|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-323 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 638.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKKYFPIKKGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD 80
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADLKESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGG 160
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 241 SEDLYTKPAHPYTQALLSSMPEPDPTnAGKERIILEGEVPSPLNSPSGCKFRTRCKFATEKCAQEVPKMVEIAKGHQVAC 320
Cdd:COG4608 242 RDELYARPLHPYTQALLSAVPVPDPE-RRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQVAC 320
|
...
gi 1078707893 321 HLF 323
Cdd:COG4608 321 HLA 323
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-322 |
0e+00 |
|
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: 533.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD---VTSGNILFDGKDIA 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 DLKESELKDYR-KRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLK--EEHLYRYPHEFSG 159
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 240 DSEDLYTKPAHPYTQALLSSMPEPDPtnAGKERIILEGEVPSPLNSPSGCKFRTRCKFATEKCAQEVPKMVEIAKGHQVA 319
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRLDP--DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVA 311
|
...
gi 1078707893 320 CHL 322
Cdd:COG0444 312 CHL 314
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-266 |
5.24e-155 |
|
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: 443.96 E-value: 5.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKKYFPIkkglfgRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIA 82
Cdd:COG1123 257 AEPLLEVRNLSKRYPV------RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 DLKESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQR 162
Cdd:COG1123 331 KLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|....
gi 1078707893 243 DLYTKPAHPYTQALLSSMPEPDPT 266
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-321 |
1.66e-152 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 430.54 E-value: 1.66e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGLFgRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK11308 5 LLQAIDLKKHYPVKRGLF-KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRI 165
Cdd:PRK11308 84 PEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 246 TKPAHPYTQALLSSMPEPDPTNAgKERIILEGEVPSPLNSPSGCKFRTRCKFATEKCAQEVPKMVEIAkGHQVACH 321
Cdd:PRK11308 244 NNPRHPYTQALLSATPRLNPDDR-RERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYD-GRLVACF 317
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-320 |
2.00e-150 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 425.66 E-value: 2.00e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIK--KGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:PRK15079 8 LLEVADLKVHFDIKdgKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNI-HGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQR 162
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 243 DLYTKPAHPYTQALLSSMPEPDPTNAGKERI-ILEGEVPSPLNSPSGCKFRTRCKFATEKCAQEVPKMvEIAKGHQVAC 320
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLERNKTIqLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL-EGSFRHAVSC 325
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-264 |
2.53e-147 |
|
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: 424.87 E-value: 2.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDvTSGNILFDGKDIADLK 85
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHG-SYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQR 164
Cdd:COG4172 354 RRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250 260
....*....|....*....|
gi 1078707893 245 YTKPAHPYTQALLSSMPEPD 264
Cdd:COG4172 514 FDAPQHPYTRALLAAAPLLE 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-239 |
2.79e-130 |
|
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: 370.30 E-value: 2.79e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQ-KEIILDLLKKVGLKEEHLYRYPHEFSGGQRQR 164
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEArKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-259 |
2.36e-120 |
|
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: 346.02 E-value: 2.36e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlK 85
Cdd:COG1124 1 MLEVRNLSVSY-------GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQkeiILDLLKKVGLKEEHLYRYPHEFSGGQRQRI 165
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....
gi 1078707893 246 TKPAHPYTQALLSS 259
Cdd:COG1124 228 AGPKHPYTRELLAA 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-281 |
1.45e-103 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 316.03 E-value: 1.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPIKKGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQ 163
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSED 243
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
250 260 270
....*....|....*....|....*....|....*...
gi 1078707893 244 LYTKPAHPYTQALLSSMPEPDPTNAGKERIILEGEVPS 281
Cdd:PRK10261 551 VFENPQHPYTRKLMAAVPVADPSRQRPQRVLLSDDLPS 588
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-278 |
5.72e-103 |
|
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: 311.62 E-value: 5.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD----VTSGNILF 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAF-------GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 77 DGKDIADLKESELKDYR-KRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLK--EEHLYRY 153
Cdd:COG4172 74 DGQDLLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdpERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 154 PHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLG 233
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1078707893 234 NIVEIADSEDLYTKPAHPYTQALLSSMP--EPDPTNAGKErIILEGE 278
Cdd:COG4172 234 EIVEQGPTAELFAAPQHPYTRKLLAAEPrgDPRPVPPDAP-PLLEAR 279
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-259 |
2.47e-89 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 267.86 E-value: 2.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPIKKGLFGRKteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIad 83
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRRQ--QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 lkesELKDYRKRMQ---IIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGG 160
Cdd:COG4167 78 ----EYGDYKYRCKhirMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*....
gi 1078707893 241 SEDLYTKPAHPYTQALLSS 259
Cdd:COG4167 234 TAEVFANPQHEVTKRLIES 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-258 |
1.56e-88 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 274.66 E-value: 1.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDvTSGNILFDGKDIADLK 85
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIH-GSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQR 164
Cdd:PRK15134 354 RRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
250
....*....|....
gi 1078707893 245 YTKPAHPYTQALLS 258
Cdd:PRK15134 514 FAAPQQEYTRQLLA 527
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-321 |
1.63e-85 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 260.43 E-value: 1.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPIKKGLfgrkteqLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRL---HDVTSGNILFDGKD 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADLKESELKDYR-KRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEH--LYRYPHEF 157
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARkrMKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVE 237
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 238 IADSEDLYTKPAHPYTQALLSSMPEPDptNAGKERIILEGEVPSPLNSPSGCKFRTRCKFATEKCaQEVPKMVEIAKGHQ 317
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRLD--AEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-SSAPPLEEFGPGRL 319
|
....
gi 1078707893 318 VACH 321
Cdd:PRK09473 320 RACF 323
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-321 |
1.46e-80 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 247.73 E-value: 1.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD----VTSGNILFDGKDIADLKESELKDY-RKRMQ 97
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLvGAEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 98 IIFQDPYASLNPTMNV-FQIIsEPMNIHGSYEKEEQKEIILDLLKKVGLK--EEHLYRYPHEFSGGQRQRISIARALSVK 174
Cdd:PRK11022 93 MIFQDPMTSLNPCYTVgFQIM-EAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 175 PDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQ 254
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 255 ALLSSMPEpdpTNAGKERII-LEGEVPSPLNSPSGCKFRTRCKFATEKCAQEVPKMVEIAkGHQVACH 321
Cdd:PRK11022 252 ALLRALPE---FAQDKARLAsLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA-GRQSKCH 315
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-265 |
3.09e-79 |
|
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: 242.02 E-value: 3.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpiKKGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRI 165
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
250 260
....*....|....*....|
gi 1078707893 246 TKpAHPYTQALLSSMPEPDP 265
Cdd:TIGR02769 240 SF-KHPAGRNLQSAVLPEHP 258
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-276 |
1.17e-76 |
|
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: 243.27 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfgrkTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVT---SGNILFDGKD 80
Cdd:COG1123 2 TPLLEVRDLSVRYP---------GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADLKESELkdyRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSyeKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGG 160
Cdd:COG1123 73 LLELSEALR---GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLS--RAEARARVLELLEAVGL-ERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 1078707893 241 SEDLYTKPAHPYTQALLSSMPEPDPTNAGKERIILE 276
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLE 262
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-273 |
1.12e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 230.35 E-value: 1.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:COG1135 2 IELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:COG1135 75 RELRAARRKIGMIFQH--FNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYT 246
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250 260
....*....|....*....|....*..
gi 1078707893 247 KPAHPYTQALLSSMPEPDPTNAGKERI 273
Cdd:COG1135 231 NPQSELTRRFLPTVLNDELPEELLARL 257
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-265 |
4.41e-70 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 226.90 E-value: 4.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV-----TSGNILFDGKDIADLKESELKDYR-KRM 96
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHASEQTLRGVRgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 97 QIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKE--EHLYRYPHEFSGGQRQRISIARALSVK 174
Cdd:PRK15134 95 AMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQaaKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 175 PDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQ 254
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
250
....*....|.
