffPNFSIAQNMAISRSLKDggykgamgLFHEVDEQRTAENQRELLALKC--------HSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 165 AIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQE 234
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-231 |
6.33e-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: 82.13 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWRE-VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGevisdwsdkr 82
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGEL----EKLSGSVSVPG---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 lnrlrgvSISLVPQDP-------------GNSLNPvktigqqveeilrlhqslsaaERRQQVLNLLAkvgLshpEQRFDQ 149
Cdd:cd03250 67 -------SIAYVSQEPwiqngtirenilfGKPFDE---------------------ERYEKVIKACA---L---EPDLEI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 150 YPHQ-----------LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILD--LLDILRResGTAVLFVTHDLAL 216
Cdd:cd03250 113 LPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQL 190
|
250
....*....|....*
gi 1031820327 217 aAERADRIMVFRQGE 231
Cdd:cd03250 191 -LPHADQIVVLDNGR 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-240 |
6.67e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISdwsdkrl 83
Cdd:PRK15056 7 IVVNDVTVTWRNG---HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPTR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSISLVPQDPGNSLN-PVktigqQVEEILRL----HQSL---SAAERRQQVLNLLAKVGLShpEQRFDQYpHQLS 155
Cdd:PRK15056 73 QALQKNLVAYVPQSEEVDWSfPV-----LVEDVVMMgrygHMGWlrrAKKRDRQIVTAALARVDMV--EFRHRQI-GELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERAD-RIMVfrQGEIQE 234
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDyTVMV--KGTVLA 221
|
....*.
gi 1031820327 235 QGATET 240
Cdd:PRK15056 222 SGPTET 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-185 |
8.91e-18 |
|
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: 82.32 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLaDNARRDAGRIVLNGEVISDWSDKR 82
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 lnrlrgvSISLVPQDpgNSLNPVKTigqqVEE------ILRLHQSLSAAERRQQVlnllAKVGLSH--PEQRFDQYPHQL 154
Cdd:cd03234 82 -------CVAYVRQD--DILLPGLT----VREtltytaILRLPRKSSDAIRKKRV----EDVLLRDlaLTRIGGNLVKGI 144
|
170 180 190
....*....|....*....|....*....|.
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALD 185
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-238 |
9.72e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 81.83 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 27 SFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDKRLnrlrgvSISLVPQDpgNSLNPVK 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPAS----GSIKVNDQSHTGLAPYQR------PVSMLFQE--NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 107 TIGQQVEeiLRLHQSLS-AAERRQQVLNLLAKVGLShpeQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALD 185
Cdd:TIGR01277 86 TVRQNIG--LGLHPGLKlNAEQQEKVVDAAQQVGIA---DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 186 VTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGAT 238
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-247 |
1.21e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.95 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLL----ADNARRDAGRIVLNGEVISDW 78
Cdd:PRK13547 1 MLTADHLHVARRHR----AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 79 SDKRLNRLRGVsislVPQ--DPGNSLNpvktigqqVEEILRL----HQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPH 152
Cdd:PRK13547 77 DAPRLARLRAV----LPQaaQPAFAFS--------AREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIA-LQPD--------LIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADR 223
Cdd:PRK13547 145 TLSGGELARVQFARVLAqLWPPhdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADR 224
|
250 260
....*....|....*....|....
gi 1031820327 224 IMVFRQGEIQEQGATETiVQRPQH 247
Cdd:PRK13547 225 IAMLADGAIVAHGAPAD-VLTPAH 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-452 |
1.37e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 86.16 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTtaqaiigLLAdnarrdagriVLNGEVISDwsDKRLNRLRGVSISLVPQDP-----G 99
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKST-------LMK----------ILNGEVLLD--DGRIIYEQDLIVARLQQDPprnveG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPV-KTIGQQVEEILRLHQ--SLSAAERRQQVLNLLAKV-------GLSHPEQRFDQYPHQ-----------LSGGM 158
Cdd:PRK11147 82 TVYDFVaEGIEEQAEYLKRYHDisHLVETDPSEKNLNELAKLqeqldhhNLWQLENRINEVLAQlgldpdaalssLSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 159 KQRVLIAIAIALQPDLIIADEPTSALDVTVqkrILDLLDILRRESGtAVLFVTHDLALAAERADRIMVFRQGEiqeqgat 238
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQG-SIIFISHDRSFIRNMATRIVDLDRGK------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 239 etIVQRPQHpYTRQLL--------HDLQDAPL-------------GLTAARHRP----LATPAIRVEGISKRFSLGKQAL 293
Cdd:PRK11147 231 --LVSYPGN-YDQYLLekeealrvEELQNAEFdrklaqeevwirqGIKARRTRNegrvRALKALRRERSERREVMGTAKM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSV-------------------------SFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDgidaghls 348
Cdd:PRK11147 308 QVEEASrsgkivfemenvnyqidgkqlvkdfSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 349 reaqrqlrRKIQFVYQNPF-ASLDPRQrlfaIIEEPLknferlsaATRRQRVEsVAARVA---------LAPELLSRTP- 417
Cdd:PRK11147 380 --------TKLEVAYFDQHrAELDPEK----TVMDNL--------AEGKQEVM-VNGRPRhvlgylqdfLFHPKRAMTPv 438
|
490 500 510
....*....|....*....|....*....|....*.
gi 1031820327 418 RELSGGQRQRVAIARaLILEPA-ILVLDEATSALDV 452
Cdd:PRK11147 439 KALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDV 473
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-502 |
1.62e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.42 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALQ------------------ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVT 338
Cdd:cd03220 1 IELENVSKSYPTYKGGSSslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 339 IDG-----IDAGH-----LS-RE-----------AQRQLRRKIQFVYQnpFASLDprqrlfAIIEEPLKNFerlsaatrr 396
Cdd:cd03220 81 VRGrvsslLGLGGgfnpeLTgREniylngrllglSRKEIDEKIDEIIE--FSELG------DFIDLPVKTY--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 397 qrvesvaarvalapellsrtprelSGGQRQRVAIARALILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFI 476
Cdd:cd03220 144 ------------------------SSGMKARLAFAIATALEPDILLIDEVLAVGDAAF-QEKCQRRLRELLKQGKTVILV 198
|
250 260
....*....|....*....|....*.
gi 1031820327 477 THDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:cd03220 199 SHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-241 |
1.70e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRisyrsrgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVISDWSDK 81
Cdd:PRK15439 267 PVLTVEDLT---------GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG----GRIMLNGKEINALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 rlNRLRgVSISLVPQDPGNS---------LNPVKTIGQQVEEILRLHQSLSAAERRQQVLNllakVGLSHPEQRFdqypH 152
Cdd:PRK15439 334 --QRLA-RGLVYLPEDRQSSglyldaplaWNVCALTHNRRGFWIKPARENAVLERYRRALN----IKFNHAEQAA----R 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKrilDLLDILRR--ESGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN---DIYQLIRSiaAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
250
....*....|.
gi 1031820327 231 EIQEQGATETI 241
Cdd:PRK15439 480 EISGALTGAAI 490
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-245 |
2.43e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSD 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL----ERITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRlnrlRGvsISLVPQdpgN-SLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMK 159
Cdd:PRK11650 74 AD----RD--IAMVFQ---NyALYPHMSVRENMAYGLKI-RGMPKAEIEERVAEAARILEL---EPLLDRKPRELSGGQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALD--VTVQKRildlLDI--LRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQ 235
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDakLRVQMR----LEIqrLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQI 216
|
250
....*....|
gi 1031820327 236 GATETIVQRP 245
Cdd:PRK11650 217 GTPVEVYEKP 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
294-520 |
2.44e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLAR-----ILLGFERADAGQVTIDGIDAGHLSREAQRqLRRKIQFVYQ--NP 366
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQypNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FasldPRQRLFAIIEEPLK-NFERLSAATRRQRVESVAARVALAPELLSRT---PRELSGGQRQRVAIARALILEPAILV 442
Cdd:PRK14267 97 F----PHLTIYDNVAIGVKlNGLVKSKKELDERVEWALKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 443 LDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELI 520
Cdd:PRK14267 173 MDEPTANIDPV--GTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
310-512 |
2.48e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.39 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 310 ALVGESGSGKTTLARILLGFERADAGQVTIDGidagHLSREAQRQL-----RRKIQFVYQNpfASLDPRQRLfaiieepL 384
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNG----RVLFDAEKGIclppeKRRIGYVFQD--ARLFPHYKV-------R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 385 KNFERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQ 464
Cdd:PRK11144 95 GNLRYGMAKSMVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1031820327 465 LQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFAAPQ 512
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
279-498 |
3.10e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.65 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 279 VEGISKRFSlGKQALQALDsvsFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTidgidAGhlsREAQRQLRRK 358
Cdd:PRK11247 15 LNAVSKRYG-ERTVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AG---TAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 359 IQFVYQNpfASLDPRQRLFAIIEEPLKNFERLSAatrRQRVESVAarvalapeLLSRT---PRELSGGQRQRVAIARALI 435
Cdd:PRK11247 83 TRLMFQD--ARLLPWKKVIDNVGLGLKGQWRDAA---LQALAAVG--------LADRAnewPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 436 LEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQV 498
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-239 |
3.17e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.60 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAgRIVLNGEVIsdwsdK 81
Cdd:PRK09984 3 TIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGS-HIELLGRTV-----Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGvsislvpqDPGNSLNPVKTIGQQ---VEEILRLHQSLSAA----------------ERRQQVLNLLAKVGLSH 142
Cdd:PRK09984 73 REGRLAR--------DIRKSRANTGYIFQQfnlVNRLSVLENVLIGAlgstpfwrtcfswftrEQKQRALQALTRVGMVH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 143 peqrfdqYPHQ----LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAA 218
Cdd:PRK09984 145 -------FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL 217
|
250 260
....*....|....*....|.
gi 1031820327 219 ERADRIMVFRQGEIQEQGATE 239
Cdd:PRK09984 218 RYCERIVALRQGHVFYDGSSQ 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
287-451 |
3.58e-17 |
|
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: 79.90 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 287 SLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLG--FERADAGQVTIDGIDAGhlsreaQRQLRRKIQFVYQ 364
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLD------KRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 365 NP--FASLDPRQRLfaiieeplknferlsaatrrqrveSVAARValapellsrtpRELSGGQRQRVAIARALILEPAILV 442
Cdd:cd03213 90 DDilHPTLTVRETL------------------------MFAAKL-----------RGLSGGERKRVSIALELVSNPSLLF 134
|
....*....
gi 1031820327 443 LDEATSALD 451
Cdd:cd03213 135 LDEPTSGLD 143
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-252 |
3.95e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAI--IGLLADNARRDaGRIVLNGEVISDwsdK 81
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVE-GRVEFFNQNIYE---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 R--LNRLRGvSISLVPQDPG--------NSLNPVKTIG--QQVEEILRLHQSLSAAERRQQVLNLLAKVGLshpeqrfdq 149
Cdd:PRK14258 80 RvnLNRLRR-QVSMVHPKPNlfpmsvydNVAYGVKIVGwrPKLEIDDIVESALKDADLWDEIKHKIHKSAL--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 150 yphQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVF-- 227
Cdd:PRK14258 150 ---DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkg 226
|
250 260
....*....|....*....|....*...
gi 1031820327 228 ---RQGEIQEQGATETIVQRPQHPYTRQ 252
Cdd:PRK14258 227 nenRIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-214 |
4.90e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.95 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRL 83
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP----LQGEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrgvsISLVPQDPgnslnpvKTIGQQVEEILRLHQSLSAAErrqQVLNLLAKVGL-SHPEQRFDQYPH-------QLS 155
Cdd:TIGR02868 408 RRR----VSVCAQDA-------HLFDTTVRENLRLARPDATDE---ELWAALERVGLaDWLRALPDGLDTvlgeggaRLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDllDILRRESGTAVLFVTHDL 214
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLE--DLLAALSGRTVVLITHHL 530
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-231 |
5.34e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISyrsRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEvisdwsDKR 82
Cdd:PRK13539 2 MLEGEDLACV---RGG-RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL----PPAAGTIKLDGG------DID 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGVSISLVPQdpgNSLNPVKTigqqVEEILRLHQSLSAAERRqQVLNLLAKVGLSHPEQRFDQYphqLSGGMKQRV 162
Cdd:PRK13539 68 DPDVAEACHYLGHR---NAMKPALT----VAENLEFWAAFLGGEEL-DIAAALEAVGLAPLAHLPFGY---LSAGQKRRV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDIlRRESGTAVLFVTH-DLALAAERADRIMVFRQGE 231
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGLPGARELDLGPFAAED 205
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-232 |
5.64e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.31 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSDKRLNRlrgVSISLVPQdpgn 100
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLCGDPRATSGRIVFDGKDITDWQTAKIMR---EAVAIVPE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 slnpvktiGQQVEEILRLHQSLSAA---ERRQQVLNLLAKVGLSHPE--QRFDQYPHQLSGGMKQRVLIAIAIALQPDLI 175
Cdd:PRK11614 88 --------GRRVFSRMTVEENLAMGgffAERDQFQERIKWVYELFPRlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 176 IADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-232 |
5.67e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRlnrlRGVSISLVPQDP- 98
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSL----PPDSGSILIDGKDVTKLPEYK----RAKYIGRVFQDPm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 -GNSlnPVKTIgqqvEEILRL------HQSLSAA---ERRQQVLNLLAKVGLSHpEQRFDQYPHQLSGGMKQRVLIAIAI 168
Cdd:COG1101 91 mGTA--PSMTI----EENLALayrrgkRRGLRRGltkKRRELFRELLATLGLGL-ENRLDTKVGLLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 169 ALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-258 |
7.14e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.53 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 24 HNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWsdkRLNRLRGvSISLVPQDPgNSLN 103
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDIDEGEILLDGHDLRDY---TLASLRN-QVALVSQNV-HLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 104 pvKTIG-------------QQVEEILRLHQSLSAAERRQQVLN-LLAKVGLShpeqrfdqyphqLSGGMKQRvlIAIAIA 169
Cdd:PRK11176 431 --DTIAnniayarteqysrEQIEEAARMAYAMDFINKMDNGLDtVIGENGVL------------LSGGQRQR--IAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 170 LQPD--LIIADEPTSALDVTVQKRILDLLDILRRESgtAVLFVTHDLAlAAERADRIMVFRQGEIQEQGATETIVQRpQH 247
Cdd:PRK11176 495 LLRDspILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELLAQ-NG 570
|
250
....*....|.
gi 1031820327 248 PYTRqlLHDLQ 258
Cdd:PRK11176 571 VYAQ--LHKMQ 579
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
291-509 |
7.37e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 291 QALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGiDAGHLSREAQRQLRRKIQFVYQnpfasl 370
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALRQQVATVFQ------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 371 DPRQRLF-----AIIEEPLKNFERLSAATRRqRVESvAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:PRK13638 85 DPEQQIFytdidSDIAFSLRNLGVPEAEITR-RVDE-ALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 446 ATSALDvTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:PRK13638 163 PTAGLD-PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
296-451 |
7.98e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.76 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQlrrKIQFVYQNPfasldprqr 375
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSYCAQTP--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 376 lfAIIEEPLKNFERLSAATRRQRVESVA-----ARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:PRK10247 91 --TLFGDTVYDNLIFPWQIRNQQPDPAIflddlERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
.
gi 1031820327 451 D 451
Cdd:PRK10247 169 D 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-237 |
9.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.82 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDK--RLNRLRGvSISLVPQDPGN 100
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS----ETGQTIVGDYAIPANLKKikEVKRLRK-EIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 101 SLNPvKTIGQQVEeILRLHQSLSAAERRQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEP 180
Cdd:PRK13645 102 QLFQ-ETIEKDIA-FGPVNLGENKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 181 TSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-509 |
9.33e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISK-----------------RFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVT 338
Cdd:COG4586 1 IIEVENLSKtyrvyekepglkgalkgLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 339 IDGIDAghlSREaQRQLRRKIQFVYQNpfasldpRQRLF---AIIE--EPLKNFERLSAATRRQRVESVAARVALApELL 413
Cdd:COG4586 81 VLGYVP---FKR-RKEFARRIGVVFGQ-------RSQLWwdlPAIDsfRLLKAIYRIPDAEYKKRLDELVELLDLG-ELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 414 SRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
250
....*....|....*.
gi 1031820327 494 RAGQVVEHGDVNRLFA 509
Cdd:COG4586 229 DHGRIIYDGSLEELKE 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-451 |
9.61e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.13 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQ-ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSrEAQRQl 355
Cdd:COG1101 2 LELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 rRKIQFVYQNPFASLDPRqrlfAIIEEplkNferLSAATRRQRVESV-----AARVALAPELLSR----------TPRE- 419
Cdd:COG1101 80 -KYIGRVFQDPMMGTAPS----MTIEE---N---LALAYRRGKRRGLrrgltKKRRELFRELLATlglglenrldTKVGl 148
|
170 180 190
....*....|....*....|....*....|..
gi 1031820327 420 LSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
295-510 |
1.12e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.74 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSreAQRQLrrkiqfVYQNpfASLDPRQ 374
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG--AERGV------VFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAIIEEPLKnFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTV 454
Cdd:PRK11248 86 NVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 455 QAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLR--AGQVVEH--GDVNRLFAA 510
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERlpLNFARRFVA 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
293-451 |
1.17e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 79.24 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 293 LQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA---GQVTIDGidaghlsREAQRQL-RRKIQFVYQNPF- 367
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG-------QPRKPDQfQKCVAYVRQDDIl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 368 -ASLDPRQRLFAIIeePLKNFERLSAATRRQRVESVAAR-VALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:cd03234 93 lPGLTVRETLTYTA--ILRLPRKSSDAIRKKRVEDVLLRdLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
....*.
gi 1031820327 446 ATSALD 451
Cdd:cd03234 170 PTSGLD 175
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
296-451 |
1.44e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.79 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAD---AGQVTIDGIDAGhlsreaQRQLRRKIQFVYQNP--FASL 370
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID------AKEMRAISAYVQQDDlfIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 371 DPRQRLfaIIEEPLKNFERLSAATRRQRVESVAARVALAP--ELLSRTP---RELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:TIGR00955 115 TVREHL--MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcaNTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
....*.
gi 1031820327 446 ATSALD 451
Cdd:TIGR00955 193 PTSGLD 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
275-452 |
1.71e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 77.47 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 275 PAIRVEGISKRfslgkqalQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLS-REAqr 353
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 qLRRKIQFVyqnpfasldPRQRL-FAIIEEplknferlsaatrrqrvESVAARVALapellsrtPRELSGGQRQRVAIAR 432
Cdd:cd03215 73 -IRAGIAYV---------PEDRKrEGLVLD-----------------LSVAENIAL--------SSLLSGGNQQKVVLAR 117
|
170 180
....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALDV 452
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDV 137
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-233 |
1.81e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarRDAGRIVLNGEVISDWSDKRLNRLrgvSISLVPQD-P 98
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG---RWEGEIFIDGKPVKIRNPQQAIAQ---GIAMVPEDrK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 GNSLNPVKTIGQ--------QVEEILRLHQSLSAAERRQQVLNLlaKVGLSHPEQRFDqyphQLSGGMKQRVLIAIAIAL 170
Cdd:PRK13549 349 RDGIVPVMGVGKnitlaaldRFTGGSRIDDAAELKTILESIQRL--KVKTASPELAIA----RLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 171 QPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQ 233
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-243 |
2.03e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDaGRIVLNGEVISDWsdkrlnRLRGVSiSLVPQDpg 99
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS-GSVLLNGMPIDAK------EMRAIS-AYVQQD-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQ--VEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRFDQYPHQ---LSGGMKQRVLIAIAIALQPDL 174
Cdd:TIGR00955 108 DLFIPTLTVREHlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 175 IIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTH----DLalaAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHqpssEL---FELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-243 |
2.62e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDPGNSL-- 102
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL----QPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLfe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 -NPVKTI--GQQVEEILRLHQSLSAAERrqqvlnlLAKVGLShpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:PRK13643 100 eTVLKDVafGPQNFGIPKEKAEKIAAEK-------LEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 180 PTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVQ 243
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
289-524 |
3.14e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 289 GKQALQALdSVSFEVrrGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAqrqLRRKIQFVYQN-PF 367
Cdd:PRK10575 23 GRTLLHPL-SLTFPA--GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKVAYLPQQlPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 368 ASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:PRK10575 97 AEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 448 SALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVNRLFaapqQAYTRELIAAIP 524
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM----RGETLEQIYGIP 248
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-220 |
3.93e-16 |
|
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: 77.01 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISyrsRGeWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISdwsdkRL 83
Cdd:TIGR01189 1 LAARNLACS---RG-ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPLA-----EQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSISLVPQDPGnsLNPVKTigqqVEEILRLHQSLSAAERRqQVLNLLAKVGLSHPEQRFdqyPHQLSGGMKQRVL 163
Cdd:TIGR01189 68 RDEPHENILYLGHLPG--LKPELS----ALENLHFWAAIHGGAQR-TIEDALAAVGLTGFEDLP---AAQLSAGQQRRLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAER 220
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEAR 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
295-493 |
4.19e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqrqlRRKIQFVYQNpfaSLDPRq 374
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------------GARVAYVPQR---SEVPD- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAIIEE--------PLKNFERLSAATRRqRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:NF040873 69 SLPLTVRDlvamgrwaRRGLWRRLTRDDRA-AVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1031820327 447 TSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVL 493
Cdd:NF040873 147 TTGLDAE-SRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-213 |
4.47e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.45 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISDWSDKRLNRlrgvSISLVPQDPG 99
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP----TSGTLLFEGEDISTLKPEIYRQ----QVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 --------NSLNPVKTIGQQVEEilrlhqslsaaerrQQVLNLLAKVGLshPEQRFDQYPHQLSGGMKQRVLIAIAIALQ 171
Cdd:PRK10247 92 lfgdtvydNLIFPWQIRNQQPDP--------------AIFLDDLERFAL--PDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1031820327 172 PDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHD 213
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
272-510 |
4.59e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 272 LATPAIRVEGISKRFSLGKQALQaldSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIdgidaghLSREA 351
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-------LGQPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQLRRK-IQFVYQNPFASLDprqrlFAIIEEPL--------KNFERLSAATRRQRVESVAARVALApELLSRTPRELSG 422
Cdd:PRK15056 72 RQALQKNlVAYVPQSEEVDWS-----FPVLVEDVvmmgryghMGWLRRAKKRDRQIVTAALARVDMV-EFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADsVTVLRAGQVVEHG 502
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKT-EARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
....*...
gi 1031820327 503 DVNRLFAA 510
Cdd:PRK15056 224 PTETTFTA 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
284-523 |
5.34e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 284 KRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaGHLSREAQRQLRRKIQFVY 363
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG---EHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 364 QNPFASLD-PRQRLFAIIEEPlknFERLSAATRRQRVESVAA--RVALAPELLSRTPRELSGGQRQRVAIARALILEPAI 440
Cdd:PRK10253 88 QNATTPGDiTVQELVARGRYP---HQPLFTRWRKEDEEAVTKamQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 441 LVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGdvnrlfaAPQQAYTRELI 520
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELI 237
|
...
gi 1031820327 521 AAI 523
Cdd:PRK10253 238 ERI 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-452 |
5.43e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnARRDAGRIVLNGEVISdWSDKRLNRLRGVSI-----SLVPQdpg 99
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGSYEGEILFDGEVCR-FKDIRDSEALGIVIihqelALIPY--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nsL---------NPVKTIGqqveeILRLHQSLSAAERrqqvlnLLAKVGLS-HPEQRFDQyphqLSGGMKQRVLIAIAIA 169
Cdd:NF040905 93 --LsiaeniflgNERAKRG-----VIDWNETNRRARE------LLAKVGLDeSPDTLVTD----IGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 170 LQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLALAAERADRIMVFRQGEiqeqgATETIvqrpqhpy 249
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGR-----TIETL-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 250 trqllhDLQDAPlgLTAAR-----------HR-PLATPAI-----RVEGISKRFSLgKQALQALDSVSFEVRRGSTHALV 312
Cdd:NF040905 222 ------DCRADE--VTEDRiirgmvgrdleDRyPERTPKIgevvfEVKNWTVYHPL-HPERKVVDDVSLNVRRGEIVGIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 313 GESGSGKTTLARILLG--FERADAGQVTIDG--IDAghlsREAQRQLRRKIQFVYQNpfasldpRQRLFAIIEEPLKN-- 386
Cdd:NF040905 293 GLMGAGRTELAMSVFGrsYGRNISGTVFKDGkeVDV----STVSDAIDAGLAYVTED-------RKGYGLNLIDDIKRni 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 387 -FERLSAATRR----QRVESVAA---RVAL---APELLSRTPReLSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:NF040905 362 tLANLGKVSRRgvidENEEIKVAeeyRKKMnikTPSVFQKVGN-LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-230 |
6.31e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 14 RSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnaRRDAGRIVLngevisdwsdkrlnrlrgvsisl 93
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG--TPVAGCVDV----------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 vpqdPGNSLNPVKTIgqqVEEILRLHQSLSAAErrqqvlnLLAKVGLSHPeQRFDQYPHQLSGGMKQRVLIAIAIALQPD 173
Cdd:COG2401 92 ----PDNQFGREASL---IDAIGRKGDFKDAVE-------LLNAVGLSDA-VLWLRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 174 LIIADEPTSALDVTVQKRI-LDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVaRNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGYG 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-236 |
6.81e-16 |
|
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: 81.60 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVIsdwsDKRLNRLRGvSISLVPQDpg 99
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTS----GTVLVGGKDI----ETNLDAVRQ-SLGMCPQH-- 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHpeqRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHH---KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 180 PTSALDVTVQKRILDLLdiLRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQG 236
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-237 |
6.95e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIsDWSDKR 82
Cdd:PRK13638 1 MLATSDLWFRYQDE----PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGKPL-DYSKRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDPGNSLN----------PVKTIGQQVEEILRlhqslsaaeRRQQVLNLLakvglshPEQRFDQYPH 152
Cdd:PRK13638 72 LLALRQ-QVATVFQDPEQQIFytdidsdiafSLRNLGVPEAEITR---------RVDEALTLV-------DAQHFRHQPI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 Q-LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRildLLDILRR--ESGTAVLFVTHDLALAAERADRIMVFRQ 229
Cdd:PRK13638 135 QcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ---MIAIIRRivAQGNHVIISSHDIDLIYEISDAVYVLRQ 211
|
....*...
gi 1031820327 230 GEIQEQGA 237
Cdd:PRK13638 212 GQILTHGA 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-236 |
7.06e-16 |
|
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: 76.30 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEvisDWSDKRL 83
Cdd:cd03369 7 IEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGI---DISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDP----GNSLNPVKTIGQQVEEilRLHQSLSAAERrqqvlnllakvGLShpeqrfdqyphqLSGGMK 159
Cdd:cd03369 78 EDLRS-SLTIIPQDPtlfsGTIRSNLDPFDEYSDE--EIYGALRVSEG-----------GLN------------LSQGQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 160 QRVLIAIAIALQPDLIIADEPTSALDVTVQKRIldlLDILRRE-SGTAVLFVTHDLALAAErADRIMVFRQGEIQEQG 236
Cdd:cd03369 132 QLLCLARALLKRPRVLVLDEATASIDYATDALI---QKTIREEfTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-231 |
7.26e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.41 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdagrivlnGEVISDwsdkrl 83
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE----------GIVTWG------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlRGVSISLVPQdpgnslnpvktigqqveeilrlhqslsaaerrqqvlnllakvglshpeqrfdqyphqLSGGMKQRVL 163
Cdd:cd03221 61 ---STVKIGYFEQ---------------------------------------------------------LSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 164 IAIAIALQPDLIIADEPTSALDV-TVQKrildLLDILRRESGTaVLFVTHDLALAAERADRIMVFRQGE 231
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLeSIEA----LEEALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-237 |
8.40e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 9 LRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnarrdagRIVLNGEVISDwsDKRLNRL-- 86
Cdd:PRK11000 6 LRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL----------EDITSGDLFIG--EKRMNDVpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 --RGVSisLVPQDpgNSLNPVKTIGQQVEEILRLhQSLSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLI 164
Cdd:PRK11000 73 aeRGVG--MVFQS--YALYPHLSVAENMSFGLKL-AGAKKEEINQRVNQVAEVLQLAHLLDR---KPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 165 AIAIALQPDLIIADEPTSALD--VTVQKRIldllDI--LRRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGA 237
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDaaLRVQMRI----EIsrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-233 |
9.18e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarRDAGRIVLNGEVISDWSDKRLNRlrgVSISLVPQD-P 98
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG---KFEGNVFINGKPVDIRNPAQAIR---AGIAMVPEDrK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 GNSLNPVKTIGQQVeeILRLHQSLS------AAERRQQVLNLLA--KVGLSHPeqrfDQYPHQLSGGMKQRVLIAIAIAL 170
Cdd:TIGR02633 347 RHGIVPILGVGKNI--TLSVLKSFCfkmridAAAELQIIGSAIQrlKVKTASP----FLPIGRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 171 QPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQ 233
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-520 |
1.00e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 269 HRPLATPAIRVEGISkrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLS 348
Cdd:PRK11160 331 TAAADQVSLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP---IA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 349 REAQRQLRRKIQFVYQNPF---ASLdpRQRLfaIIEEPLKNFERLSAatrrqrvesVAARVALAPELLSRTP-------- 417
Cdd:PRK11160 406 DYSEAALRQAISVVSQRVHlfsATL--RDNL--LLAAPNASDEALIE---------VLQQVGLEKLLEDDKGlnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 418 -RELSGGQRQRVAIARALILEPAILVLDEATSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRIaDSVTVLRAG 496
Cdd:PRK11160 473 gRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET--ERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNG 549
|
250 260
....*....|....*....|....
gi 1031820327 497 QVVEHGDVNRLFAapQQAYTRELI 520
Cdd:PRK11160 550 QIIEQGTHQELLA--QQGRYYQLK 571
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-232 |
1.25e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISDWSdkrlnrlrgvsislvPQD----- 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVTRS---------------PQDglang 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 --------PGNSLnpvkTIGQQVEEILRL---------HQSLSAAERRQQVLNLLAKVGLSHPEQrfDQYPHQLSGGMKQ 160
Cdd:PRK10762 329 ivyisedrKRDGL----VLGMSVKENMSLtalryfsraGGSLKHADEQQAVSDFIRLFNIKTPSM--EQAIGLLSGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
274-493 |
1.41e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVtidgidaghlsreaQR 353
Cdd:PRK09544 2 TSLVSLENVSVSFG----QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 QLRRKIQFVYQNpfASLDPRQRLfaiieePLKNFERLSAATRRQRVESVAARVAlAPELLSRTPRELSGGQRQRVAIARA 433
Cdd:PRK09544 64 NGKLRIGYVPQK--LYLDTTLPL------TVNRFLRLRPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 434 LILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
1.80e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrDAGRIVLNGEVISdwSD 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP----DAGKITVLGVPVP--AR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRgvsISLVPQdpGNSLNPVKTIGQQVEEILRlHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQ 160
Cdd:PRK13536 109 ARLARAR---IGVVPQ--FDNLDLEFTVRENLLVFGR-YFGMSTREIEAVIPSLLEFARL---ESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILD-LLDILRResGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWErLRSLLAR--GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
273-502 |
3.06e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGID-AGHLSREA 351
Cdd:PRK11300 2 SQPLLSVSGLMMRFG----GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 352 QRQ-LRRKIQFVyqnpfasldprqRLF---AIIEEPLKNFER-----------LSAATRRQRVESV--AA----RVALAp 410
Cdd:PRK11300 78 ARMgVVRTFQHV------------RLFremTVIENLLVAQHQqlktglfsgllKTPAFRRAESEALdrAAtwleRVGLL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 411 ELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSV 490
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250
....*....|..