gi 1078707893 255 ALLSSMPEPDP 265
Cdd:PRK15134 255 KLLNSEPSGDP 265
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-252 |
2.09e-68 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 217.27 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:COG3842 5 ALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 EselkdYRKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:COG3842 74 P-----EKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHD----LSMvrhiSDRIGVMYLGNIVEIADS 241
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVGTP 220
|
250
....*....|.
gi 1078707893 242 EDLYTKPAHPY 252
Cdd:COG3842 221 EEIYERPATRF 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-321 |
3.33e-68 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 216.31 E-value: 3.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 5 NLIEVRNLKKYFPIKKGLfgrkteqLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD----VTSGNILFDGKD 80
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGR-------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADLKESELKDY-RKRMQIIFQDPYASLNPTMNVFQIISEPMNiHGSYE------KEEQKEIILDLLKKVGLKEEHLYR- 152
Cdd:COG4170 75 LLKLSPRERRKIiGREIAMIFQEPSSCLDPSAKIGDQLIEAIP-SWTFKgkwwqrFKWRKKRAIELLHRVGIKDHKDIMn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 -YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMY 231
Cdd:COG4170 154 sYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 232 LGNIVEIADSEDLYTKPAHPYTQALLSSMPEPDPTNAGKERI-ILEGEVPSPLNSPSGCKFRTRCKFATEKCAQeVPKMV 310
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLnTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVE-TPRLR 312
|
330
....*....|.
gi 1078707893 311 EIaKGHQVACH 321
Cdd:COG4170 313 KI-KGHEFACH 322
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-259 |
1.14e-67 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 212.73 E-value: 1.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPIKKGLFGRktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIad 83
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 lkesELKDYRKRMQ---IIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGG 160
Cdd:PRK15112 78 ----HFGDYSYRSQrirMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*....
gi 1078707893 241 SEDLYTKPAHPYTQALLSS 259
Cdd:PRK15112 234 TADVLASPLHELTKRLIAG 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-265 |
1.66e-67 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 212.24 E-value: 1.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 5 NLIEVRNLKKYFPiKKGLFGRKTEQlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADL 84
Cdd:PRK10419 2 TLLNVSGLSHHYA-HGGLSGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 85 KESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQR 164
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
250 260
....*....|....*....|.
gi 1078707893 245 YTKpAHPYTQALLSSMPEPDP 265
Cdd:PRK10419 240 LTF-SSPAGRVLQNAVLPAFP 259
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-248 |
1.50e-65 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 205.89 E-value: 1.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:cd03258 1 MIELKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDpYASLNpTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLKEEHlYRYPHEFSGGQRQRI 165
Cdd:cd03258 74 GKELRKARRRIGMIFQH-FNLLS-SRTVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 1078707893 246 TKP 248
Cdd:cd03258 230 ANP 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-252 |
5.98e-65 |
|
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: 204.66 E-value: 5.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03261 1 IELRGLTKSF-------GGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHlYRYPHEFSGGQRQRIS 166
Cdd:cd03261 70 AELYRLRRRMGMLFQS--GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYT 246
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*.
gi 1078707893 247 KPaHPY 252
Cdd:cd03261 227 SD-DPL 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-257 |
1.33e-64 |
|
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: 203.67 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:COG1127 3 EPMIEVRNLTKSF-------GDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESELKDYRKRMQIIFQDP--YASlnptMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQ 161
Cdd:COG1127 72 LSEKELYELRRRIGMLFQGGalFDS----LTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALD-VSVqAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
250
....*....|....*..
gi 1078707893 241 SEDLYTKPaHPYTQALL 257
Cdd:COG1127 226 PEELLASD-DPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-235 |
4.01e-63 |
|
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: 199.25 E-value: 4.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03255 1 IELKNLSKTY-------GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYR-KRMQIIFQDPYasLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:cd03255 74 KELAAFRrRHIGFVFQSFN--LLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNI 235
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-249 |
4.57e-61 |
|
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: 194.38 E-value: 4.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03300 1 IELENVSKFY-----------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selkdYRKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:cd03300 70 -----HKRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYT 246
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
...
gi 1078707893 247 KPA 249
Cdd:cd03300 221 EPA 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-239 |
1.04e-60 |
|
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: 192.73 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKyfpikkgLFGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03259 1 LELKGLSK-------TYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selkdYRKRMQIIFQDPyaSLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:cd03259 70 -----ERRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-260 |
1.09e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 193.67 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlK 85
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQdpyaSLN--PTMNVFQIISE-PMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQR 162
Cdd:COG1126 69 KKDINKLRRKVGMVFQ----QFNlfPHLTVLENVTLaPIKVKK-MSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
250
....*....|....*...
gi 1078707893 243 DLYTKPAHPYTQALLSSM 260
Cdd:COG1126 222 EFFENPQHERTRAFLSKV 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-259 |
1.17e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 196.95 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:PRK11153 2 IELKNISKVFPQGGR-------TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQdpYASLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:PRK11153 75 KELRKARRQIGMIFQ--HFNLLSSRTVFDNVALPLELAGT-PKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYT 246
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
250
....*....|...
gi 1078707893 247 KPAHPYTQALLSS 259
Cdd:PRK11153 231 HPKHPLTREFIQS 243
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-252 |
3.84e-60 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 194.54 E-value: 3.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:COG1125 2 IEFENVTKRYP----------DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELkdyRKRMQIIFQDpyASLNPTMNVFQiisepmNIH------GsYEKEEQKEIILDLLKKVGLK-EEHLYRYPHEFSG 159
Cdd:COG1125 72 VEL---RRRIGYVIQQ--IGLFPHMTVAE------NIAtvprllG-WDKERIRARVDELLELVGLDpEEYRDRYPHELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:COG1125 140 GQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYD 219
|
250
....*....|...
gi 1078707893 240 DSEDLYTKPAHPY 252
Cdd:COG1125 220 TPEEILANPANDF 232
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-321 |
9.70e-60 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 194.25 E-value: 9.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD----VTSGNILFDGKDI 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG-------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADLKESEL-KDYRKRMQIIFQDPYASLNPTMNV-FQIISepmNIHGSYEKEE-------QKEIILDLLKKVGLKEEH--L 150
Cdd:PRK15093 76 LRLSPRERrKLVGHNVSMIFQEPQSCLDPSERVgRQLMQ---NIPGWTYKGRwwqrfgwRKRRAIELLHRVGIKDHKdaM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 151 YRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 231 YLGNIVEIADSEDLYTKPAHPYTQALLSSMPEPDPTNAGKERI-ILEGEVPSPLNSPSGCKFRTRCKFATEKCAqEVPKM 309
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLnTLPGAIPLLEHLPIGCRLGPRCPYAQRECI-ETPRL 311
|
330
....*....|..
gi 1078707893 310 VEIaKGHQVACH 321
Cdd:PRK15093 312 TGA-KNHLYACH 322
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-262 |
1.35e-59 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 201.24 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGK----------DIADLKESELKDY 92
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 93 R-KRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEH--LYRYPHEFSGGQRQRISIAR 169
Cdd:PRK10261 102 RgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 170 ALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPA 249
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
250
....*....|...
gi 1078707893 250 HPYTQALLSSMPE 262
Cdd:PRK10261 262 HPYTRALLAAVPQ 274
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-252 |
2.55e-59 |
|
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: 190.20 E-value: 2.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfGRKteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03295 1 IEFENVTKRYG------GGK----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELkdyRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLKEEHLY-RYPHEFSGGQRQRI 165
Cdd:cd03295 71 VEL---RRKIGYVIQQ--IGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGLDPAEFAdRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
....*..
gi 1078707893 246 TKPAHPY 252
Cdd:cd03295 225 RSPANDF 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-237 |
4.72e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 189.10 E-value: 4.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTgrsiirLH------DVTSGNILFD 77
Cdd:COG1136 2 SPLLELRNLTKSY-------GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL------LNilggldRPTSGEVLID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 78 GKDIADLKESELKDYRKRmQI--IFQDPYasLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPH 155
Cdd:COG1136 69 GQDISSLSERELARLRRR-HIgfVFQFFN--LLPELTALENVALPLLLAG-VSRKERRERARELLERVGL-GDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNI 235
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
..
gi 1078707893 236 VE 237
Cdd:COG1136 223 VS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-230 |
6.47e-59 |
|
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: 188.45 E-value: 6.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLke 86
Cdd:cd03293 1 LEVRNVSKTY-------GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selkdyRKRMQIIFQDPyaSLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLKEeHLYRYPHEFSGGQRQRIS 166
Cdd:cd03293 72 ------GPDRGYVFQQD--ALLPWLTVLDNVALGLELQGV-PKAEARERAEELLELVGLSG-FENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-252 |
5.54e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 187.59 E-value: 5.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:COG3839 4 LELENVSKSY-------GGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selkdyRKR---MqiIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQ 163
Cdd:COG3839 73 ------KDRniaM--VFQS-YA-LYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHD----LSMvrhiSDRIGVMYLGNIVEIA 239
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVG 216
|
250
....*....|...
gi 1078707893 240 DSEDLYTKPAHPY 252
Cdd:COG3839 217 TPEELYDRPANLF 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-253 |
9.71e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 186.89 E-value: 9.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlke 86
Cdd:COG1118 3 IEVRNISKRFG-----------SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpYAsLNPTMNVFQiisepmNI-----HGSYEKEEQKEIILDLLKKVGLkeEHL-YRYPHEFSGG 160
Cdd:COG1118 68 TNLPPRERRVGFVFQH-YA-LFPHMTVAE------NIafglrVRPPSKAEIRARVEELLELVQL--EGLaDRYPSQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
250
....*....|...
gi 1078707893 241 SEDLYTKPAHPYT 253
Cdd:COG1118 218 PDEVYDRPATPFV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-252 |
2.63e-56 |
|
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: 183.61 E-value: 2.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYF--------PIKKGLFGR-----KTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGN 73
Cdd:cd03294 1 IKIKGLYKIFgknpqkafKLLAKGKSKeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 74 ILFDGKDIADLKESELKDYR-KRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYR 152
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRrKKISMVFQS-FA-LLPHRTVLENVAFGLEVQG-VPRAEREERAAEALELVGL-EGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
250 260
....*....|....*....|
gi 1078707893 233 GNIVEIADSEDLYTKPAHPY 252
Cdd:cd03294 237 GRLVQVGTPEEILTNPANDY 256
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-230 |
2.14e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 180.67 E-value: 2.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 2 HEENLIEVRNLKKYFPIKKGlfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI 81
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADLkeselkdyRKRMQIIFQDPyaSLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQ 161
Cdd:COG1116 76 TGP--------GPDRGVVFQEP--ALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGL-AGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALDvsvqAQVVNMLQD----IQEETGVTYLFIAHDLS-MVRhISDRIGVM 230
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALD----ALTRERLQDellrLWQETGKTVLFVTHDVDeAVF-LADRVVVL 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-236 |
2.28e-55 |
|
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: 180.19 E-value: 2.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKglfgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----------QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDpYAsLNPTMNVFQ-IISEPMNIHGSYE------KEEQKEIILDLLKKVGLKEEHLYRyPHEFS 158
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQH-YN-LIERLTVLEnVLHGRLGYKPTWRsllgrfSEEDKERALSALERVGLADKAYQR-ADQLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 159 GGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-254 |
4.81e-55 |
|
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: 183.13 E-value: 4.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 25 RKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDY-RKRMQIIFQDp 103
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 yASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:TIGR01186 80 -FALFPHMTILQNTSLGPELLG-WPEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 184 ISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQ 254
Cdd:TIGR01186 157 FSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-236 |
3.36e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.56 E-value: 3.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:COG3638 2 MLELRNLSKRYP------GGTP----ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRMQIIFQDPYasLNPTMNVFQ--------IISEPMNIHGSYEKEEqKEIILDLLKKVGLkEEHLYRYPHEF 157
Cdd:COG3638 72 GRALRRLRRRIGMIFQQFN--LVPRLSVLTnvlagrlgRTSTWRSLLGLFPPED-RERALEALERVGL-ADKAYQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-235 |
7.16e-54 |
|
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: 175.41 E-value: 7.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIaDLKE 86
Cdd:cd03262 1 IEIKNLHKSF-----------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpyASLNPTMNVFQIISE-PMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:cd03262 69 KNINELRQKVGMVFQQ--FNLFPHLTVLENITLaPIKVKGM-SKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-252 |
3.16e-53 |
|
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: 174.45 E-value: 3.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlke 86
Cdd:cd03296 3 IEVRNVSKRFG-----------DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selKDYRKRmQI--IFQDpYAsLNPTMNVFQIISEPMNIHGSYEKEEQKEI---ILDLLKKVGLkeEHLY-RYPHEFSGG 160
Cdd:cd03296 69 ---VPVQER-NVgfVFQH-YA-LFRHMTVFDNVAFGLRVKPRSERPPEAEIrakVHELLKLVQL--DWLAdRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
250
....*....|..
gi 1078707893 241 SEDLYTKPAHPY 252
Cdd:cd03296 221 PDEVYDHPASPF 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-244 |
3.76e-53 |
|
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: 173.91 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV-----TSGNILFDGKDI 81
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADLKESELKdYRKRMQIIFQDPyaslNP-TMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYR-YPHEFSG 159
Cdd:cd03260 70 YDLDVDVLE-LRRRVGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETgvTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 1078707893 240 DSEDL 244
Cdd:cd03260 223 PTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-244 |
8.93e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.33 E-value: 8.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlke 86
Cdd:COG1131 1 IEVRGLTKRY-------GDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 sELKDYRKRMQIIFQDPyaSLNPTMNVFQIIsepmNIHGSY---EKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQ 163
Cdd:COG1131 67 -DPAEVRRRIGYVPQEP--ALYPDLTVRENL----RFFARLyglPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSED 243
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
.
gi 1078707893 244 L 244
Cdd:COG1131 218 L 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-230 |
6.16e-52 |
|
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: 169.29 E-value: 6.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkE 86
Cdd:cd03229 1 LELKNVSKRYG-----------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-E 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDPyaSLNPTMNVFQIISEPMnihgsyekeeqkeiildllkkvglkeehlyryphefSGGQRQRIS 166
Cdd:cd03229 69 DELPPLRRRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-236 |
6.39e-52 |
|
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: 171.21 E-value: 6.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKglfgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03256 1 IEVENLSKTYPNGK----------KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDPyaSLNPTMNVFQ-IISEPMNIHGSYE------KEEQKEIILDLLKKVGLkEEHLYRYPHEFSG 159
Cdd:cd03256 71 KALRQLRRQIGMIFQQF--NLIERLSVLEnVLSGRLGRRSTWRslfglfPKEEKQRALAALERVGL-LDKAYQRADQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-239 |
2.85e-51 |
|
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: 168.59 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKglfgrkteqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03301 1 VELENVTKRFGNVT-----------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SElkdyrKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:cd03301 70 KD-----RDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-258 |
9.99e-51 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 168.68 E-value: 9.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKKYFpikkglfGRKteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV-----TSGNILFD 77
Cdd:COG1117 8 LEPKIEVRNLNVYY-------GDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 78 GKDIADlKESELKDYRKRMQIIFQDPyaslNP-TMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEE---HLYRY 153
Cdd:COG1117 77 GEDIYD-PDVDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEvkdRLKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 154 PHEFSGGQRQRISIARALSVKPDFILCDEPISALD-VSVqAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYL 228
|
250 260
....*....|....*....|....*.