gi 1031820327 491 TVLRAGQVVEHG 502
Cdd:PRK11300 225 YVVNQGTPLANG 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
281-497 |
7.17e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 281 GISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLG------FEradaGQVTIDG--IDAGHLsREAQ 352
Cdd:PRK13549 10 NITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtYE----GEIIFEGeeLQASNI-RDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RqlrRKIQFVYQNpfASLDPR----QRLFaIIEEPLKnFERLSAATRRQRVESVAARVALAPELLSRTpRELSGGQRQRV 428
Cdd:PRK13549 81 R---AGIAIIHQE--LALVKElsvlENIF-LGNEITP-GGIMDYDAMYLRAQKLLAQLKLDINPATPV-GNLGLGQQQLV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 429 AIARALILEPAILVLDEATSAL---DVTVqaqiLALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQ 497
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLtesETAV----LLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-517 |
1.40e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 299 VSFEVRRGSTHALVGESGSGKTTLARILLGF-ERADAGQVTIDGIDAGHLSREAQRQ--------LRRKIQFVYQNPFAS 369
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNEQDYQgdeeqnvgMKNVNEFSLTKEGGS 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 370 ------------------------LDPRQRLFAII-EEP----LKNFERLSAATRRQRVESV--AARVALAPELLSRTP- 417
Cdd:PTZ00265 1267 gedstvfknsgkilldgvdicdynLKDLRNLFSIVsQEPmlfnMSIYENIKFGKEDATREDVkrACKFAAIDEFIESLPn 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 418 ----------RELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRiA 487
Cdd:PTZ00265 1347 kydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
250 260 270
....*....|....*....|....*....|....*
gi 1031820327 488 DSVTVL----RAGQVVE-HGDVNRLFAAPQQAYTR 517
Cdd:PTZ00265 1426 DKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKK 1460
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-230 |
1.94e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 18 EWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARrdAGRIVLNGEVISDWSDKRlnrlrgvsISLVPQD 97
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNF--TGTILANNRKPTKQILKR--------TGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 98 pgNSLNPVKTIGQQVE--EILRLHQSLSAAERRQQVLNLLAKVGLSHPEQRF--DQYPHQLSGGMKQRVLIAIAIALQPD 173
Cdd:PLN03211 149 --DILYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 174 LIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQG 230
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-245 |
2.31e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLrGVsislvpqdpgnsl 102
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY----KPTGGTILLRGQHIEGLPGHQIARM-GV------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 npVKTIgQQVeeilRLHQSLSA------AERRQQVLNLLA------------------------KVGLSHPEQRfdqYPH 152
Cdd:PRK11300 83 --VRTF-QHV----RLFREMTVienllvAQHQQLKTGLFSgllktpafrraesealdraatwleRVGLLEHANR---QAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
250
....*....|...
gi 1031820327 233 QEQGATETIVQRP 245
Cdd:PRK11300 233 LANGTPEEIRNNP 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-452 |
3.10e-14 |
|
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: 75.36 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADnarrdagrivLNGEVisdWSDKrlnrlrGVSISLVPQDPg 99
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD----------FNGEA---RPQP------GIKVGYLPQEP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nSLNPVKTIGQQVEE-------ILRLHQSLSA------------AERRQQVLNLLAKVGLSHPEQRFDQYPH-------- 152
Cdd:TIGR03719 78 -QLDPTKTVRENVEEgvaeikdALDRFNEISAkyaepdadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDalrcppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 ----QLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVtvqKRILDLLDILRRESGTaVLFVTHDLALAAERADRIMVFR 228
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPGT-VVAVTHDRYFLDNVAGWILELD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 229 QGE------------------IQEQGATETIVQRP---------QHPYTRQ------------LLHDLQDAPLGlTAARH 269
Cdd:TIGR03719 233 RGRgipwegnysswleqkqkrLEQEEKEESARQKTlkrelewvrQSPKGRQakskarlaryeeLLSQEFQKRNE-TAEIY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 270 RP----LATPAIRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTI-DGIDA 344
Cdd:TIGR03719 312 IPpgprLGDKVIEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 345 GHL--SREAqrqlrrkiqfvyqnpfasLDPRQRLFAIIEEPLK-----NFERLSaatrRQRVESVAARVALAPELLSrtp 417
Cdd:TIGR03719 388 AYVdqSRDA------------------LDPNKTVWEEISGGLDiiklgKREIPS----RAYVGRFNFKGSDQQKKVG--- 442
|
490 500 510
....*....|....*....|....*....|....*
gi 1031820327 418 rELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:TIGR03719 443 -QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
296-517 |
3.53e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNP--FA----- 368
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD---VAKFGLTDLRRVLSIIPQSPvlFSgtvrf 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 369 SLDPRQRlfaiieeplKNFERLSAATRRQRVESVAARVALAPEL-LSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:PLN03232 1329 NIDPFSE---------HNDADLWEALERAHIKDVIDRNPFGLDAeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 448 SALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFAAPQQAYTR 517
Cdd:PLN03232 1400 ASVDVRT--DSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
296-504 |
3.89e-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: 71.02 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFE--RADAGQVTIDGIDAGHLSREaQRQlRRKIQFVYQNPfasldpr 373
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE-ERA-RLGIFLAFQYP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 qrlfaiIEEP---LKNFERlsaatrrqrveSVAArvalapellsrtprELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:cd03217 87 ------PEIPgvkNADFLR-----------YVNE--------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 451 DVtVQAQILALLQQLQQQLGLSYLFITHdlatVRRI-----ADSVTVLRAGQVVEHGDV 504
Cdd:cd03217 136 DI-DALRLVAEVINKLREEGKSVLIITH----YQRLldyikPDRVHVLYDGRIVKSGDK 189
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-260 |
4.88e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdaGRIVLNGEVISDWSDKRLNRlrgvSISLVPQDPgnsLNP 104
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-----GSLKINGIELRELDPESWRK----HLSWVGQNP---QLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQQVeeilRLHQSLSAAERRQQVLNLlAKV---------GLSHPEQrfDQyPHQLSGGMKQRVLIAIAIALQPDLI 175
Cdd:PRK11174 436 HGTLRDNV----LLGNPDASDEQLQQALEN-AWVseflpllpqGLDTPIG--DQ-AAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 176 IADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQGATETIVQrpQHPYTRQLLH 255
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQ--AGGLFATLLA 582
|
....*
gi 1031820327 256 DLQDA 260
Cdd:PRK11174 583 HRQEE 587
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
296-454 |
5.39e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.88 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVtidgidaghlsreaQRQLRRKIQFVYQNPFasldprqr 375
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------GMPEGEDLLFLPQRPY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 376 lfaiieeplknferLSAATRRqrvesvaarvalapELLSRtP--RELSGGQRQRVAIARALILEPAILVLDEATSALDVT 453
Cdd:cd03223 75 --------------LPLGTLR--------------EQLIY-PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
.
gi 1031820327 454 V 454
Cdd:cd03223 126 S 126
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
281-504 |
5.77e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.06 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 281 GISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLG------FEradaGQVTIDGidaghlsreaqrQ 354
Cdd:NF040905 6 GITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDG------------E 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRkiqfvyqnpFASL-DPRQRLFAIIEEPLKNFERLSAA------------------TRRQRVESVAARVAL--APELL 413
Cdd:NF040905 66 VCR---------FKDIrDSEALGIVIIHQELALIPYLSIAeniflgnerakrgvidwnETNRRARELLAKVGLdeSPDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 414 SRtprELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLfITHDLATVRRIADSVTVL 493
Cdd:NF040905 137 VT---DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVL 212
|
250
....*....|.
gi 1031820327 494 RAGQVVEHGDV 504
Cdd:NF040905 213 RDGRTIETLDC 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-273 |
5.83e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRgewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGlladNARRDAGRIVLNGEVISDWSDKRL 83
Cdd:PRK10790 341 IDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG----YYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRlrgvSISLVPQDP---GNSLNPVKTIGQQVEEilrlHQSLSAAERRQqvlnlLAKVGLSHPE---QRFDQYPHQLSGG 157
Cdd:PRK10790 414 RQ----GVAMVQQDPvvlADTFLANVTLGRDISE----EQVWQALETVQ-----LAELARSLPDglyTPLGEQGNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 158 MKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRREsgTAVLFVTHDLALAAErADRIMVFRQGEIQEQGA 237
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
250 260 270
....*....|....*....|....*....|....*.
gi 1031820327 238 TETIVQRPQHPYTrqlLHDLQDAPLGLTAARHRPLA 273
Cdd:PRK10790 558 HQQLLAAQGRYWQ---MYQLQLAGEELAASVREEES 590
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
299-452 |
1.49e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 299 VSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGiDAGHLSREAQrqlrrkiQFVY---QNPF-ASLDPRQ 374
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-GDIDDPDVAE-------ACHYlghRNAMkPALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 375 RLfaiieeplkNFERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK13539 93 NL---------EFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-227 |
1.57e-13 |
|
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: 73.28 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 29 SIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdagrivlNGEVISDwsdkrlnrlrgVSISLVPQDPGNSlnpvktI 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPD----------EGEVDED-----------LKISYKPQYISPD------Y 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 109 GQQVEEILRLH--QSLSAAERRQQVLNLLakvGLshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDv 186
Cdd:COG1245 415 DGTVEEFLRSAntDDFGSSYYKTEIIKPL---GL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD- 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1031820327 187 tVQKRILdLLDILRR---ESGTAVLFVTHDLALAAERADRIMVF 227
Cdd:COG1245 488 -VEQRLA-VAKAIRRfaeNRGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
296-517 |
1.71e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNP--FA----- 368
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCD---ISKFGLMDLRKVLGIIPQAPvlFSgtvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 369 SLDP-RQRLFAIIEEPLknfER--LSAATRRQRVeSVAARVALAPEllsrtprELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:PLN03130 1332 NLDPfNEHNDADLWESL---ERahLKDVIRRNSL-GLDAEVSEAGE-------NFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 446 ATSALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVrrI-ADSVTVLRAGQVVEHGDVNRLFAAPQQAYTR 517
Cdd:PLN03130 1401 ATAAVD--VRTDALIQKTIREEFKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
278-454 |
2.73e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 278 RVEGISKRF--SLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDgIDAGHLSREAqrql 355
Cdd:COG2401 26 RVAIVLEAFgvELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFGREA---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 rrkiqfvyqnpfasldprqrlfAIIEEPLKNFERLSAatrrqrVEsVAARVALA-PELLSRTPRELSGGQRQRVAIARAL 434
Cdd:COG2401 101 ----------------------SLIDAIGRKGDFKDA------VE-LLNAVGLSdAVLWLRRFKELSTGQKFRFRLALLL 151
|
170 180
....*....|....*....|
gi 1031820327 435 ILEPAILVLDEATSALDVTV 454
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQT 171
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-212 |
2.73e-13 |
|
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: 67.95 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRIsYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnarrdagrivlngevisDWSDKRL 83
Cdd:cd03223 1 IELENLSL-ATPDG--RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-------------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGVSISLVPQDPgnsLNPVKTIgqqveeilrlhqslsaaerRQQVLnllakvglshpeqrfdqYP--HQLSGGMKQR 161
Cdd:cd03223 59 GMPEGEDLLFLPQRP---YLPLGTL-------------------REQLI-----------------YPwdDVLSGGEQQR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLdilrRESGTAVLFVTH 212
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-231 |
2.82e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYrsrGEWREVVHniSFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdagrivlNGEVISDwsdk 81
Cdd:PRK13409 339 TLVEYPDLTKKL---GDFSLEVE--GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD----------EGEVDPE---- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 rlnrlrgVSISLVPQ----DPGNSlnpvktigqqVEEILRlhqslSAAER------RQQVLNLLakvGLshpEQRFDQYP 151
Cdd:PRK13409 400 -------LKISYKPQyikpDYDGT----------VEDLLR-----SITDDlgssyyKSEIIKPL---QL---ERLLDKNV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDV----TVQKRIldlldilRR---ESGTAVLFVTHDLALAAERADRI 224
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAI-------RRiaeEREATALVVDHDIYMIDYISDRL 524
|
....*..
gi 1031820327 225 MVFrQGE 231
Cdd:PRK13409 525 MVF-EGE 530
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-224 |
3.14e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISyrsRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWSDKR 82
Cdd:PRK13538 1 MLEARNLACE---RDE-RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL----ARPDAGEVLWQGEPIRRQRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 ------LNRLRGVSISLVPqdpgnslnpvktigqqvEEILRLHQSLSAAERRQQVLNLLAKVGLshpeQRFDQYP-HQLS 155
Cdd:PRK13538 73 hqdllyLGHQPGIKTELTA-----------------LENLRFYQRLHGPGDDEALWEALAQVGL----AGFEDVPvRQLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 156 GGMKQRVLIA-IAIALQPdLIIADEPTSALDVTVQKRILDLLDiLRRESGTAVLFVTH-DLALAAERADRI 224
Cdd:PRK13538 132 AGQQRRVALArLWLTRAP-LWILDEPFTAIDKQGVARLEALLA-QHAEQGGMVILTTHqDLPVASDKVRKL 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-224 |
4.56e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.29 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 15 SRGeWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNrlrgvSISLV 94
Cdd:cd03231 9 ERD-GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLS----PPLAGRVLLNGGPLDFQRDSIAR-----GLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 95 PQDPGnslnpVKTIgQQVEEILRLHQSLSAaerRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAIALQPDL 174
Cdd:cd03231 79 GHAPG-----IKTT-LSVLENLRFWHADHS---DEQVEEALARVGLNGFE---DRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1031820327 175 IIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRI 224
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
297-452 |
4.67e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 297 DSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLrrkiqfVYQNPFASLDPRqrL 376
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL------LYLGHQPGIKTE--L 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 377 FAiiEEPLKNFERLSAATRRQRVESVAARVALA--PELLSRTpreLSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK13538 90 TA--LENLRFYQRLHGPGDDEALWEALAQVGLAgfEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-239 |
4.78e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.08 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnARRDAGrIVLNGEV-----ISdW 78
Cdd:PLN03130 615 ISIKNGYFSWDSKAE-RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP--PRSDAS-VVIRGTVayvpqVS-W 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 79 ---SDKRLNRLRGVsislvPQDPGnslnpvktigqqveeilRLHQSLSAAERrQQVLNLLAKVGLSHPEQRfdqyPHQLS 155
Cdd:PLN03130 690 ifnATVRDNILFGS-----PFDPE-----------------RYERAIDVTAL-QHDLDLLPGGDLTEIGER----GVNIS 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 156 GGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILD--LLDILRREsgTAVLfVTHDLALAAeRADRIMVFRQGEIQ 233
Cdd:PLN03130 743 GGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK--TRVL-VTNQLHFLS-QVDRIILVHEGMIK 818
|
....*.
gi 1031820327 234 EQGATE 239
Cdd:PLN03130 819 EEGTYE 824
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
254-451 |
6.03e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 254 LHDLQDAplgLTAARHRPLATPAIRVEGiSKRFSLGKQALQA------LDSVSFEVRRGSTHALVGESGSGKTTLARill 327
Cdd:COG4178 335 LAGFEEA---LEAADALPEAASRIETSE-DGALALEDLTLRTpdgrplLEDLSLSLKPGERLLITGPSGSGKSTLLR--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 328 gferadagqvTIDGI---DAGHLSR-EAQRQLrrkiqFVYQNPFasldprqrlfaIIEEPLKN---FERLSAATRRQRVE 400
Cdd:COG4178 408 ----------AIAGLwpyGSGRIARpAGARVL-----FLPQRPY-----------LPLGTLREallYPATAEAFSDAELR 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 401 SVAARVALaPELLSRT------PRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:COG4178 462 EALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
274-507 |
6.15e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAG-------QVTIDGIDAgh 346
Cdd:PRK10762 2 QALLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 347 lSREAqrqlrrKIQFVYQ--NPFASLDPRQRLFaIIEEPLKNFERLSAATRRQRVESVAARVALapellSRTPR----EL 420
Cdd:PRK10762 76 -SQEA------GIGIIHQelNLIPQLTIAENIF-LGREFVNRFGRIDWKKMYAEADKLLARLNL-----RFSSDklvgEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 421 SGGQRQRVAIARALILEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVE 500
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT-ETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
....*..
gi 1031820327 501 HGDVNRL 507
Cdd:PRK10762 222 EREVADL 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
277-502 |
8.31e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGF---ERADAGQVTIDGID---AGHLSRE 350
Cdd:PRK09984 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTvqrEGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 351 AqRQLRRKIQFVYQ--NPFASLDPRQRLF--AIIEEPL-KNFERLSAATRRQRVESVAARVALAPELLSRTpRELSGGQR 425
Cdd:PRK09984 81 I-RKSRANTGYIFQqfNLVNRLSVLENVLigALGSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRV-STLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 426 QRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
290-451 |
9.16e-13 |
|
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: 66.88 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 290 KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGfeRADA----GQVTIDGidaghlsREAQRQLRRKIQFVYQN 365
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILING-------RPLDKNFQRSTGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 366 PFasLDPrqrlFAIIEEPLknfeRLSAATrrqrvesvaarvalapellsrtpRELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:cd03232 88 DV--HSP----NLTVREAL----RFSALL-----------------------RGLSVEQRKRLTIGVELAAKPSILFLDE 134
|
....*.
gi 1031820327 446 ATSALD 451
Cdd:cd03232 135 PTSGLD 140
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
277-453 |
9.19e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVT-IDGIDAGHLSReaqrql 355
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTwGSTVKIGYFEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 rrkiqfvyqnpfasldprqrlfaiieeplknferlsaatrrqrvesvaarvalapellsrtpreLSGGQRQRVAIARALI 435
Cdd:cd03221 71 ----------------------------------------------------------------LSGGEKMRLALAKLLL 86
|
170
....*....|....*...
gi 1031820327 436 LEPAILVLDEATSALDVT 453
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLE 104
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
241-451 |
1.09e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 241 IVQRPQHPYTRqLLHDLQDAPLGLTAARHRPLATPAIRVEgiSKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKT 320
Cdd:PRK10789 279 IVERGSAAYSR-IRAMLAEAPVVKDGSEPVPEGRGELDVN--IRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 321 TLARILLGFERADAGQVTIDGIdagHLSREAQRQLRRKIQFVYQNPFasldprqrLFAiiEEPLKNFERLSAATRRQRVE 400
Cdd:PRK10789 356 TLLSLIQRHFDVSEGDIRFHDI---PLTKLQLDSWRSRLAVVSQTPF--------LFS--DTVANNIALGRPDATQQEIE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 401 SVAaRVALAPELLSRTPR-----------ELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:PRK10789 423 HVA-RLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
293-450 |
1.10e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 293 LQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLsrEAQRQLRRKIqfvyqnpfasldp 372
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMREAV------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 373 rqrlfAIIEEPLKNFERLSA----------ATRRQRVESVAARVALAPELLSRTPRE---LSGGQRQRVAIARALILEPA 439
Cdd:PRK11614 83 -----AIVPEGRRVFSRMTVeenlamggffAERDQFQERIKWVYELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPR 157
|
170
....*....|.
gi 1031820327 440 ILVLDEATSAL 450
Cdd:PRK11614 158 LLLLDEPSLGL 168
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
295-521 |
1.19e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLAR-------ILLGFeRADaGQVTIDG--IDAGHLSreaQRQLRRKIQFVYQ- 364
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF-RVE-GKVTFHGknLYAPDVD---PVEVRRRIGMVFQk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 365 -NPFasldprqrlfaiieePLKNFERLSAATR--------RQRVESVAARVALAPEL---LSRTPRELSGGQRQRVAIAR 432
Cdd:PRK14243 100 pNPF---------------PKSIYDNIAYGARingykgdmDELVERSLRQAALWDEVkdkLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 433 ALILEPAILVLDEATSALDVTvqAQILALLQQLQQQLGLSYLFITHDLATVRRIAD---------SVTVLRAGQVVEHGD 503
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPI--STLRIEELMHELKEQYTIIIVTHNMQQAARVSDmtaffnvelTEGGGRYGYLVEFDR 242
|
250
....*....|....*...
gi 1031820327 504 VNRLFAAPQQAYTRELIA 521
Cdd:PRK14243 243 TEKIFNSPQQQATRDYVS 260
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
296-505 |
1.30e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.74 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAD--AGQVTIDGIDAghLSREAQRQLRRKIQFVYQNPF------ 367
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESI--LDLEPEERAHLGIFLAFQYPIeipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 368 ------ASLDPRQRLFAIIE-EPLKNFERLSaatrrqrveSVAARVALAPELLSRTPRE-LSGGQRQRVAIARALILEPA 439
Cdd:CHL00131 101 nadflrLAYNSKRKFQGLPElDPLEFLEIIN---------EKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 440 ILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHdlatVRR-----IADSVTVLRAGQVVEHGDVN 505
Cdd:CHL00131 172 LAILDETDSGLDID-ALKIIAEGINKLMTSENSIILITH----YQRlldyiKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
294-451 |
1.56e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRqlRRKIQFVYQNpfASLDPR 373
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYLPQE--ASIFRR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 374 QRLFAIIEEPLKNFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:PRK10895 93 LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-513 |
1.89e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 299 VSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDgiDAGHLSREAQRQLRRKIQFVYQNP------------ 366
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPllfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 --------------------FASLDPRQRLFAIIEEPLKNFERLSAAT---------------RRQRVESVAARVaLAPE 411
Cdd:PTZ00265 482 yslyslkdlealsnyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTdsneliemrknyqtiKDSEVVDVSKKV-LIHD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 412 LLSRTP-----------RELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDL 480
Cdd:PTZ00265 561 FVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
250 260 270
....*....|....*....|....*....|...
gi 1031820327 481 ATVrRIADSVTVLRAGQVVEHGDVNRLFAAPQQ 513
Cdd:PTZ00265 641 STI-RYANTIFVLSNRERGSTVDVDIIGEDPTK 672
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-232 |
2.15e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 13 YRSR--GEWREVVHN---------ISFSIQRGEMLAFVGESGSGKTTTAQAIIGllADnaRRDAGRIVLNGEVISDWSDK 81
Cdd:PRK11288 248 YRPRplGEVRLRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYG--AT--RRTAGQVYLDGKPIDIRSPR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRlrgVSISLVPQD-PGNSLNPVKTIGQQVEEILRLHQSL-----------SAAERRQQVLNllakVGLSHPEQRFdq 149
Cdd:PRK11288 324 DAIR---AGIMLCPEDrKAEGIIPVHSVADNINISARRHHLRagclinnrweaENADRFIRSLN----IKTPSREQLI-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 150 ypHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQ 229
Cdd:PRK11288 395 --MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMRE 471
|
...
gi 1031820327 230 GEI 232
Cdd:PRK11288 472 GRI 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
292-452 |
2.52e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.84 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 292 ALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLrrkiqfVYQNPFASLD 371
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI------LYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 PrqRLFAiiEEPLKNFERLSAATRRQrVESVAARVALAPelLSRTP-RELSGGQRQRVAIARALILEPAILVLDEATSAL 450
Cdd:TIGR01189 86 P--ELSA--LENLHFWAAIHGGAQRT-IEDALAAVGLTG--FEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
..
gi 1031820327 451 DV 452
Cdd:TIGR01189 159 DK 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
295-497 |
2.71e-12 |
|
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: 65.95 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqrqlrrKIQFVYQNPF---ASLd 371
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------------SIAYVSQEPWiqnGTI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 pRQR-LFAiieEPLKNferlsaatrrQRVESVAARVALAP--ELLS---RTprE-------LSGGQRQRVAIARALILEP 438
Cdd:cd03250 83 -RENiLFG---KPFDE----------ERYEKVIKACALEPdlEILPdgdLT--EigekginLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 439 AILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQ 497
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-236 |
4.71e-12 |
|
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: 65.89 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 29 SIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdagrivlNGEVISDwsdkrlnrlrGVSISLVPQdpgnSLNPvKTI 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD----------EGDIEIE----------LDTVSYKPQ----YIKA-DYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 109 GQqVEEILR--LHQSLSAAERRQQVLNLLakvglsHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDv 186
Cdd:cd03237 76 GT-VRDLLSsiTKDFYTHPYFKTEIAKPL------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 187 tVQKRILdLLDILRR---ESGTAVLFVTHDLALAAERADRIMVFrQGEIQEQG 236
Cdd:cd03237 148 -VEQRLM-ASKVIRRfaeNNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNG 197
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
277-451 |
5.30e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.87 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFslgkQALQALDSVSFEVRRGSTHALVGESGSGKTTL----ARILlgfeRADAGQVTIDGIDaghLSREAQ 352
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLlsmiSRLL----PPDSGEVLVDGLD---VATTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RQLRRKIQFVYQ-NPFASldprqRLfaIIEEpLKNF-------ERLSAATRRQrVESVAARVALAPeLLSRTPRELSGGQ 424
Cdd:COG4604 71 RELAKRLAILRQeNHINS-----RL--TVRE-LVAFgrfpyskGRLTAEDREI-IDEAIAYLDLED-LADRYLDELSGGQ 140
|
170 180
....*....|....*....|....*..
gi 1031820327 425 RQRVAIARALILEPAILVLDEATSALD 451
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-185 |
5.71e-12 |
|
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: 64.57 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLAdnARRDAGriVLNGEVISDWSDKR 82
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLA--GRKTAG--VITGEILINGRPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRgvSISLVPQdpgnslNPVKTIGQQVEEILRlhqsLSAAERrqqvlnllakvGLShPEQRfdqyphqlsggmkQRV 162
Cdd:cd03232 75 KNFQR--STGYVEQ------QDVHSPNLTVREALR----FSALLR-----------GLS-VEQR-------------KRL 117
|
170 180
....*....|....*....|...
gi 1031820327 163 LIAIAIALQPDLIIADEPTSALD 185
Cdd:cd03232 118 TIGVELAAKPSILFLDEPTSGLD 140
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
277-499 |
1.21e-11 |
|
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: 66.77 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA--GQVTIDG--IDAGHLsREAQ 352
Cdd:TIGR02633 2 LEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGspLKASNI-RDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 353 RqlrRKIQFVYQNpfASLDPRQRLFAII---EEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVA 429
Cdd:TIGR02633 77 R---AGIVIIHQE--LTLVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 430 IARALILEPAILVLDEATSALdVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-339 |
1.34e-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: 67.66 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGevisdwsdkrlnrlrgvSISLVPQDP---G 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM----DKVEGHVHMKG-----------------SVAYVPQQAwiqN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 NSLNPVKTIGQQVEEilrlhqslsaaERRQQVLN---LLAKVGL--SHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDL 174
Cdd:TIGR00957 713 DSLRENILFGKALNE-----------KYYQQVLEacaLLPDLEIlpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 175 IIADEPTSALDVTVQKRILD-LLDILRRESGTAVLFVTHDLALAAErADRIMVFRQGEIQEQGATETIVQRP-------- 245
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQRDgafaeflr 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 246 QHPYTRQLLHdLQDAPLGLTAARHRplatPAIRVE-GISKRFSLGKQALQALDSVSFEVRRGSTH----ALVGESGSGKT 320
Cdd:TIGR00957 861 TYAPDEQQGH-LEDSWTALVSGEGK----EAKLIEnGMLVTDVVGKQLQRQLSASSSDSGDQSRHhgssAELQKAEAKEE 935
|
330
....*....|....*....
gi 1031820327 321 TLAriLLGFERADAGQVTI 339
Cdd:TIGR00957 936 TWK--LMEADKAQTGQVEL 952
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-239 |
1.95e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 2 TVLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRdaGRIVLNGEVISDWS-D 80
Cdd:CHL00131 6 PILEIKNLHASVNEN----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILE--GDILFKGESILDLEpE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRlrgvSISLVPQdpgnslNPVKTIGQQVEEILRLhqslsAAERRQQVLNL---------------LAKVGLShpeq 145
Cdd:CHL00131 80 ERAHL----GIFLAFQ------YPIEIPGVSNADFLRL-----AYNSKRKFQGLpeldplefleiinekLKLVGMD---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 146 rfdqyPHQL--------SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRReSGTAVLFVTH-DLAL 216
Cdd:CHL00131 141 -----PSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMT-SENSIILITHyQRLL 214
|
250 260
....*....|....*....|...
gi 1031820327 217 AAERADRIMVFRQGEIQEQGATE 239
Cdd:CHL00131 215 DYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-245 |
2.15e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.27 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWsdkRLNRLRGvSISLVPQDP- 98
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKST----LLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRS-RLAVVSQTPf 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 -------GN-SLNPVKTIGQQVEEILRLhqslsaAERRQQVLNL----LAKVGlshpeqrfdQYPHQLSGGMKQRVLIAI 166
Cdd:PRK10789 400 lfsdtvaNNiALGRPDATQQEIEHVARL------ASVHDDILRLpqgyDTEVG---------ERGVMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 167 AIALQPDLIIADEPTSALDVTVQKRILDLLDILRResGTAVLFVTHDLALAAErADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
280-507 |
2.78e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 280 EGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAG-HLSREAqrqLRRK 358
Cdd:PRK10982 2 SNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEA---LENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 359 IQFVYQ------------NPFASLDPRQRLFA----IIEEPLKNFERLSAatrrqrveSVAARVALApellsrtprELSG 422
Cdd:PRK10982 75 ISMVHQelnlvlqrsvmdNMWLGRYPTKGMFVdqdkMYRDTKAIFDELDI--------DIDPRAKVA---------TLSV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALdVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:PRK10982 138 SQMQMIEIAKAFSYNAKIVIMDEPTSSL-TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQ 216
|
....*
gi 1031820327 503 DVNRL 507
Cdd:PRK10982 217 PLAGL 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-289 |
3.30e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVIsdwsdkrlnrlrgvsislvpqDPGNsL 102
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE----GEAWLFGQPV---------------------DAGD-I 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTIG--QQ---------VEEILRLHQ---SLSAAERRQQVLNLLAKVGLSHPEqrfDQYPHQLSGGMKQRVLIAIAI 168
Cdd:NF033858 336 ATRRRVGymSQafslygeltVRQNLELHArlfHLPAAEIAARVAEMLERFDLADVA---DALPDSLPLGIRQRLSLAVAV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 169 ALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLAlAAERADRIMVFRQGEIQEQGATETIVQRPQHP 248
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN-EAERCDRISLMHAGRVLASDTPAALVAARGAA 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 249 ytrqllhDLQDA-------------PLGLTAARHRPLATPAIRVEGISKRFSLG 289
Cdd:NF033858 492 -------TLEEAfiayleeaagaaaAPAAAAAPAAAAAAPAAPAPAPRRRFSLR 538
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-231 |
4.64e-11 |
|
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: 60.85 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 32 RGEMLAFVGESGSGKTTTAQAIIGLLadnARRDAGRIVLNGEVISDWSDKRLNrlrgvsislvpqdpgnslnpvktigqq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL---GPPGGGVIYIDGEDILEEVLDQLL--------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 112 veeilrlhqslsaaerrqqvlnllakvglshpEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKR 191
Cdd:smart00382 51 --------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1031820327 192 ILDL-----LDILRRESGTAVLFVTHDL-----ALAAERADRIMVFRQGE 231
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-452 |
5.08e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.19 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 1 MTVLSVEDLRisyrsRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIVLNGEVISDWSD 80
Cdd:PRK10636 1 MIVFSSLQIR-----RGV-RVLLDNATATINPGQKVGLVGKNGCGKST----LLALLKNEISADGGSYTFPGNWQLAWVN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLRGVSISLVpQDPGNSLNPVKTIGQQVEE------ILRLHQSLSAAER---RQQVLNLLAKVGLSHPEqrFDQYP 151
Cdd:PRK10636 71 QETPALPQPALEYV-IDGDREYRQLEAQLHDANErndghaIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQ--LERPV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVqkrILDLLDILRRESGTAVLfVTHDLALAAERADRIMVFRQGE 231
Cdd:PRK10636 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLIL-ISHDRDFLDPIVDKIIHIEQQS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 232 IQE----------QGATETIVQRPQHPYTRQLLHDLQ----------------------------------DAPLGLTAA 267
Cdd:PRK10636 224 LFEytgnyssfevQRATRLAQQQAMYESQQERVAHLQsyidrfrakatkakqaqsrikmlermeliapahvDNPFHFSFR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 268 RHRPLATPAIRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTI-DGIDAGH 346
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGY--GDRII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 347 LsreAQRQLRrkiqfvyqnpFASLDprqrlfaiiEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQ 426
Cdd:PRK10636 380 F---AQHQLE----------FLRAD---------ESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKA 437
|
490 500
....*....|....*....|....*.