gi 1078707893 233 GNIVEIADSEDLYTKPAHPYTQALLS 258
Cdd:COG1117 229 GELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-237 |
1.85e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.77 E-value: 1.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKglfgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:COG2884 2 IRFENVSKRYPGGR----------EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:COG2884 72 REIPYLRRRIGVVFQD--FRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVE 237
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-230 |
2.34e-50 |
|
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: 166.10 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQD 102
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PYASL-NPTmnVFQ-IISEPMNIHgsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILC 180
Cdd:cd03225 84 PDDQFfGPT--VEEeVAFGLENLG--LPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-248 |
4.75e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 165.97 E-value: 4.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlKE 86
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDPYAslnptmnvfQIISE---------PMNIhgSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEF 157
Cdd:COG1122 68 KNLRELRRKVGLVFQNPDD---------QLFAPtveedvafgPENL--GLPREEIRERVEEALELVGL-EHLADRPPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVE 237
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|.
gi 1078707893 238 IADSEDLYTKP 248
Cdd:COG1122 215 DGTPREVFSDY 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
48-284 |
2.95e-48 |
|
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: 164.59 E-value: 2.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 48 LVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlkeSELKDYRKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGSy 127
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 128 EKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETG 207
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 208 VTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALL--SSMPEPDPTNAGKERIILEGEVPSPLN 284
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIgeINVFEATVIERKSEQVVLAGVEGRRCD 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-257 |
2.98e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 159.10 E-value: 2.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK09493 1 MIEFKNVSKHF-----------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESElKDYRKRMQIIFQDPYasLNPTMNVFQ-IISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQR 164
Cdd:PRK09493 70 VDE-RLIRQEAGMVFQQFY--LFPHLTALEnVMFGPLRVRGA-SKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
250
....*....|...
gi 1078707893 245 YTKPAHPYTQALL 257
Cdd:PRK09493 224 IKNPPSQRLQEFL 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-236 |
2.64e-46 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 157.13 E-value: 2.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKkyfpikkglFGRKTEQLkaVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:COG1120 1 MLEAENLS---------VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELkdyRKRMQIIFQDPYASLNptMNVFQIISepmniHGSY--------EKEEQKEIILDLLKKVGLkeEHL-YRYPHE 156
Cdd:COG1120 70 RREL---ARRIAYVPQEPPAPFG--LTVRELVA-----LGRYphlglfgrPSAEDREAVEEALERTGL--EHLaDRPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 157 FSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-257 |
2.92e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 156.50 E-value: 2.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkGLFgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlke 86
Cdd:TIGR00968 1 IEIANISKRF----GSF-------QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDA----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHgSYEKEEQKEIILDLLKKVGLkeEHLY-RYPHEFSGGQRQRI 165
Cdd:TIGR00968 65 TRVHARDRKIGFVFQH-YA-LFKHLTVRDNIAFGLEIR-KHPKAKIKARVEELLELVQL--EGLGdRYPNQLSGGQRQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:TIGR00968 140 ALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVY 219
|
250
....*....|..
gi 1078707893 246 TKPAHPYTQALL 257
Cdd:TIGR00968 220 DHPANPFVMSFL 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-248 |
3.84e-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: 153.65 E-value: 3.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKyfpiKKGLFGRKteqlkavdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03299 1 LKVENLSK----DWKEFKLK--------NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SelkdyRKRMQIIFQDpYAsLNPTMNVFQIISEPMnIHGSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:cd03299 69 E-----KRDISYVPQN-YA-LFPHMTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYT 246
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
..
gi 1078707893 247 KP 248
Cdd:cd03299 220 KP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-183 |
8.37e-45 |
|
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: 149.72 E-value: 8.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkesELKDYRKRMQIIFQDPyaSLNPTMN 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD---ERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 113 VFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLKE---EHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:pfam00005 76 VRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-252 |
2.55e-44 |
|
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: 160.77 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKkyfpikkglFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLke 86
Cdd:COG2274 474 IELENVS---------FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI-- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 sELKDYRKRMQIIFQDPYaslnptmnVFQ--IISepmNIHGSYEKEEQKEIIlDLLKKVGLKEEhLYRYPH--------- 155
Cdd:COG2274 543 -DPASLRRQIGVVLQDVF--------LFSgtIRE---NITLGDPDATDEEII-EAARLAGLHDF-IEALPMgydtvvgeg 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 156 --EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLG 233
Cdd:COG2274 609 gsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
250
....*....|....*....
gi 1078707893 234 NIVEIADSEDLYTKPAHPY 252
Cdd:COG2274 686 RIVEDGTHEELLARKGLYA 704
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-260 |
1.22e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 153.84 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK11607 19 LLEIRNLTKSF-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 EselkdYRKRMQIIFQDpYAsLNPTMNVFQIISEPMNiHGSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:PRK11607 88 P-----YQRPINMMFQS-YA-LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
250
....*....|....*
gi 1078707893 246 TKPAHPYTQALLSSM 260
Cdd:PRK11607 239 EHPTTRYSAEFIGSV 253
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-230 |
1.48e-43 |
|
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: 147.14 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKkyfpikkglFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKe 86
Cdd:cd03228 1 IEFKNVS---------FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 seLKDYRKRMQIIFQDPYaslnptmnVFqiisepmniHGSyekeeqkeiILD-LLkkvglkeehlyryphefSGGQRQRI 165
Cdd:cd03228 71 --LESLRKNIAYVPQDPF--------LF---------SGT---------IREnIL-----------------SGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVM 230
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-257 |
1.53e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 154.04 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFP---------IKKGLFGR----KTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGN 73
Cdd:PRK10070 5 LEIKNLYKIFGehpqrafkyIEQGLSKEqileKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 74 ILFDGKDIADLKESELKDYR-KRMQIIFQDpyASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYR 152
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRrKKIAMVFQS--FALMPHMTVLDNTAFGMELAG-INAEERREKALDALRQVGL-ENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250 260
....*....|....*....|....*
gi 1078707893 233 GNIVEIADSEDLYTKPAHPYTQALL 257
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-235 |
2.47e-43 |
|
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: 146.77 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlke 86
Cdd:cd03230 1 IEVRNLSKRY-------GKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 sELKDYRKRMQIIFQDPyaSLNPTMNVfqiisepmnihgsyekeeqkeiildllkkvglkEEHLyryphEFSGGQRQRIS 166
Cdd:cd03230 67 -EPEEVKRRIGYLPEEP--SLYENLTV---------------------------------RENL-----KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-253 |
4.01e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 152.41 E-value: 4.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK09452 14 LVELRGISKSF-------DGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESelkdyRKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:PRK09452 83 AE-----NRHVNTVFQS-YA-LFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHD----LSMvrhiSDRIGVMYLGNIVEIADS 241
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGTP 229
|
250
....*....|..
gi 1078707893 242 EDLYTKPAHPYT 253
Cdd:PRK09452 230 REIYEEPKNLFV 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-227 |
4.69e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.27 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQD 102
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PYAslnPTMNVFQIISEPMNIHgsyEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDE 182
Cdd:COG4619 83 PAL---WGGTVRDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRI 227
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRV 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-238 |
7.47e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.32 E-value: 7.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPYaslnpt 110
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTF------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 mnVFQI-ISEpmNIhgSYEKEE--QKEIIlDLLKKVGLKE--EHLyryPH-----------EFSGGQRQRISIARALSVK 174
Cdd:COG1132 425 --LFSGtIRE--NI--RYGRPDatDEEVE-EAAKAAQAHEfiEAL---PDgydtvvgergvNLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 175 PDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEI 238
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-240 |
9.79e-42 |
|
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: 144.89 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikKGLfgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03219 1 LEVRGLTKRF---GGL--------VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SElkdyRKRMQII--FQDPyaSLNPTMNVFQIISEPMNIHGSY---------EKEEQKEIILDLLKKVGLkEEHLYRYPH 155
Cdd:cd03219 70 HE----IARLGIGrtFQIP--RLFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGL-ADLADRPAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
....*
gi 1078707893 236 veIAD 240
Cdd:cd03219 222 --IAE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-240 |
2.87e-41 |
|
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: 144.03 E-value: 2.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFpikkGlfGrkteqLKAVDDLSFTIKKGETFGLVGESGCGKST-----TGrsiirLHDVTSGNILFDG 78
Cdd:COG0411 2 DPLLEVRGLTKRF----G--G-----LVAVDDVSLEVERGEIVGLIGPNGAGKTTlfnliTG-----FYRPTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 79 KDIADLKESElkdyRKRMQII--FQDPyaSLNPTMNVFQ------------IISEPMNIHGSYEKEEQK--EIILDLLKK 142
Cdd:COG0411 66 RDITGLPPHR----IARLGIArtFQNP--RLFPELTVLEnvlvaaharlgrGLLAALLRLPRARREEREarERAEELLER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 143 VGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRH 222
Cdd:COG0411 140 VGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMG 218
|
250
....*....|....*...
gi 1078707893 223 ISDRIGVMYLGNIveIAD 240
Cdd:COG0411 219 LADRIVVLDFGRV--IAE 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-259 |
3.10e-41 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.07 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLH----DVTSGNILFDGKDIAdlkeseLKDYRKRM-QIIFQDPYASL 107
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVA------PCALRGRKiATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 108 NPTMNVFQIISEPMNIHGsyeKEEQKEIILDLLKKVGLKEEH--LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPIS 185
Cdd:PRK10418 93 NPLHTMHTHARETCLALG---KPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 186 ALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALLSS 259
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-233 |
5.77e-41 |
|
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: 140.07 E-value: 5.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 8 EVRNLKKYFPIKKglfgrkteqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKes 87
Cdd:cd00267 1 EIENLSFRYGGRT-----------ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 88 eLKDYRKRMQIIFQdpyaslnptmnvfqiisepmnihgsyekeeqkeiildllkkvglkeehlyrypheFSGGQRQRISI 167
Cdd:cd00267 68 -LEELRRRIGYVPQ-------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 168 ARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLG 233
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-245 |
8.17e-41 |
|
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: 142.37 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQD 102
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PYAsLNPTmnVFQiisepmNIHGSYEKEEQKEIIlDLLKKVGLkeehlyrypHEF-------------------SGGQRQ 163
Cdd:cd03251 85 VFL-FNDT--VAE------NIAYGRPGATREEVE-EAARAANA---------HEFimelpegydtvigergvklSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSED 243
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
..
gi 1078707893 244 LY 245
Cdd:cd03251 223 LL 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-237 |
2.95e-40 |
|
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: 140.56 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGK-------LDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYR-KRMQIIFQdpYASLNPTMNVFQIISEPMNIhGSYEKEEQKEIILDLLKKVGLKEEhLYRYPHEFSGGQRQR 164
Cdd:TIGR02211 74 SNERAKLRnKKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKSVKEAKERAYEMLEKVGLEHR-INHRPSELSGGERQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHIsDRIGVMYLGNIVE 237
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-255 |
3.60e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 140.92 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKGLFgrkteqlkavdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNIlfdgkDIADLK- 85
Cdd:PRK11124 3 IQLNGINCFYGAHQALF-----------DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGNHf 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 -------ESELKDYRKRMQIIFQDpYaSLNPTMNVFQ-IISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEF 157
Cdd:PRK11124 67 dfsktpsDKAIRELRRNVGMVFQQ-Y-NLWPHLTVQQnLIEAPCRVLG-LSKDQALARAEKLLERLRL-KPYADRFPLHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVE 237
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
250
....*....|....*...
gi 1078707893 238 IADSEDLytkpAHPYTQA 255
Cdd:PRK11124 222 QGDASCF----TQPQTEA 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
4.71e-40 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 141.22 E-value: 4.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKKYFPIKKGLfgrkteqlkavDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGK- 79
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGC-----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 80 ----DIADLKESElkdyRKRMQ-----IIFQDPYASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHL 150
Cdd:PRK11701 70 gqlrDLYALSEAE----RRRLLrtewgFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 151 YRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|....*....
gi 1078707893 231 YLGNIVEIADSEDLYTKPAHPYTQALLSS 259
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
8.94e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 8.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLkkyfpikkGL-FGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGK 79
Cdd:COG1121 1 MMMMPAIELENL--------TVsYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 80 DIadlkeselKDYRKRM----QiifqdpYASLNPT--MNVFQIIS----EPMNIHGSYEKEEqKEIILDLLKKVGLkEEH 149
Cdd:COG1121 69 PP--------RRARRRIgyvpQ------RAEVDWDfpITVRDVVLmgryGRRGLFRRPSRAD-REAVDEALERVGL-EDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 150 LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRI-- 227
Cdd:COG1121 133 ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVll 211
|
250 260
....*....|....*....|
gi 1078707893 228 ---GVMYLGNIVEIADSEDL 244
Cdd:COG1121 212 lnrGLVAHGPPEEVLTPENL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-249 |
1.06e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 142.55 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRF-------GSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADlKESELKDyrkrMQIIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLK--EEhlyRYPHEFS 158
Cdd:PRK11432 70 VTH-RSIQQRD----ICMVFQS-YA-LFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDLAgfED---RYVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 159 GGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEI 238
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
250
....*....|.
gi 1078707893 239 ADSEDLYTKPA 249
Cdd:PRK11432 219 GSPQELYRQPA 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-247 |
1.19e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 139.61 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlk 85
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 eSELKDYRKRMQIIFQDPYasLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:COG4555 67 -KEPREARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLY 245
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
..
gi 1078707893 246 TK 247
Cdd:COG4555 221 EE 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-260 |
1.46e-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: 139.58 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGLFgrkteqlkavdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCR-----------DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKRM------QIIFQDPYASLNPTMNVFQIISE-PMNIhGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFS 158
Cdd:TIGR02323 72 LYQLSEAERRRlmrtewGFVHQNPRDGLRMRVSAGANIGErLMAI-GARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 159 GGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEI 238
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
250 260
....*....|....*....|..
gi 1078707893 239 ADSEDLYTKPAHPYTQALLSSM 260
Cdd:TIGR02323 231 GLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-252 |
2.16e-39 |
|
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: 138.83 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkesELKDYRKRMQIIFQDP------- 103
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQIGLVSQEPvlfdgti 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 -----YASLNPTMNVFQIISEPMNIHgsyekeeqkEIILDLLKK----VGLKEEHLyryphefSGGQRQRISIARALSVK 174
Cdd:cd03249 94 aenirYGKPDATDEEVEEAAKKANIH---------DFIMSLPDGydtlVGERGSQL-------SGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 175 PDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTKPAHPY 252
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-227 |
6.00e-39 |
|
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: 136.77 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03292 1 IEFINVTKTYP----------NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGSYEKEEQKEiILDLLKKVGLKEEHlYRYPHEFSGGQRQRIS 166
Cdd:cd03292 71 RAIPYLRRKIGVVFQD--FRLLPDRNVYENVAFALEVTGVPPREIRKR-VPAALELVGLSHKH-RALPAELSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRI 227
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRV 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-249 |
6.77e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 140.60 E-value: 6.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:PRK10851 3 IEIANIKKSF-------GRT----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SElkdyrKRMQIIFQDpYAsLNPTMNVFQIISEPMNIHGSYEKEEQKEI---ILDLLKKVGLkeEHLY-RYPHEFSGGQR 162
Cdd:PRK10851 72 RD-----RKVGFVFQH-YA-LFRHMTVFDNIAFGLTVLPRRERPNAAAIkakVTQLLEMVQL--AHLAdRYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
....*..