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDL 463
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-242 |
6.15e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.91 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 14 RSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGevisdwsdkrlnrlrgvSISL 93
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNK----GTVDIKG-----------------SAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 VPQDPG--NSLNPVKTIgqqveEILRLHQSLSAAERRQ---QVLNLlAKVGlshpeqRFDQYP-HQLSGGMKQRVLIAIA 167
Cdd:PRK13545 90 IAISSGlnGQLTGIENI-----ELKGLMMGLTKEKIKEiipEIIEF-ADIG------KFIYQPvKTYSSGMKSRLGFAIS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 168 IALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIV 242
Cdd:PRK13545 158 VHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
296-510 |
7.02e-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: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDaghLSREAQRQLRRKIQFVYQNPF-------A 368
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN---IAKIGLHDLRFKITIIPQDPVlfsgslrM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 369 SLDP-----RQRLFAIIE-EPLKNFerlsaatrrqrvesVAARVALAPELLSRTPRELSGGQRQRVAIARALILEPAILV 442
Cdd:TIGR00957 1379 NLDPfsqysDEEVWWALElAHLKTF--------------VSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 443 LDEATSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRIAdSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:TIGR00957 1445 LDEATAAVDLET--DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-231 |
1.02e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.57 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNAR--RDAGRIVLNGEVisDW---SDKRLNRLRGVSIslvpq 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGkiKHSGRISFSSQF--SWimpGTIKENIIFGVSY----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 97 DPGNSLNPVKTIgQQVEEILRLhqslsaAERRQQVlnlLAKVGLShpeqrfdqyphqLSGGMKQRVLIAIAIALQPDLII 176
Cdd:cd03291 125 DEYRYKSVVKAC-QLEEDITKF------PEKDNTV---LGEGGIT------------LSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLAlAAERADRIMVFRQGE 231
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANKTRIL-VTSKME-HLKKADKILILHEGS 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
296-452 |
1.35e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.97 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLrrkiqfVYQNPFASLDPRQr 375
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL------LYLGHAPGIKTTL- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 376 lfaiieEPLKNFERLSAATRRQRVESVAARVALApELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:cd03231 89 ------SVLENLRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
296-532 |
1.66e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERAdAGQVTIDGIDAGHLSREAQRQLRrkiqfvyqnpfASLDPRQR 375
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHR-----------AYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 376 LFAIieepLKNFERLS--------AATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALI-------LEPAI 440
Cdd:COG4138 80 PPFA----MPVFQYLAlhqpagasSEAVEQLLAQLAEALGLED-KLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 441 LVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDvnrlfaaPQQAYTRELI 520
Cdd:COG4138 155 LLLDEPMNSLDVA-QQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE-------TAEVMTPENL 226
|
250
....*....|..
gi 1031820327 521 AAIPQVSSRLAQ 532
Cdd:COG4138 227 SEVFGVKFRRLE 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-242 |
1.71e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAII----------------------------- 54
Cdd:PTZ00265 1166 IEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 55 -------------------GLLADNAR--RDAGRIVLNGEVISDWSDKRLNRLrgvsISLVPQDPgnslnpvKTIGQQVE 113
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeGGSGEDSTvfKNSGKILLDGVDICDYNLKDLRNL----FSIVSQEP-------MLFNMSIY 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 114 EILRLHQSLSAAERRQQVLNLLA--KVGLSHPEQrFDQ----YPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVT 187
Cdd:PTZ00265 1314 ENIKFGKEDATREDVKRACKFAAidEFIESLPNK-YDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 188 VQKRILDLLDILRRESGTAVLFVTHDLAlAAERADRIMVF----RQGE-IQEQGATETIV 242
Cdd:PTZ00265 1393 SEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
302-512 |
1.74e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 302 EVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQ--------LRRKIQFVYQNPFASLDpr 373
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADyegtvrdlLSSITKDFYTHPYFKTE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 qrlfaiIEEPLKnferlsaatrrqrVESvaarvalapeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVT 453
Cdd:cd03237 99 ------IAKPLQ-------------IEQ----------ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 454 VQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRaGQVVEHGDVNrlfaAPQ 512
Cdd:cd03237 150 QRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVAN----PPQ 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
286-452 |
2.03e-10 |
|
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: 60.81 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 286 FSLGkQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLRR-KIQFVYQ 364
Cdd:cd03290 8 FSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 365 NPFAsldprqrLFAIIEEPLKnferLSAATRRQRVESVAARVALAPEL----------LSRTPRELSGGQRQRVAIARAL 434
Cdd:cd03290 87 KPWL-------LNATVEENIT----FGSPFNKQRYKAVTDACSLQPDIdllpfgdqteIGERGINLSGGQRQRICVARAL 155
|
170
....*....|....*...
gi 1031820327 435 ILEPAILVLDEATSALDV 452
Cdd:cd03290 156 YQNTNIVFLDDPFSALDI 173
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
306-453 |
2.49e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 306 GSTHALVGESGSGKTTLARILLGFERAD--AGQVTIDGidaghlsREAQRQLRRKIQFVYQNP--FASLDPRQRLF--AI 379
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANN-------RKPTKQILKRTGFVTQDDilYPHLTVRETLVfcSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 380 IEEP--LKNFERLSAAtrrqrvESVAARVALAP---ELLSRT-PRELSGGQRQRVAIARALILEPAILVLDEATSALDVT 453
Cdd:PLN03211 167 LRLPksLTKQEKILVA------ESVISELGLTKcenTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
289-515 |
3.53e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 289 GKQALQALDsvsFEVRRGSTHALVGESGSGKTTLARILLGFE--RADAGQVTIDGIDAGHLSREaqRQLRRKIQFVYQNP 366
Cdd:PRK09580 13 DKAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE--DRAGEGIFMAFQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FASLDPRQRLF------AIIE----EPLKNFERlsaatrRQRVESVAARVALAPELLSRTPRE-LSGGQRQRVAIARALI 435
Cdd:PRK09580 88 VEIPGVSNQFFlqtalnAVRSyrgqEPLDRFDF------QDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 436 LEPAILVLDEATSALDVTvQAQILALLQQLQQQLGLSYLFITHdlatVRRI-----ADSVTVLRAGQVVEHGDVNRLFAA 510
Cdd:PRK09580 162 LEPELCILDESDSGLDID-ALKIVADGVNSLRDGKRSFIIVTH----YQRIldyikPDYVHVLYQGRIVKSGDFTLVKQL 236
|
....*
gi 1031820327 511 PQQAY 515
Cdd:PRK09580 237 EEQGY 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
277-452 |
4.01e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISkrFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARIL--------------LGFERADAG------Q 336
Cdd:PLN03073 178 IHMENFS--ISVGGRDL--IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkncqiLHVEQEVVGddttalQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 337 VTIDG-IDAGHLSREAQRQLRRKIQFVYQNPFA----------SLDP-RQRLfaiiEEPLKNFERLSAATRRQRVESVAA 404
Cdd:PLN03073 254 CVLNTdIERTQLLEEEAQLVAQQRELEFETETGkgkgankdgvDKDAvSQRL----EEIYKRLELIDAYTAEARAASILA 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1031820327 405 RVALAPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PLN03073 330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
296-533 |
4.41e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADA--------GQVTIDG-----IDAGHLSReaqrqLRRKIQFV 362
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGeplaaIDAPRLAR-----LRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 363 YQNPFAsldprqrlFAIIEEPL----KNFERLSAATRRQR-VESVAARVALAPELLSRTPRELSGGQRQRVAIARAL--- 434
Cdd:PRK13547 92 AQPAFA--------FSAREIVLlgryPHARRAGALTHRDGeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 435 ------ILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGdvnrlf 508
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG------ 237
|
250 260
....*....|....*....|....*
gi 1031820327 509 aAPQQAYTRELIAAIPQVSSRLAQA 533
Cdd:PRK13547 238 -APADVLTPAHIARCYGFAVRLVDA 261
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-241 |
9.13e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnaRRDAGRIVLNGevisdwsdkrl 83
Cdd:PLN03232 615 ISIKNGYFSWDSKTS-KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS---HAETSSVVIRG----------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlrgvSISLVPQDP---GNSLNPVKTIGQQVEEiLRLHQSLSAAERrQQVLNLLAKVGLSHPEQRfdqyPHQLSGGMKQ 160
Cdd:PLN03232 680 ------SVAYVPQVSwifNATVRENILFGSDFES-ERYWRAIDVTAL-QHDLDLLPGRDLTEIGER----GVNISGGQKQ 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIALQPDLIIADEPTSALDVTVQKRILD--LLDILRresGTAVLFVTHDLALAAErADRIMVFRQGEIQEQGAT 238
Cdd:PLN03232 748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTF 823
|
...
gi 1031820327 239 ETI 241
Cdd:PLN03232 824 AEL 826
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-452 |
1.08e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarRDAGRIVLNGEVISDWSDKRLNRlRGVSIslvpqdpgnslnp 104
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ----KDSGSILFQGKEIDFKSSKEALE-NGISM------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 vktigqqveeilrLHQSLSAAERRQQVLNL----LAKVGLSHPEQR--------FDQY-----PHQ----LSGGMKQRVL 163
Cdd:PRK10982 78 -------------VHQELNLVLQRSVMDNMwlgrYPTKGMFVDQDKmyrdtkaiFDELdididPRAkvatLSVSQMQMIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 164 IAIAIALQPDLIIADEPTSALdvtVQKRILDLLDILR--RESGTAVLFVTHDLALAAERADRIMVFRQGE-IQEQGATE- 239
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQwIATQPLAGl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 240 TIVQRPQHPYTRQLLHDLQDAplgltaaRHRPLATpAIRVEGISkrfSLGKQALQaldSVSFEVRRGSTHALVGESGSGK 319
Cdd:PRK10982 222 TMDKIIAMMVGRSLTQRFPDK-------ENKPGEV-ILEVRNLT---SLRQPSIR---DVSFDLHKGEILGIAGLVGAKR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 320 TTLARILLGFERADAGQVTIDGID-AGHLSREAqrqlrrkiqfvYQNPFASLDPRQR--------------LFAIIEEPL 384
Cdd:PRK10982 288 TDIVETLFGIREKSAGTITLHGKKiNNHNANEA-----------INHGFALVTEERRstgiyayldigfnsLISNIRNYK 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 385 KNFERLSAATRRQRVESV--AARValapellsRTPRE------LSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK10982 357 NKVGLLDNSRMKSDTQWVidSMRV--------KTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
273-507 |
1.34e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 273 ATPAIRVEGISKRFSlgkqALQALDSVSFEVRRGSTHALVGESGSGKTTlarillgferaDAGQVTIDGIDAGHLSRE-- 350
Cdd:NF000106 10 ARNAVEVRGLVKHFG----EVKAVDGVDLDVREGTVLGVLGP*GAA**R-----------GALPAHV*GPDAGRRPWRf* 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 351 ----AQRQLRRKIQF---VYQNPFASLDPRQRLFAIieeplKNFERLSAATRRQRVESVAARVALApELLSRTPRELSGG 423
Cdd:NF000106 75 twcaNRRALRRTIG*hrpVR*GRRESFSGRENLYMI-----GR*LDLSRKDARARADELLERFSLT-EAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 424 QRQRVAIARALILEPAILVLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGD 503
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRT-RNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
....
gi 1031820327 504 VNRL 507
Cdd:NF000106 228 VDEL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
282-451 |
1.58e-09 |
|
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: 57.66 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 282 ISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLG----FERADaGQVTIDGIDAghlsREAQRQLRR 357
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPY----KEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 358 KIQFVYQNP--FASLDPRQRLfaiieeplknferlSAATRRQRVESVaarvalapellsrtpRELSGGQRQRVAIARALI 435
Cdd:cd03233 84 EIIYVSEEDvhFPTLTVRETL--------------DFALRCKGNEFV---------------RGISGGERKRVSIAEALV 134
|
170
....*....|....*.