gi 1078707893 243 DLYTKPA 249
Cdd:PRK10851 223 QVWREPA 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-239 |
2.11e-38 |
|
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: 135.50 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKkGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADL-KESELKDYRKRMQIIFQDpyASLNPTMNV 113
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrKKINLPPQQRKIGLVFQQ--YALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 114 FQIISEPMNIHGSYEKEEQKEIILDLLKKVGLkeehLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQA 193
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLLGLDHL----LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1078707893 194 QVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIA 239
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
33-236 |
3.09e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 133.71 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQdpyaslnptmn 112
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 vfqiisepmnihgsyekeeqkeiildLLKKVGLkeEHL-YRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:cd03214 81 --------------------------ALELLGL--AHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1078707893 192 QAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-244 |
3.57e-38 |
|
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: 135.19 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadLKE 86
Cdd:cd03265 1 IEVENLVKKY-----------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SelKDYRKRMQIIFQDPyaSLNPTMNVFqiisEPMNIHG---SYEKEEQKEIILDLLKKVGLKEEHlYRYPHEFSGGQRQ 163
Cdd:cd03265 68 P--REVRRRIGIVFQDL--SVDDELTGW----ENLYIHArlyGVPGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSED 243
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
.
gi 1078707893 244 L 244
Cdd:cd03265 219 L 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-248 |
6.14e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 136.04 E-value: 6.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 29 QLKAVDDLSFTIKKGETFGLVGESGCGKSTtgrsIIRLHDV----TSGNILFDGKDIADLKESELKDYRKRMQIIFQDPY 104
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKST----LIQHLNGllkpTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 ASLnptmnvFQ------IISEPMNIhgSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFI 178
Cdd:TIGR04521 93 HQL------FEetvykdIAFGPKNL--GLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 179 LCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKP 248
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-260 |
3.12e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 133.77 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRkTEQLKAVddlSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI----- 81
Cdd:COG4598 9 LEVRDLHKSF-------GD-LEVLKGV---SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 -------ADLKEseLKDYRKRMQIIFQdpyaSLN--PTMNVFQ-IISEPMNIHGSyEKEEQKEIILDLLKKVGLKEEHLY 151
Cdd:COG4598 78 rdgelvpADRRQ--LQRIRTRLGMVFQ----SFNlwSHMTVLEnVIEAPVHVLGR-PKAEAIERAEALLAKVGLADKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 152 rYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRigVMY 231
Cdd:COG4598 151 -YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSH--VVF 226
|
250 260 270
....*....|....*....|....*....|.
gi 1078707893 232 L--GNIVEIADSEDLYTKPAHPYTQALLSSM 260
Cdd:COG4598 227 LhqGRIEEQGPPAEVFGNPKSERLRQFLSSS 257
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-258 |
1.32e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.01 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfgrKTEQLKAVddlSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:PRK10619 3 ENKLNVIDLHKRYG--------EHEVLKGV---SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKES----------ELKDYRKRMQIIFQdpYASLNPTMNVFQIISE-PMNIHGsYEKEEQKEIILDLLKKVGLKEEHLYR 152
Cdd:PRK10619 72 VRDKdgqlkvadknQLRLLRTRLTMVFQ--HFNLWSHMTVLENVMEaPIQVLG-LSKQEARERAVKYLAKVGIDERAQGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:PRK10619 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
250 260
....*....|....*....|....*.
gi 1078707893 233 GNIVEIADSEDLYTKPAHPYTQALLS 258
Cdd:PRK10619 228 GKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
33-257 |
1.68e-36 |
|
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: 134.35 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRL--HDVTSGNILFDGKDIadlkeSELKDYRKRMQIIFQDpYAsLNPT 110
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFvkAAGLTGRIAIADRDL-----THAPPHKRGLALLFQN-YA-LFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQIISEPMNIHgSYEKEEQKEIILDLLKKVGLKEeHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVS 190
Cdd:TIGR03258 94 LKVEDNVAFGLRAQ-KMPKADIAERVADALKLVGLGD-AAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDAN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 191 VQAQVVNMLQDIQEE-TGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALL 257
Cdd:TIGR03258 172 IRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-244 |
2.42e-36 |
|
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: 136.86 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKK-YFPIKKGLfgrkteqLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILF----D 77
Cdd:TIGR03269 276 GEPIIKVRNVSKrYISVDRGV-------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 78 GKDIADLKESELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILdlLKKVGLKEEH----LYRY 153
Cdd:TIGR03269 349 WVDMTKPGPDGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMKAVIT--LKMVGFDEEKaeeiLDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 154 PHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLG 233
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
250
....*....|.
gi 1078707893 234 NIVEIADSEDL 244
Cdd:TIGR03269 505 KIVKIGDPEEI 515
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-258 |
4.40e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 130.26 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 5 NLIEVRNLKKYFpikKGlfgrkTEQLKAVDdlsFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSG-----NILFDGK 79
Cdd:PRK11264 2 SAIEVKNLVKKF---HG-----QTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 80 DIADLKESELKDYRKRMQIIFQDpyASLNPTMNVFQ-IISEPMNIHGSyEKEEQKEIILDLLKKVGL--KEEhlyRYPHE 156
Cdd:PRK11264 71 RSLSQQKGLIRQLRQHVGFVFQN--FNLFPHRTVLEnIIEGPVIVKGE-PKEEATARARELLAKVGLagKET---SYPRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 157 FSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGvTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
250 260
....*....|....*....|..
gi 1078707893 237 EIADSEDLYTKPAHPYTQALLS 258
Cdd:PRK11264 224 EQGPAKALFADPQQPRTRQFLE 245
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
235-322 |
5.06e-36 |
|
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: 125.17 E-value: 5.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 235 IVEIADSEDLYTKPAHPYTQALLSSMPEP-DPtnaGKERIILEGEVPSPLNSPSGCKFRTRCKFATEKCAQEVPKMVEIA 313
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTIkKR---DRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIA 78
|
....*....
gi 1078707893 314 KGHQVACHL 322
Cdd:TIGR01727 79 EGHRVACHL 87
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-255 |
5.90e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 129.75 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKGLFgrkteqlkavdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI---AD 83
Cdd:COG4161 3 IQLKNINCFYGSHQALF-----------DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESELKDYRKRMQIIFQDpYaSLNPTMNVFQ-IISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQR 162
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQ-Y-NLWPHLTVMEnLIEAPCKVLG-LSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
250
....*....|...
gi 1078707893 243 DLytkpAHPYTQA 255
Cdd:COG4161 227 HF----TQPQTEA 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-227 |
6.04e-36 |
|
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: 128.81 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkeselkdyRKRMQIIFQdpYASLNPTM 111
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIGYVPQ--RRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 --NVFQIISEPMNIH---GSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISA 186
Cdd:cd03235 84 piSVRDVVLMGLYGHkglFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1078707893 187 LDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRI 227
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-244 |
8.47e-36 |
|
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: 129.27 E-value: 8.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKkyfpikkglFGRKTEQlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03253 1 IEFENVT---------FAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELkdyRKRMQIIFQDP------------YASLNPTMNvfQII--SEPMNIHgsyekeeqkEIILDLLK----KVGlkEE 148
Cdd:cd03253 71 DSL---RRAIGVVPQDTvlfndtigynirYGRPDATDE--EVIeaAKAAQIH---------DKIMRFPDgydtIVG--ER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 149 HLYrypheFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeeTGVTYLFIAHDLSMVRHiSDRIG 228
Cdd:cd03253 135 GLK-----LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKII 206
|
250
....*....|....*.
gi 1078707893 229 VMYLGNIVEIADSEDL 244
Cdd:cd03253 207 VLKDGRIVERGTHEEL 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
37-257 |
1.72e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.33 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 37 SFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyRKrMQIIFQDpyASLNPTMNVFQI 116
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RP-VSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 117 ISEPMNIHGSYEKEEQKEIIlDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVV 196
Cdd:COG3840 92 IGLGLRPGLKLTAEQRAQVE-QALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 197 NMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALL 257
Cdd:COG3840 170 DLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
32-247 |
2.92e-35 |
|
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: 134.12 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPYaslnptm 111
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPY------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 nVFqiisepmniHGS-------YEKEEQKEIILDLLKKVGLKEEhLYRYPH-------E----FSGGQRQRISIARALSV 173
Cdd:COG4988 422 -LF---------AGTirenlrlGRPDASDEELEAALEAAGLDEF-VAALPDgldtplgEggrgLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 174 KPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-238 |
3.10e-35 |
|
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: 127.58 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESelkdyrkRMqIIFQDpyASLNPTMN 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-------RM-VVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 VFQIISEPMN-IHGSYEKEEQKEIILDLLKKVGLKEEHlYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:TIGR01184 71 VRENIALAVDrVLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 192 QAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVM------YLGNIVEI 238
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEV 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-237 |
4.00e-35 |
|
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: 126.84 E-value: 4.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLK-KYfpikkglfgRKTEQLkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:cd03244 3 IEFKNVSlRY---------RPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 eseLKDYRKRMQIIFQDPYaslnptmnVFQ-IISEPMNIHGSYEKEEqkeiILDLLKKVGLKE---EHLYRYPHE----- 156
Cdd:cd03244 73 ---LHDLRSRISIIPQDPV--------LFSgTIRSNLDPFGEYSDEE----LWQALERVGLKEfveSLPGGLDTVveegg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 157 --FSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQdiQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGN 234
Cdd:cd03244 138 enLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
...
gi 1078707893 235 IVE 237
Cdd:cd03244 215 VVE 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-236 |
1.65e-34 |
|
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: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlke 86
Cdd:cd03263 1 LQIRNLTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDpyASLNPTMNVfqiiSEPMNIHG---SYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQ 163
Cdd:cd03263 68 TDRKAARQSLGYCPQF--DALFDELTV----REHLRFYArlkGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVtyLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-237 |
6.71e-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: 123.87 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 28 EQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDP---- 103
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMIGVVLQDTflfs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 --------YASLNPTMNVFQIISEPMNIHgsyekeeqkEIILDLLKkvGLkEEHLYRYPHEFSGGQRQRISIARALSVKP 175
Cdd:cd03254 91 gtimenirLGRPNATDEEVIEAAKEAGAH---------DFIMKLPN--GY-DTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 176 DFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVE 237
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIE 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-258 |
1.34e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.12 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFpikkglfGRKteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV-----TSGNILFDG 78
Cdd:PRK14239 3 EPILQVSDLSVYY-------NKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 79 KDIADLKeSELKDYRKRMQIIFQDPyaslNP-TMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEE---HLYRYP 154
Cdd:PRK14239 72 HNIYSPR-TDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEvkdRLHDSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 155 HEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRIGVMYLGN 234
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGD 224
|
250 260
....*....|....*....|....
gi 1078707893 235 IVEIADSEDLYTKPAHPYTQALLS 258
Cdd:PRK14239 225 LIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
33-201 |
2.48e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.82 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD---VTSGNILFDGKDIADLKEselkdYRKRMQIIFQDPYasLNP 109
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPA-----EQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TMNVFQIIsePMNIHGSYEKEEQKEIILDLLKKVGLkeEHLY-RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:COG4136 90 HLSVGENL--AFALPPTIGRAQRRARVEQALEEAGL--AGFAdRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170
....*....|....*..
gi 1078707893 189 VSVQAQ----VVNMLQD 201
Cdd:COG4136 166 AALRAQfrefVFEQIRQ 182
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-245 |
3.77e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 3.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKKYFPikkglfgrKTEQLkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDia 82
Cdd:PRK13635 2 KEEIIRVEHISFRYP--------DAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 dLKESELKDYRKRMQIIFQDPYASLNPTmNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQR 162
Cdd:PRK13635 71 -LSEETVWDVRRQVGMVFQNPDNQFVGA-TVQDDVAFGLENIG-VPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSE 242
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
...
gi 1078707893 243 DLY 245
Cdd:PRK13635 226 EIF 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-236 |
3.81e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 3.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlKESELKDYRKRMQIIFQDPYASLNPT 110
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQIISEPMNIhgSYEKEEQKEIILDLLKKVGLK-EEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PRK13637 100 TIEKDIAFGPINL--GLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1078707893 190 SVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-254 |
4.44e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 122.85 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV------TSGNILFDGKDIADLKESELkdyRKRMQIIFQDPyaSLN 108
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQP--NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 109 PTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGL-KEEH--LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPIS 185
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 186 ALDVSVQAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQ 254
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-246 |
6.93e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.41 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKkyfpikkglFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlke 86
Cdd:PRK13632 8 IKVENVS---------FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDPYaslnptmNVFQIISEPMNIHGSYE-----KEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQ 161
Cdd:PRK13632 76 ENLKEIRKKIGIIFQNPD-------NQFIGATVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRhISDRIGVMYLGNIVEIADS 241
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
....*
gi 1078707893 242 EDLYT 246
Cdd:PRK13632 227 KEILN 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-242 |
9.54e-33 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 121.00 E-value: 9.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKST-----TGrsiirLHDVTSGNILFDG 78
Cdd:COG4181 6 APIIELRGLTKTV-------GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTllgllAG-----LDRPTSGTVRLAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 79 KDIADLKESELKDYR-KRMQIIFQdpyaS--LNPTMNVFQIISEPMNIHGSYEKEEQKEiilDLLKKVGLKE--EHlyrY 153
Cdd:COG4181 74 QDLFALDEDARARLRaRHVGFVFQ----SfqLLPTLTALENVMLPLELAGRRDARARAR---ALLERVGLGHrlDH---Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 154 PHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLG 233
Cdd:COG4181 144 PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
....*....
gi 1078707893 234 NIVEIADSE 242
Cdd:COG4181 223 RLVEDTAAT 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-227 |
1.27e-32 |
|
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: 120.62 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKkgLFGRKTeqLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGK----DI 81
Cdd:COG4778 4 LLEVENLSKTFTLH--LQGGKR--LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADLKESELKDYRKRMqiIfqdPYAS--LN--PTMNVFQIISEPMnIHGSYEKEEQKEIILDLLKKVGLKEE--HLYryPH 155
Cdd:COG4778 80 AQASPREILALRRRT--I---GYVSqfLRviPRVSALDVVAEPL-LERGVDREEARARARELLARLNLPERlwDLP--PA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRI 227
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-249 |
1.44e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.80 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgRKTEqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:PRK11650 4 LKLQAVRKSYD-------GKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SElkdyrkR---MqiIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQ 163
Cdd:PRK11650 74 AD------RdiaM--VFQN-YA-LYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILEL-EPLLDRKPRELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDL--SMVrhISDRIGVMYLGNIVEIADS 241
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQveAMT--LADRVVVMNGGVAEQIGTP 219
|
....*...