gi 1031820327 436 LEPAILVLDEATSALD 451
Cdd:cd03233 135 SRASVLCWDNSTRGLD 150
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-236 |
1.64e-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: 57.33 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQaiiglladnarrdagrivlngEVISDWSDKRLNRLRgvsislvpqdPGNSLNP 104
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVN---------------------EGLYASGKARLISFL----------PKFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQqveeilrlhqslsaaerrqqvLNLLAKVGLSHpeQRFDQYPHQLSGGMKQRVLIA--IAIALQPDLIIADEPTS 182
Cdd:cd03238 62 LIFIDQ---------------------LQFLIDVGLGY--LTLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPST 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 183 ALDvtvQKRILDLLDILRR--ESGTAVLFVTHDLALaAERADRIMVF------RQGEIQEQG 236
Cdd:cd03238 119 GLH---QQDINQLLEVIKGliDLGNTVILIEHNLDV-LSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
281-451 |
2.00e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 281 GISKRFSLGKQALQALdSVSFevRRGSTHALVGESGSGKTTLARILLGFERADAGQVTI-DGIDAGHLSREAQrqlrrki 359
Cdd:TIGR03719 9 RVSKVVPPKKEILKDI-SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYLPQEPQ------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 360 qfvyqnpfasLDPRQRLFAIIEEP-------LKNFERLSA------------ATRRQRVE---------SVAARVALAPE 411
Cdd:TIGR03719 79 ----------LDPTKTVRENVEEGvaeikdaLDRFNEISAkyaepdadfdklAAEQAELQeiidaadawDLDSQLEIAMD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1031820327 412 LLsRTP------RELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:TIGR03719 149 AL-RCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
251-445 |
2.70e-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: 59.43 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 251 RQLLHDLQDAPLGLTAARHRPLATP--AIRVEGIS---------KRFSLGkqalqaldSVSFEVRRGSTHALVGESGSGK 319
Cdd:COG4615 300 EELELALAAAEPAAADAAAPPAPADfqTLELRGVTyrypgedgdEGFTLG--------PIDLTIRRGELVFIVGGNGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 320 TTLARILLGFERADAGQVTIDGIDAGHLSREAQRQlrrkiqfvyqnpfasldprqrLFAIIEEPLKNFERLSAATRrqrv 399
Cdd:COG4615 372 STLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ---------------------LFSAVFSDFHLFDRLLGLDG---- 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 400 esvAARVALAPELLSR--------------TPRELSGGQRQRVAIARALiLEPA-ILVLDE 445
Cdd:COG4615 427 ---EADPARARELLERleldhkvsvedgrfSTTDLSQGQRKRLALLVAL-LEDRpILVFDE 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-230 |
3.15e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 22 VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLL--ADNARRDAGRIVLNGEVisDW---SDKRLNRLRGVSIslvpq 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELepSEGKIKHSGRISFSPQT--SWimpGTIKDNIIFGLSY----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 97 DPGNSLNPVKTIgqQVEEILRLHqslsaAERRQQVlnlLAKVGLShpeqrfdqyphqLSGGMKQRVLIAIAIALQPDLII 176
Cdd:TIGR01271 514 DEYRYTSVIKAC--QLEEDIALF-----PEKDKTV---LGEGGIT------------LSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRRESGTAVLfVTHDLAlAAERADRIMVFRQG 230
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFESCLCKLMSNKTRIL-VTSKLE-HLKKADKILLLHEG 623
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-245 |
3.60e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLAdnarrdagriVLNGEVisdWSDKrlnrlrgvSISLVPQDP- 98
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE----------ISEGRV---WAER--------SIAYVPQQAw 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 99 -------GNSL--NPvktigqqvEEILRLHQSLSAAERRQQVLNLLAkvGLshpEQRFDQYPHQLSGGMKQRVLIAIAIA 169
Cdd:PTZ00243 732 imnatvrGNILffDE--------EDAARLADAVRVSQLEADLAQLGG--GL---ETEIGEKGVNLSGGQKARVSLARAVY 798
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 170 LQPDLIIADEPTSALDVTVQKRILDLLdILRRESGTAVLFVTHDLALAAeRADRIMVFRQGEIQEQGATETIVQRP 245
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
296-509 |
4.62e-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: 57.23 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLAriLLGFERADA--GQVTIDGIDaghLSREAQRQLRRKIQFVYQNPFA----- 368
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfdGKIVIDGID---ISKLPLHTLRSRLSIILQDPILfsgsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 369 --SLDPRQRlfaIIEEPLknFERLSAATRRQRVESVAARValaPELLSRTPRELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:cd03288 112 rfNLDPECK---CTDDRL--WEALEIAQLKNMVKSLPGGL---DAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 447 TSALDVTVqaQILALLQQLQQQLGLSYLFITHDLATVRRiADSVTVLRAGQVVEHGDVNRLFA 509
Cdd:cd03288 184 TASIDMAT--ENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-248 |
6.43e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwREVVHNISFSIQRGEMLAFVGESGSGKTTTAQaIIGLLADNARrdaGRIVLNGEviSDWSDKRL 83
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYDPTE---GDIIINDS--HNLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDP---GNS-----------LNPVKTIGQQVEEILRLHQS-----LSAAERRQQVLNLLAKV----GL 140
Cdd:PTZ00265 456 KWWRS-KIGVVSQDPllfSNSiknnikyslysLKDLEALSNYYNEDGNDSQEnknkrNSCRAKCAGDLNDMSNTtdsnEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 141 SHPEQRF-------------------------DQY-------PHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTV 188
Cdd:PTZ00265 535 IEMRKNYqtikdsevvdvskkvlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 189 QKRILDLLDILRRESGTAVLFVTHDLAlAAERADRIMVFRQgeiQEQGATETIVQRPQHP 248
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN---RERGSTVDVDIIGEDP 670
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
296-509 |
7.80e-09 |
|
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: 58.80 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGiDAGHLSREAQRQ---LRRKIQFVYQnpfasldp 372
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQndsLRENILFGKA-------- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 373 rqrlfaiIEEPlknferlsaatrrqRVESVAARVALAP--ELLSRTPR--------ELSGGQRQRVAIARALILEPAILV 442
Cdd:TIGR00957 725 -------LNEK--------------YYQQVLEACALLPdlEILPSGDRteigekgvNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 443 LDEATSALDVTVQAQI-LALLQQLQQQLGLSYLFITHDLATVRRIaDSVTVLRAGQVVEHGDVNRLFA 509
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIfEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-234 |
1.07e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwreVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRL 83
Cdd:PRK10522 323 LELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY----QPQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLrgvsISLVPQD---------PGNSlNPVKTIGQQVEEILRLHQSLSAAERRqqVLNLlakvglshpeqrfdqyphQL 154
Cdd:PRK10522 396 RKL----FSAVFTDfhlfdqllgPEGK-PANPALVEKWLERLKMAHKLELEDGR--ISNL------------------KL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAaERADRIMVFRQGEIQE 234
Cdd:PRK10522 451 SKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
287-451 |
1.08e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 287 SLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDgidaGHLSREAQRQlrRKIQFVYQNP 366
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID----GKTATRGDRS--RFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 367 FASLDprqrlfaiiEEPLKNFERLSA--ATRRQRVESVAARVALAPELLSRTPRELSGGQRQRVAIARaLILEPAIL-VL 443
Cdd:PRK13543 92 GLKAD---------LSTLENLHFLCGlhGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLL 161
|
....*...
gi 1031820327 444 DEATSALD 451
Cdd:PRK13543 162 DEPYANLD 169
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-226 |
1.10e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 21 EVVHNI---SFSIQR------GEMLAFVGESGSGKTTTAQaiigLLADNARRDAGRIVLNGevisDWsDKRLNRLRGVSI 91
Cdd:cd03236 5 EPVHRYgpnSFKLHRlpvpreGQVLGLVGPNGIGKSTALK----ILAGKLKPNLGKFDDPP----DW-DEILDEFRGSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 92 slvpQD-----PGNSLNPVKTIgQQVEEILR-----LHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQLSGGMKQR 161
Cdd:cd03236 76 ----QNyftklLEGDVKVIVKP-QYVDLIPKavkgkVGELLKKKDERGKLDELVDQLEL---RHVLDRNIDQLSGGELQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVtvqKRILDLLDILRR--ESGTAVLFVTHDLALAAERADRIMV 226
Cdd:cd03236 148 VAIAAALARDADFYFFDEPSSYLDI---KQRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHC 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
303-493 |
1.17e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 303 VRRGSTHALVGESGSGKTTLARILLG-----FERADaGQVTIDG-IDA-------GHLSREAQRQLR--RKIQFVYQNPf 367
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnLGDYE-EEPSWDEvLKRfrgtelqNYFKKLYNGEIKvvHKPQYVDLIP- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 368 asldprQRLFAIIEEPLKNferlsaATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEAT 447
Cdd:PRK13409 174 ------KVFKGKVRELLKK------VDERGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1031820327 448 SALDvtVQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:PRK13409 241 SYLD--IRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-452 |
1.39e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdagrivlNGEVIsdWSDkrlnrlrGVSISLVPQDPg 99
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF----------EGEAR--PAP-------GIKVGYLPQEP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 100 nSLNPVKTIGQQVEE-------ILRLHQSLSA------------AERRQQVLNLLAKVGLSHPEQRFDQY------PH-- 152
Cdd:PRK11819 80 -QLDPEKTVRENVEEgvaevkaALDRFNEIYAayaepdadfdalAAEQGELQEIIDAADAWDLDSQLEIAmdalrcPPwd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 ----QLSGGMKQRVliaiaiAL------QPDLIIADEPTSALDV-TVQKrildLLDILRRESGTaVLFVTHD---LALAA 218
Cdd:PRK11819 159 akvtKLSGGERRRV------ALcrllleKPDMLLLDEPTNHLDAeSVAW----LEQFLHDYPGT-VVAVTHDryfLDNVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 219 E-----------------------RADRImvfRQGEIQEQGATETIVQ-----RpQHPYTRQllhDLQDAPLG-----LT 265
Cdd:PRK11819 228 GwileldrgrgipwegnysswleqKAKRL---AQEEKQEAARQKALKRelewvR-QSPKARQ---AKSKARLAryeelLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 266 AARHRPLAT-----PA--------IRVEGISKRFslGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERA 332
Cdd:PRK11819 301 EEYQKRNETneifiPPgprlgdkvIEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 333 DAGQVTI-DGIdaghlsreaqrqlrrKIQFVYQNPfASLDPRQRLFAIIEE-----PLKNFERLSAATrrqrvesVAA-- 404
Cdd:PRK11819 377 DSGTIKIgETV---------------KLAYVDQSR-DALDPNKTVWEEISGgldiiKVGNREIPSRAY-------VGRfn 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 405 --------RVAlapellsrtprELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK11819 434 fkggdqqkKVG-----------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
290-451 |
1.65e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 290 KQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLgfERADAGQVTIDGIDAGhlSREAQRQLRRKIQFVYQN---- 365
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVN--GRPLDSSFQRSIGYVQQQdlhl 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 366 PFASLDPRQRLFAIIEEPLKnferLSAATRRQRVESVAARVALA--PELLSRTPRE-LSGGQRQRVAIARALILEPAILV 442
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKS----VSKSEKMEYVEEVIKLLEMEsyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLL 924
|
170
....*....|
gi 1031820327 443 -LDEATSALD 451
Cdd:TIGR00956 925 fLDEPTSGLD 934
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
294-451 |
1.78e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 294 QALDSVSFEVRRGSTHALVGESGSGKTTLARILL----GFERADAGQVTIDGIDaghlSREAQRQLRRKIQFVYQNP--F 367
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT----PEEIKKHYRGDVVYNAETDvhF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 368 ASLDPRQRL-FAIIEEPLKNfeRLSAATRRQRVESVAArVALAPELLSRTP---------RELSGGQRQRVAIARALILE 437
Cdd:TIGR00956 151 PHLTVGETLdFAARCKTPQN--RPDGVSREEYAKHIAD-VYMATYGLSHTRntkvgndfvRGVSGGERKRVSIAEASLGG 227
|
170
....*....|....
gi 1031820327 438 PAILVLDEATSALD 451
Cdd:TIGR00956 228 AKIQCWDNATRGLD 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
296-499 |
2.66e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTID--------------------------GI--DAGHL 347
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnvegtvydfvaeGIeeQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 348 srEAQRQLRRKIQFvyqnpfaslDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARVALAPE-LLSrtprELSGGQRQ 426
Cdd:PRK11147 99 --KRYHDISHLVET---------DPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDaALS----SLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 427 RVAIARALILEPAILVLDEATSALDVTvqaqILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVV 499
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-232 |
2.90e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 11 ISYRSRGEWRE--VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDaGRIVLNGEVisdwSDKRLNRLRG 88
Cdd:cd03233 9 ISFTTGKGRSKipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVE-GDIHYNGIP----YKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 89 vSISLVPQDpgNSLNPVKTIGQQVEEILRLhqslsaaerrqqvlnllakvglshpeqRFDQYPHQLSGGMKQRVLIAIAI 168
Cdd:cd03233 84 -EIIYVSEE--DVHFPTLTVRETLDFALRC---------------------------KGNEFVRGISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 169 ALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTaVLFVThdLALAAERA----DRIMVFRQGEI 232
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKT-TTFVS--LYQASDEIydlfDKVLVLYEGRQ 198
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-224 |
3.28e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.19 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAqaiIGLLADNARRdagRIVlngEVISDWSDKRL--------NRLRGVSISLVPQ 96
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLA---FDTIYAEGQR---RYV---ESLSAYARQFLgqmdkpdvDSIEGLSPAIAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 97 DPGNSLNPVKTIGqQVEEI---LRLHQSLSAAERRqqvLNLLAKVGLSHpeQRFDQYPHQLSGGMKQRVLIA--IAIALQ 171
Cdd:cd03270 84 QKTTSRNPRSTVG-TVTEIydyLRLLFARVGIRER---LGFLVDVGLGY--LTLSRSAPTLSGGEAQRIRLAtqIGSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 172 PDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAErADRI 224
Cdd:cd03270 158 GVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
295-505 |
3.31e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDA---------GHLSREAQRQLRRKIQFVYQN 365
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaissglnGQLTGIENIELKGLMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 366 PFASLDPRQRLFA----IIEEPLKNFerlsaatrrqrvesvaarvalapellsrtprelSGGQRQRVAIARALILEPAIL 441
Cdd:PRK13545 119 KIKEIIPEIIEFAdigkFIYQPVKTY---------------------------------SSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 442 VLDEATSALDVTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVN 505
Cdd:PRK13545 166 VIDEALSVGDQTF-TKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-258 |
4.68e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdaGRIVLNGEVisdwsdkrlnrlrgvsiSLVPQDPGnsLNP 104
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV----GKVDRNGEV-----------------SVIAISAG--LSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 VKTIGQQVEeilrlHQSLSAAERRQQVLNLLAK-VGLSHPEQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSA 183
Cdd:PRK13546 99 QLTGIENIE-----FKMLCMGFKRKEIKAMTPKiIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 184 LDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATETIVqrpqhPYTRQLLHDLQ 258
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL-----PKYEAFLNDFK 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-230 |
5.92e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.49 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 25 NISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSDKRLNRLRGVSISLVPQDPGnslnp 104
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 105 vkTIGQQVEEILRLHQSLSAaERRQQVLNLLAKvglsHPEqrFDQYPH-----------QLSGGMKQRVLIAIAIALQPD 173
Cdd:cd03290 90 --LLNATVEENITFGSPFNK-QRYKAVTDACSL----QPD--IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 174 LIIADEPTSALDVTVQKRILD--LLDILRRESGTAVLfVTHDLALAAErADRIMVFRQG 230
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
296-502 |
6.23e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTT-LARI--LLGFEradaGQVTIDGIDAGHLSreAQRQLRRKIQFVYQ-NPFASLD 371
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTlLARMagLLPGS----GSIQFAGQPLEAWS--AAELARHRAYLSQQqTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 PRQRLfaiieePLKNFERLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIArALILE--PAI------LVL 443
Cdd:PRK03695 86 VFQYL------TLHQPDKTRTEAVASALNEVAEALGLDD-KLGRSVNQLSGGEWQRVRLA-AVVLQvwPDInpagqlLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 444 DEATSALDVTvQAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHG 502
Cdd:PRK03695 158 DEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
295-445 |
6.52e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQLrrkiqfvyqnpFASLDPRQ 374
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-----------FSAVFTDF 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 375 RLFAIIEEPlKNFERLSAAtrrqrVESVAARVALAPELLSRTPR----ELSGGQRQRVAIARALILEPAILVLDE 445
Cdd:PRK10522 407 HLFDQLLGP-EGKPANPAL-----VEKWLERLKMAHKLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-232 |
7.66e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGllADNARRDAGRIVLNGEVIsdwsdkrlnRLRGVS------ISL 93
Cdd:NF040905 273 RKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRNISGTVFKDGKEV---------DVSTVSdaidagLAY 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 VPQD-PGNSLNPVKTIGQQV----------EEILRLHQSLSAAERRQQVLN-----LLAKVGlshpeqrfdqyphQLSGG 157
Cdd:NF040905 342 VTEDrKGYGLNLIDDIKRNItlanlgkvsrRGVIDENEEIKVAEEYRKKMNiktpsVFQKVG-------------NLSGG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 158 MKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-212 |
1.09e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGllaDNARRDAGRIVL------NGEVIsdWSDKRlnRLRGVSISL 93
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG---DHPQGYSNDLTLfgrrrgSGETI--WDIKK--HIGYVSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 vPQDPGNSLNPVKTIGQQVEEILRLHQSLSAAERR--QQVLNLLakvGLShpEQRFDQYPHQLSGGMKQRVLIAIAIALQ 171
Cdd:PRK10938 346 -HLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKlaQQWLDIL---GID--KRTADAPFHSLSWGQQRLALIVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1031820327 172 PDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTH 212
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-225 |
1.32e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.21 E-value: 1.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 152 HQLSGGMKQRVLIAIAIALQP----DLIIADEPTSALDVTVQKRILDLLdILRRESGTAVLFVTHDLALaAERADRIM 225
Cdd:cd03227 76 LQLSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAI-LEHLVKGAQVIVITHLPEL-AELADKLI 151
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
298-454 |
1.53e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.98 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 298 SVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqrqlRRKIQFVYQNPFASLdprQRLF 377
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA--------------KGKLFYVPQRPYMTL---GTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 378 AIIEEPLKNFERLSAATRRQRVESVAARVALApELLSRT---------PRELSGGQRQRVAIARALILEPAILVLDEATS 448
Cdd:TIGR00954 533 DQIIYPDSSEDMKRRGLSDKDLEQILDNVQLT-HILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
....*.
gi 1031820327 449 ALDVTV 454
Cdd:TIGR00954 612 AVSVDV 617
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
279-451 |
1.55e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 279 VEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADaGQVTIDGIDAGHLSREAQRQ---- 354
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKafgv 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 LRRKIqFVYQNPF-ASLDPrqrlfaiieeplknFERLSaatrRQRVESVAARVALApELLSRTPRE-----------LSG 422
Cdd:TIGR01271 1297 IPQKV-FIFSGTFrKNLDP--------------YEQWS----DEEIWKVAEEVGLK-SVIEQFPDKldfvlvdggyvLSN 1356
|
170 180
....*....|....*....|....*....
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-213 |
2.55e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLriSYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaIIGLLADNARRDAGRIvlngevisdwsdKR 82
Cdd:PRK11147 319 VFEMENV--NYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTT----LLKLMLGQLQADSGRI------------HC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLrgvSISLVPQDPGNsLNPVKTIGQQVEEilrLHQSLSAAERRQQVLNLLAKVgLSHPeQRFDQYPHQLSGGMKQRV 162
Cdd:PRK11147 379 GTKL---EVAYFDQHRAE-LDPEKTVMDNLAE---GKQEVMVNGRPRHVLGYLQDF-LFHP-KRAMTPVKALSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 163 LIAiAIALQP-DLIIADEPTSALDVtvqkRILDLL-DILRRESGTaVLFVTHD 213
Cdd:PRK11147 450 LLA-RLFLKPsNLLILDEPTNDLDV----ETLELLeELLDSYQGT-VLLVSHD 496
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-236 |
4.36e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYrsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGllADNARRDAGRIVLNGEVISDWSDKR 82
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LnrlRGVSISLVPQdpgnslNPVKTIGqqVEEILRLHQSLSAAE--RRQQVLNLLAKVGLSHPEQRFDQYPHQL------ 154
Cdd:PRK09580 75 R---AGEGIFMAFQ------YPVEIPG--VSNQFFLQTALNAVRsyRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvn 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 ---SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESgTAVLFVTH-DLALAAERADRIMVFRQG 230
Cdd:PRK09580 144 vgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHyQRILDYIKPDYVHVLYQG 222
|
....*.
gi 1031820327 231 EIQEQG 236
Cdd:PRK09580 223 RIVKSG 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-189 |
4.89e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGewREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdaGRIVLNGevISdWSDKRL 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-----GEIQIDG--VS-WNSVTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDpgnslnpVKTIGQQVEEILRLHQSLSaaerRQQVLNLLAKVGLshpEQRFDQYPHQ---------- 153
Cdd:TIGR01271 1288 QTWRK-AFGVIPQK-------VFIFSGTFRKNLDPYEQWS----DEEIWKVAEEVGL---KSVIEQFPDKldfvlvdggy 1352
|
170 180 190
....*....|....*....|....*....|....*...
gi 1031820327 154 -LSGGMKQRVLIAIAIALQPDLIIADEPTSALD-VTVQ 189
Cdd:TIGR01271 1353 vLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-251 |
8.22e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 7 EDLRISYRSrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSdkrLNRL 86
Cdd:PLN03232 1238 EDVHLRYRP--GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELEKGRIMIDDCDVAKFG---LTDL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 RGVsISLVPQDPGNSLNPVKTIGQQVEEilrlHQ--SLSAAERRQQVLNLLAKVGLSHPEQRFDQyPHQLSGGMKQRVLI 164
Cdd:PLN03232 1309 RRV-LSIIPQSPVLFSGTVRFNIDPFSE----HNdaDLWEALERAHIKDVIDRNPFGLDAEVSEG-GENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 165 AIAIALQPDLIIADEPTSALDVtvqkRILDLLDILRRES--GTAVLFVTHDLALAAErADRIMVFRQGEIQEQGATETIV 242
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDV----RTDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
....*....
gi 1031820327 243 QRPQHPYTR 251
Cdd:PLN03232 1458 SRDTSAFFR 1466
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-236 |
8.54e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYrsrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNArrdagrivlnGEVisDWSDKrl 83
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS----------GTV--KWSEN-- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 nrlrgVSISLVPQDPG----NSLNPVKTIGQ---------QVEEIL-RLhqSLSAAERRQQVlnllaKVglshpeqrfdq 149
Cdd:PRK15064 382 -----ANIGYYAQDHAydfeNDLTLFDWMSQwrqegddeqAVRGTLgRL--LFSQDDIKKSV-----KV----------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 150 yphqLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVtvqKRILDLLDILRRESGTaVLFVTHDLALAAERADRIMvfrq 229
Cdd:PRK15064 439 ----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEGT-LIFVSHDREFVSSLATRII---- 506
|
....*..
gi 1031820327 230 gEIQEQG 236
Cdd:PRK15064 507 -EITPDG 512
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-230 |
9.28e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 16 RGEWREVVHNISFSIQRGEMLAFVGESGSGKTTtaqaiigLLADNARRDAGRIVLNGEVISDWS--DKRLNRlrgvSISL 93
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTT-------LLNVLAERVTTGVITGGDRLVNGRplDSSFQR----SIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 VPQDPGNSlnPVKTIGQ--QVEEILRLHQSLSAAERR---QQVLNLL-------AKVGLS----HPEQRfdqyphqlsgg 157
Cdd:TIGR00956 841 VQQQDLHL--PTSTVREslRFSAYLRQPKSVSKSEKMeyvEEVIKLLemesyadAVVGVPgeglNVEQR----------- 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 158 mkQRVLIAIAIALQPDLII-ADEPTSALDVTVQKRILDLLDILrRESGTAVLFVTHD-LALAAERADRIMVFRQG 230
Cdd:TIGR00956 908 --KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQpSAILFEEFDRLLLLQKG 979
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
303-493 |
1.00e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 303 VRRGSTHALVGESGSGKTTLARILLG--------FERADAGQVTIDGIDAGHLSREAQRQLRRKIQFVYQNPFASLDPRQ 374
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAIIEeplknfeRLSAATRRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTv 454
Cdd:cd03236 103 VKGKVGE-------LLKKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK- 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1031820327 455 QAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
252-503 |
1.30e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 252 QLLHDLQDAPLGLTAARHRPLATPAIRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLG-FE 330
Cdd:PTZ00243 634 ASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELEPKVL--LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 331 radagqvtidgIDAGHLSREaqrqlrRKIQFVYQNPF---ASLdpRQRLFAIIEEplkNFERLSAATRRQRVEsvaARVA 407
Cdd:PTZ00243 712 -----------ISEGRVWAE------RSIAYVPQQAWimnATV--RGNILFFDEE---DAARLADAVRVSQLE---ADLA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 408 LAPELLSRTPRE----LSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQLGLSYLfITHDLATV 483
Cdd:PTZ00243 767 QLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVV 845
|
250 260
....*....|....*....|
gi 1031820327 484 RRiADSVTVLRAGQVVEHGD 503
Cdd:PTZ00243 846 PR-ADYVVALGDGRVEFSGS 864
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-239 |
1.31e-06 |
|
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: 51.55 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGllaDNARRDAGRIVLNGEVISDWSDKRLNrlrgvsISLVPQdpGNSL 102
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILTNISDVHQN------MGYCPQ--FDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 103 NPVKTiGQqveEILRLHQSLSA--AERRQQVLNL-LAKVGLShpeQRFDQYPHQLSGGMKQRVLIAIAIALQPDLIIADE 179
Cdd:TIGR01257 2024 DDLLT-GR---EHLYLYARLRGvpAEEIEKVANWsIQSLGLS---LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 180 PTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE 239
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-227 |
1.54e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 1.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 154 LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAAERADRIMVF 227
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
267-454 |
1.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 267 ARHRPL--ATPAIRVEgiSKRFSL-GKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGfERADAGQVTIDgid 343
Cdd:PLN03232 603 AQNPPLqpGAPAISIK--NGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETSSVV--- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 344 aghlsreaqrqLRRKIQFVYQNP--FASLDPRQRLFAIIEEPLKNFERLSAATRRQRVESVAARvalapELLSRTPR--E 419
Cdd:PLN03232 677 -----------IRGSVAYVPQVSwiFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGR-----DLTEIGERgvN 740
|
170 180 190
....*....|....*....|....*....|....*
gi 1031820327 420 LSGGQRQRVAIARALILEPAILVLDEATSALDVTV 454
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-452 |
3.04e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 20 REVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDW---------SDKRLNRLRGVS 90
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDttalqcvlnTDIERTQLLEEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 91 ISLVPQ--------DPGNSLNPVKT------IGQQVEEILRLHQSLSAAERRQQVLNLLAkvGLSHPEQRFDQYPHQLSG 156
Cdd:PLN03073 270 AQLVAQqrelefetETGKGKGANKDgvdkdaVSQRLEEIYKRLELIDAYTAEARAASILA--GLSFTPEMQVKATKTFSG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 157 GMKQRVLIAIAIALQPDLIIADEPTSALDVTVqkrILDLLDILRRESGTaVLFVTHDLA-LAAERADRIMVFRQGEIQEQ 235
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKT-FIVVSHAREfLNTVVTDILHLHGQKLVTYK 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 236 GATETIVQ-RPQHPYTRQLLHDLQDaplglTAARHRPLATPAIRVEgiSKRFSLGKQALQALD----------------- 297
Cdd:PLN03073 424 GDYDTFERtREEQLKNQQKAFESNE-----RSRSHMQAFIDKFRYN--AKRASLVQSRIKALDrlghvdavvndpdykfe 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 298 ------------------------------SVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTidgidaghl 347
Cdd:PLN03073 497 fptpddrpgppiisfsdasfgypggpllfkNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 348 sreaqRQLRRKIQFVYQNPFASLDprqrlfaIIEEPLKNFERLSAATRRQRVESVAARVALAPELLSRTPRELSGGQRQR 427
Cdd:PLN03073 568 -----RSAKVRMAVFSQHHVDGLD-------LSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSR 635
|
490 500
....*....|....*....|....*
gi 1031820327 428 VAIARALILEPAILVLDEATSALDV 452
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
300-453 |
3.08e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 300 SFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAGHLSREAQRQL------RRKIQFVYQNPfaslDPR 373
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLvsdewqRNNTDMLSPGE----DDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 374 QRLFA-IIEEPLKNferlsaatrRQRVESVAARVALAPeLLSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDV 452
Cdd:PRK10938 99 GRTTAeIIQDEVKD---------PARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
.
gi 1031820327 453 T 453
Cdd:PRK10938 169 A 169
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
295-505 |
3.51e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 295 ALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqrqlrrKIQFVYQNpfASLDPRQ 374
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--AGLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 375 RLFAIIEeplknFERLSAATRRQRVESVAARVALAPEL---LSRTPRELSGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:PRK13546 101 TGIENIE-----FKMLCMGFKRKEIKAMTPKIIEFSELgefIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 452 VTVqAQILALLQQLQQQLGLSYLFITHDLATVRRIADSVTVLRAGQVVEHGDVN 505
Cdd:PRK13546 176 QTF-AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
238-532 |
4.99e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 238 TETIVQRPQHPytrqllhdlqdaplglTAARHRPLATPAIRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGS 317
Cdd:PTZ00243 1286 TGTVVIEPASP----------------TSAAPHPVQAGSLVFEGVQMRYREGLPLV--LRGVSFRIAPREKVGIVGRTGS 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 318 GKTTLariLLGFER---ADAGQVTIDGIDAGHLsreAQRQLRRKIQFVYQNPFasldprqrLF-AIIEEPLKNFERLSAA 393
Cdd:PTZ00243 1348 GKSTL---LLTFMRmveVCGGEIRVNGREIGAY---GLRELRRQFSMIPQDPV--------LFdGTVRQNVDPFLEASSA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 394 TRRQRVESVAARVALAPELLSRTPRELSG------GQRQRVAIARALILE-PAILVLDEATS----ALDVTVqaqilall 462
Cdd:PTZ00243 1414 EVWAALELVGLRERVASESEGIDSRVLEGgsnysvGQRQLMCMARALLKKgSGFILMDEATAnidpALDRQI-------- 1485
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 463 QQLQQQLGLSYLFIT--HDLATVRRIaDSVTVLRAGQVVEHGDVNRLFAAPQQAYTRELIAAIPQVSSRLAQ 532
Cdd:PTZ00243 1486 QATVMSAFSAYTVITiaHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSEAKRFLQ 1556
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-77 |
5.12e-06 |
|
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: 49.03 E-value: 5.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 4 LSVEDLRISYRSRGEWRE-VVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISD 77
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLY----RPESGEILLDGQPVTA 398
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
274-451 |
1.17e-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: 48.47 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 274 TPAIRVEGISKRFSlgKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqR 353
Cdd:TIGR01257 1935 TDILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-----------K 2001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 354 QLRRKIQFVYQNpfASLDPRqrlFAIIEEPLKNFERLSAATR-----RQRVESVA------ARVALAPELLSRTpreLSG 422
Cdd:TIGR01257 2002 SILTNISDVHQN--MGYCPQ---FDAIDDLLTGREHLYLYARlrgvpAEEIEKVAnwsiqsLGLSLYADRLAGT---YSG 2073
|
170 180
....*....|....*....|....*....
gi 1031820327 423 GQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:TIGR01257 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-222 |
1.18e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 3 VLSVEDLRISYRSRgewrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVIsdwsDKR 82
Cdd:PRK13540 1 MLDVIELDFDYHDQ----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL----NPEKGEILFERQSI----KKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 83 LNRLRGvSISLVPQDPGnsLNPVKTIGQQVeeILRLHQSLSAAErrqqVLNLLAKVGLSHpeqrFDQYP-HQLSGGMKQR 161
Cdd:PRK13540 69 LCTYQK-QLCFVGHRSG--INPYLTLRENC--LYDIHFSPGAVG----ITELCRLFSLEH----LIDYPcGLLSSGQKRQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 162 VLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRRESGtAVLFVTH-DLALaaERAD 222
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGG-AVLLTSHqDLPL--NKAD 194
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
310-487 |
1.47e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 310 ALVGESGSGKTTLARILLGFERADAGQVTIdgIDAGHLSREAQRQLRRKIQFvyqnpfasldprqrlfaiieeplknfer 389
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVG---------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 390 lsaatrrqrvesvaarvalapellsRTPRELSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILALLQQLQQQL 469
Cdd:smart00382 56 -------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170 180
....*....|....*....|...
gi 1031820327 470 GLSY-----LFITHDLATVRRIA 487
Cdd:smart00382 111 LKSEknltvILTTNDEKDLGPAL 133
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-212 |
1.54e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 26 ISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEvisdwSDKRLNRLRGVSIslvpqdpgnsLNPV 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLL----HVESGQIQIDGK-----TATRGDRSRFMAY----------LGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 106 KTIGQQVEEILRLH--QSLSAAERRQQVLNLLAKVGLSHPEQRFDQyphQLSGGMKQRVLIAiAIALQP-DLIIADEPTS 182
Cdd:PRK13543 91 PGLKADLSTLENLHflCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALA-RLWLSPaPLWLLDEPYA 166
|
170 180 190
....*....|....*....|....*....|...
gi 1031820327 183 ALD---VTVQKRILDlldiLRRESGTAVLFVTH 212
Cdd:PRK13543 167 NLDlegITLVNRMIS----AHLRGGGAALVTTH 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
122-247 |
1.94e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 122 LSAAERRQQVLNLLAKVGLSHPEQRfdqYPHQLSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLDILRR 201
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGR---AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1031820327 202 EsGTAVLFVTHDLALAAERADRIMVFRQGEIQEQGATE---------TIVQRPQH 247
Cdd:NF000106 193 D-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDelktkvggrTLQIRPAH 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-269 |
2.74e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEWreVVHNISFSIQRGEMLAFVGESGSGKTT---TAQAIIGLLadnarrdAGRIVLNGEVISDWSD 80
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPL--VLRGVSFRIAPREKVGIVGRTGSGKSTlllTFMRMVEVC-------GGEIRVNGREIGAYGL 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 81 KRLNRLrgvsISLVPQDP----GnslnpvkTIGQQVEEILRlhqsLSAAErrqqVLNLLAKVGL----SHPEQRFDQypH 152
Cdd:PTZ00243 1380 RELRRQ----FSMIPQDPvlfdG-------TVRQNVDPFLE----ASSAE----VWAALELVGLrervASESEGIDS--R 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMK----QRVLIAIAIAL---QPDLIIADEPTS----ALDVTVQKRILDLLdilrreSGTAVLFVTHDLALAAErA 221
Cdd:PTZ00243 1439 VLEGGSNysvgQRQLMCMARALlkkGSGFILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQ-Y 1511
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1031820327 222 DRIMVFRQGEIQEQGATETIVQRPQhpytrQLLHDLQDApLGLTAARH 269
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPRELVMNRQ-----SIFHSMVEA-LGRSEAKR 1553
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
302-493 |
3.49e-05 |
|
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: 44.49 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 302 EVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIdaghlsreaqrqlrrkiqfvyqnpfasldprqrlfaiie 381
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI--------------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 382 eplknferlsaatrrqrvesvaaRVALAPELLSrtpreLSGGQRQRVAIARALILEPAILVLDEATSALDVTVQAQILAL 461
Cdd:cd03222 62 -----------------------TPVYKPQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|..
gi 1031820327 462 LQQLQQQLGLSYLFITHDLATVRRIADSVTVL 493
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
102-383 |
7.38e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPVKTIGQQVEEILrlhQSLsaaerrQQVLNLLAKVGLSH--PEQRFDQyphqLSGGMKQRVliAIAIALQPDLI---- 175
Cdd:PRK00635 436 LSQLPSKSLSIEEVL---QGL------KSRLSILIDLGLPYltPERALAT----LSGGEQERT--ALAKHLGAELIgity 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 176 IADEPTSALDVTVQKRILDLLDILRrESGTAVLFVTHDLALAAeRADRIM-------VFrQGEIQEQGATETIVQRPQHP 248
Cdd:PRK00635 501 ILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEHDEQMIS-LADRIIdigpgagIF-GGEVLFNGSPREFLAKSDSL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 249 YTRQLLHDLQdapLGLTAARHRPLATpairvegiskrFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTLARILL- 327
Cdd:PRK00635 578 TAKYLRQELT---IPIPEKRTNSLGT-----------LTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINDTLv 643
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031820327 328 -GFER-ADAGQVTIDGIDAG------HLSREAQRQLRRKIQFVYQNPFaslDPRQRLFAiiEEP 383
Cdd:PRK00635 644 pAVEEfIEQGFCSNLSIQWGaisrlvHITRDLPGRSQRSIPLTYIKAF---DDLRELFA--EQP 702
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-189 |
8.41e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSRGEwrEVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLADNarrdaGRIVLNGeviSDWSDKRL 83
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-----GDIQIDG---VSWNSVPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 84 NRLRGvSISLVPQDPGNSLNPvktigqqveeiLRLHQSLSAAERRQQVLNLLAKVGLshpEQRFDQYPHQ---------- 153
Cdd:cd03289 73 QKWRK-AFGVIPQKVFIFSGT-----------FRKNLDPYGKWSDEEIWKVAEEVGL---KSVIEQFPGQldfvlvdggc 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 1031820327 154 -LSGGMKQRVLIAIAIALQPDLIIADEPTSALD-VTVQ 189
Cdd:cd03289 138 vLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-243 |
1.46e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 14 RSRGEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnaRRDAGRIVLNGEVISDWSdkrLNRLRGVsISL 93
Cdd:PLN03130 1246 RYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV----ELERGRILIDGCDISKFG---LMDLRKV-LGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 94 VPQ-------------DPGNSLNPVKTIgqqvEEILRLHqsLSAAERRQQvLNLLAKVglSHPEQRFdqyphqlSGGmkQ 160
Cdd:PLN03130 1318 IPQapvlfsgtvrfnlDPFNEHNDADLW----ESLERAH--LKDVIRRNS-LGLDAEV--SEAGENF-------SVG--Q 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 161 RVLIAIAIAL--QPDLIIADEPTSALDV----TVQKRIldlldilRRE--SGTaVLFVTHDLALAAErADRIMVFRQGEI 232
Cdd:PLN03130 1380 RQLLSLARALlrRSKILVLDEATAAVDVrtdaLIQKTI-------REEfkSCT-MLIIAHRLNTIID-CDRILVLDAGRV 1450
|
250
....*....|.
gi 1031820327 233 QEQGATETIVQ 243
Cdd:PLN03130 1451 VEFDTPENLLS 1461
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
296-454 |
1.66e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGF--ERADAGqVTIDGIDA--GHLSREAQRQLRRKIQFvyQNPFaslD 371
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElpPRSDAS-VVIRGTVAyvPQVSWIFNATVRDNILF--GSPF---D 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 372 PRQRLFAIieeplknferlsaatrrqRVESVAARVALAP-----ELLSRTPrELSGGQRQRVAIARALILEPAILVLDEA 446
Cdd:PLN03130 707 PERYERAI------------------DVTALQHDLDLLPggdltEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
....*...
gi 1031820327 447 TSALDVTV 454
Cdd:PLN03130 768 LSALDAHV 775
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
268-451 |
2.25e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 268 RHRPLATPAIRVEGISKRFS-LGKQALQALDSVSFEvrrGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGIDAgH 346
Cdd:TIGR01257 920 RELPGLVPGVCVKNLVKIFEpSGRPAVDRLNITFYE---NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 347 LSREAQRQlrrkiqfvyqnpFASLDPRQRLF---AIIEEPLKNFERLSAATRRQ---RVESVAARVALAPELlSRTPREL 420
Cdd:TIGR01257 996 TNLDAVRQ------------SLGMCPQHNILfhhLTVAEHILFYAQLKGRSWEEaqlEMEAMLEDTGLHHKR-NEEAQDL 1062
|
170 180 190
....*....|....*....|....*....|.
gi 1031820327 421 SGGQRQRVAIARALILEPAILVLDEATSALD 451
Cdd:TIGR01257 1063 SGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
277-451 |
3.19e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 42.53 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 277 IRVEGISKRFSLGKQALqaLDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADaGQVTIDGIDAGHLSREAQRQ-- 354
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 355 --LRRKIqFVYQNPF-ASLDPRQRLFAiiEEPLKNFERLSAatrRQRVESVAARVALapeLLSRTPRELSGGQRQRVAIA 431
Cdd:cd03289 80 gvIPQKV-FIFSGTFrKNLDPYGKWSD--EEIWKVAEEVGL---KSVIEQFPGQLDF---VLVDGGCVLSHGHKQLMCLA 150
|
170 180
....*....|....*....|
gi 1031820327 432 RALILEPAILVLDEATSALD 451
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLD 170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
102-322 |
3.87e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 LNPV-KTIGQQV-EEILrlhqslsaaERrqqvLNLLAKVGLSH--PEQRFDQyphqLSGGMKQRVLIA--IAIALQPDLI 175
Cdd:TIGR00630 450 LTPEeKKIAEEVlKEIR---------ER----LGFLIDVGLDYlsLSRAAGT----LSGGEAQRIRLAtqIGSGLTGVLY 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 176 IADEPTSALDvtvQKRILDLLDILR--RESGTAVLFVTHDlALAAERADRIM-------VFrQGEIQEQGATETIVQRPq 246
Cdd:TIGR00630 513 VLDEPSIGLH---QRDNRRLINTLKrlRDLGNTLIVVEHD-EDTIRAADYVIdigpgagEH-GGEVVASGTPEEILANP- 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031820327 247 HPYTRQLLhdlqdaplgltaARHRPLATPAIRVEGISKRFSLGKQALQALDSVSFEVRRGSTHALVGESGSGKTTL 322
Cdd:TIGR00630 587 DSLTGQYL------------SGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
296-453 |
4.51e-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: 43.36 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 296 LDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVTIDGidaghlsreaqrqlrrKIQFVYQNPFasldprqr 375
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTSW-------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 376 lfaIIEEPLKNFERLSAATRRQRVESVAARVALApELLSRTPRE-----------LSGGQRQRVAIARALILEPAILVLD 444
Cdd:TIGR01271 498 ---IMPGTIKDNIIFGLSYDEYRYTSVIKACQLE-EDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
....*....
gi 1031820327 445 EATSALDVT 453
Cdd:TIGR01271 574 SPFTHLDVV 582
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-236 |
5.74e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 30 IQRGEMLAFVGESGSGKTTTAQAIIGLLADNARRDAGRIVLNGEVISDWsdkrLNRLRGVSISlvpqdpgNSLN----PV 105
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEI----KKHYRGDVVY-------NAETdvhfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 106 KTIGQQVEEILRLH------QSLSAAERRQQVLNL-LAKVGLSHPEQRF--DQYPHQLSGGMKQRVLIAIAIALQPDLII 176
Cdd:TIGR00956 153 LTVGETLDFAARCKtpqnrpDGVSREEYAKHIADVyMATYGLSHTRNTKvgNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031820327 177 ADEPTSALDVTVQKRILDLLDILRRESGTAVLFVTHDLALAA-ERADRIMVFRQGEIQEQG 236
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAyELFDKVIVLYEGYQIYFG 293
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
497-529 |
7.13e-04 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 38.88 E-value: 7.13e-04
10 20 30
....*....|....*....|....*....|...
gi 1031820327 497 QVVEHGDVNRLFAAPQQAYTRELIAAIPQVSSR 529
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKR 33
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
24-196 |
9.44e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 24 HNISFSIQRGeMLAFVGESGSGKTTTAQAIIGLLADNARRDA-----------GRIVLNGEVIS------DWSDKRLNRL 86
Cdd:COG3950 17 LEIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLDdvkfrkllirnGEFGDSAKLILyygtsrLLLDGPLKKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 87 RGVSISLVPQ--------DPGNSLNPVKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVgLSHPEQ-RFDQYP------ 151
Cdd:COG3950 96 ERLKEEYFSRldgydsllDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREALNKL-LPDFKDiRIDRDPgrlvil 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031820327 152 ---------HQLSGGMKQRVLIAIAIALQ-----PDLIIA---------DEPTSALDVTVQKRILDLL 196
Cdd:COG3950 175 dkngeelplNQLSDGERSLLALVGDLARRlaelnPALENPlegegivliDEIDLHLHPKWQRRILPDL 242
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-255 |
1.15e-03 |
|
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: 37.38 E-value: 1.15e-03
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-250 |
1.33e-03 |
|
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: 40.66 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 4 LSVEDLRISYRSrgEWREVVHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLLadnarrDA--GRIVLNGeviSDWSDK 81
Cdd:cd03288 20 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV------DIfdGKIVIDG---IDISKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 82 RLNRLRGvSISLVPQDP----GN---SLNPVKTIGQQveeilRLHQSLSAAERRQQVLNLLAkvGLshpEQRFDQYPHQL 154
Cdd:cd03288 89 PLHTLRS-RLSIILQDPilfsGSirfNLDPECKCTDD-----RLWEALEIAQLKNMVKSLPG--GL---DAVVTEGGENF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 155 SGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQkrildllDILRRESGTAvlFVTHDLALAAER------ADRIMVFR 228
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-------NILQKVVMTA--FADRTVVTIAHRvstildADLVLVLS 228
|
250 260
....*....|....*....|..
gi 1031820327 229 QGEIQEQGATETIVQRPQHPYT 250
Cdd:cd03288 229 RGILVECDTPENLLAQEDGVFA 250
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
276-451 |
1.53e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 276 AIRVEGISKRFSLGKqalqALDSVSFEVRRGSTHALVGESGSGKTTLARILLGFERADAGQVtidgidagHLSREAQrql 355
Cdd:PRK15064 319 ALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENAN--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 356 rrkIQFVYQNPFASLDprqrlfaiieEPLKNFERLSAATRR----QRVESVAARVALAPELLSRTPRELSGGQRQRVAIA 431
Cdd:PRK15064 384 ---IGYYAQDHAYDFE----------NDLTLFDWMSQWRQEgddeQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 1031820327 432 RALILEPAILVLDEATSALD 451
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-232 |
1.59e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 23 VHNISFSIQRGEMLAFVGESGSGKTTTAQAIIGLladnARRDAGRIVLNGEVISDWS-DKRLNRlrgvSISLVPQDPgns 101
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI----REKSAGTITLHGKKINNHNaNEAINH----GFALVTEER--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 102 lnpvKTIGQQVEEILRLHQSLSAAERRQQVLNLLAKVGLSHPEQ------RFDQYPHQ-----LSGGMKQRVLIAIAIAL 170
Cdd:PRK10982 333 ----RSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQwvidsmRVKTPGHRtqigsLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031820327 171 QPDLIIADEPTSALDVTVQKRILDLLDILRREsGTAVLFVTHDLALAAERADRIMVFRQGEI 232
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
310-385 |
2.71e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 2.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820327 310 ALVGESGSGKTTLARILL-GFERADAGQVTIDGIDAGhlsreAQRQLRRKIQFVYQNPFASLDPRQRLFAIIEEPLK 385
Cdd:pfam13401 9 VLTGESGTGKTTLLRRLLeQLPEVRDSVVFVDLPSGT-----SPKDLLRALLRALGLPLSGRLSKEELLAALQQLLL 80
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
275-337 |
3.69e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 3.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031820327 275 PAIRVEGISkrfSLGKQALQALDSVsfeVRRGSTHALVGESGSGKTTLARILLGFERADAGQV 337
Cdd:PRK01889 170 PGVPVLAVS---ALDGEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
36-95 |
3.96e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 39.11 E-value: 3.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 36 LAFVGESGSGKTTTAQAIigLLADNARRDAGRiVLNGEVISDWSDKRLNRLRGVSISLVP 95
Cdd:cd04170 2 IALVGHSGSGKTTLAEAL--LYATGAIDRLGR-VEDGNTVSDYDPEEKKRKMSIETSVAP 58
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
153-213 |
4.37e-03 |
|
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: 38.74 E-value: 4.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820327 153 QLSGGMKqrVLIAIAIAL--------QPDLIIADEPTSALDV-TVQKRILDLLDILRRESGTAVLFVTHD 213
Cdd:cd03240 115 RCSGGEK--VLASLIIRLalaetfgsNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
154-212 |
4.58e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 39.73 E-value: 4.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1031820327 154 LSGGMKQRVLIAIAIALQPDLIIADEPTSALDVTVQKRILDLLdilrRESGTAVLFVTH 212
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| |