gi 1078707893 242 EDLYTKPA 249
Cdd:PRK11650 220 VEVYEKPA 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-248 |
3.68e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.57 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPikkglfgRKTEQLKAVDdlsFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK13639 1 ILETRDLKYSYP-------DGTEALKGIN---FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKdYRKRMQIIFQDPYASL-NPTmnVFQIIS-EPMNIhgSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQ 163
Cdd:PRK13639 71 KSLLE-VRKTVGIVFQNPDDQLfAPT--VEEDVAfGPLNL--GLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSED 243
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
....*
gi 1078707893 244 LYTKP 248
Cdd:PRK13639 224 VFSDI 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-234 |
7.67e-32 |
|
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: 117.74 E-value: 7.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 28 EQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlkeseLKDYRKRMQIIFQDPYasl 107
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERRKSIGYVMQDVD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 108 nptmnvFQIISEP------MNIHGSYEKEEQKEIILDLLKKVGLKEEHlyryPHEFSGGQRQRISIARALSVKPDFILCD 181
Cdd:cd03226 82 ------YQLFTDSvreellLGLKELDAGNEQAETVLKDLDLYALKERH----PLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 182 EPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRigVMYLGN 234
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDR--VLLLAN 201
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-244 |
8.70e-32 |
|
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: 118.74 E-value: 8.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkesELKDYRKRMQIIFQ---------- 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQVGVVLQenvlfnrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 102 DPYASLNPTMNVFQIIsEPMNIHGSYE-----KEEQKEIILDllKKVGLkeehlyryphefSGGQRQRISIARALSVKPD 176
Cdd:cd03252 94 DNIALADPGMSMERVI-EAAKLAGAHDfiselPEGYDTIVGE--QGAGL------------SGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 177 FILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDL 244
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-252 |
1.09e-31 |
|
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: 121.37 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD-LKESELKDYRKRMQIIFQDpyASLNPTMNV 113
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsRKGIFLPPEKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 114 FQIISEPMNIHGSYEKEEQKEIILDLLkkvGLkeEHLY-RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQ 192
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELL---GI--GHLLgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 193 AQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPY 252
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
30-247 |
1.40e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 124.04 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 30 LKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPyaslnp 109
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAEL---RARMALVPQDP------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 tmNVFQIiSEPMNI-HGSYEKEEQKEIILdllKKVGLKEEHLYRYPHEF-----------SGGQRQRISIARALSVKPDF 177
Cdd:TIGR02204 424 --VLFAA-SVMENIrYGRPDATDEEVEAA---ARAAHAHEFISALPEGYdtylgergvtlSGGQRQRIAIARAILKDAPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 178 ILCDEPISALDVSVQAQVVNMLQDIQeeTGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:TIGR02204 498 LLLDEATSALDAESEQLVQQALETLM--KGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-236 |
1.56e-31 |
|
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: 117.47 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKGLFgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlk 85
Cdd:cd03266 1 MITADALTKRFRDVKKTV-------QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 eSELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:cd03266 71 -KEPAEARRRLGFVSDS--TGLYDRLTARENLEYFAGLYG-LKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-252 |
1.62e-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: 123.72 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPY---ASL- 107
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRRIAVVPQRPHlfdTTLr 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 108 ------NPTMNvfqiisepmnihgsyekEEQkeiILDLLKKVGLkEEHLYRYPH-------E----FSGGQRQRISIARA 170
Cdd:COG4987 427 enlrlaRPDAT-----------------DEE---LWAALERVGL-GDWLAALPDgldtwlgEggrrLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 171 LSVKPDFILCDEPISALDVSVQAQVvnmLQDIQEET-GVTYLFIAHDLSMVRHIsDRIGVMYLGNIVEIADSEDLYTKPA 249
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNG 561
|
...
gi 1078707893 250 HPY 252
Cdd:COG4987 562 RYR 564
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
34-244 |
2.25e-31 |
|
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: 123.91 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 34 DDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDpyASLNPTmNV 113
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV---RRQLGVVLQN--GRLMSG-SI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 114 FQII--SEPMNIHGSYEKeeqkeiildlLKKVGLkEEHLYRYP---H--------EFSGGQRQRISIARALSVKPDFILC 180
Cdd:TIGR03797 544 FENIagGAPLTLDEAWEA----------ARMAGL-AEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQeetgVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDL 244
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-236 |
2.31e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.65 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLkkYFPIKKGlfgRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIA 82
Cdd:PRK13633 1 MNEMIKCKNV--SYKYESN---EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 DlkESELKDYRKRMQIIFQDPYASLnptmnVFQIISE-----PMNIhgSYEKEEQKEIILDLLKKVGLKEehlYRY--PH 155
Cdd:PRK13633 76 D--EENLWDIRNKAGMVFQNPDNQI-----VATIVEEdvafgPENL--GIPPEEIRERVDESLKKVGMYE---YRRhaPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNI 235
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
.
gi 1078707893 236 V 236
Cdd:PRK13633 223 V 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-216 |
3.78e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.66 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfGRKTEQLkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI----A 82
Cdd:COG4525 4 LTVRHVSVRYP------GGGQPQP-ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 DlkeselkdyRKrmqIIFQDpYAsLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQR 162
Cdd:COG4525 77 D---------RG---VVFQK-DA-LLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGL-ADFARRRIWQLSGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHD 216
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-254 |
4.94e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.32 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 5 NLIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV-----TSGNILFDGK 79
Cdd:PRK14247 2 NKIEIRDLKVSF-----------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 80 DIADLKESELkdyRKRMQIIFQDPYASlnPTMNVFQIISEPMNIHG-SYEKEEQKEIILDLLKKVGLKEE---HLYRYPH 155
Cdd:PRK14247 71 DIFKMDVIEL---RRRVQMVFQIPNPI--PNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLWDEvkdRLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*....
gi 1078707893 236 VEIADSEDLYTKPAHPYTQ 254
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTE 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-237 |
6.03e-31 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 115.78 E-value: 6.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03268 1 LKTNDLTKTY-------GKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SelkdyRKRMQIIFQDPyaSLNPTMNVFQIISEPMNIHGsYEKEEQKEIildlLKKVGLKEehlyrYPHE----FSGGQR 162
Cdd:cd03268 70 A-----LRRIGALIEAP--GFYPNLTARENLRLLARLLG-IRKKRIDEV----LDVVGLKD-----SAKKkvkgFSLGMK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVE 237
Cdd:cd03268 133 QRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-236 |
6.39e-31 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.06 E-value: 6.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGK--DIADL 84
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 85 KESElkdyRKRMQIIFQdpyaslnptmnvfqiisepmnihgsyekeeqkeiildllkkvglkeehlyrypheFSGGQRQR 164
Cdd:cd03216 70 RDAR----RAGIAMVYQ-------------------------------------------------------LSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-258 |
7.37e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 116.87 E-value: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfgrKTEQLKAVDdlsFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVT-----SGNILFDG 78
Cdd:PRK14267 2 KFAIETVNLRVYYG--------SNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 79 KDIADLKESELkDYRKRMQIIFQdpYASLNPTMNVFQIISEPMNIHG-SYEKEEQKEIILDLLKKVGLKEE---HLYRYP 154
Cdd:PRK14267 71 RNIYSPDVDPI-EVRREVGMVFQ--YPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEvkdRLNDYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 155 HEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRIGVMYLGN 234
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGK 225
|
250 260
....*....|....*....|....
gi 1078707893 235 IVEIADSEDLYTKPAHPYTQALLS 258
Cdd:PRK14267 226 LIEVGPTRKVFENPEHELTEKYVT 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-236 |
8.86e-31 |
|
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: 115.46 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03269 1 LEVENVTKRF-------GRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 S-------ELKDYRKrMQIIFQDPY-ASLnptmnvfqiisepmniHGsYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFS 158
Cdd:cd03269 70 NrigylpeERGLYPK-MKVIDQLVYlAQL----------------KG-LKKEEARRRIDEWLERLEL-SEYANKRVEELS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 159 GGQRQRISIARALSVKPDFILCDEPISALDVsVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-244 |
1.17e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 115.22 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03224 1 LEVENLNAGY-----------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SElkdyRKRMQI--------IFqdpyaslnPTMNVFQiisepmNIH-GSY-----EKEEQKEIILDLLKKvgLKEEhLYR 152
Cdd:cd03224 70 HE----RARAGIgyvpegrrIF--------PELTVEE------NLLlGAYarrraKRKARLERVYELFPR--LKER-RKQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:cd03224 129 LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLER 207
|
250
....*....|..
gi 1078707893 233 GNIVEIADSEDL 244
Cdd:cd03224 208 GRVVLEGTAAEL 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-237 |
2.04e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 120.84 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPY---ASLN 108
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNIAVVFQDAGlfnRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 109 PTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKK----VGLKEEHLyryphefSGGQRQRISIARALSVKPDFILCDEPI 184
Cdd:PRK13657 427 DNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGydtvVGERGRQL-------SGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 185 SALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVE 237
Cdd:PRK13657 500 SALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-244 |
6.31e-30 |
|
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: 119.44 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfGRkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:TIGR02203 328 RGDVEFRNVTFRYP------GR---DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKeseLKDYRKRMQIIFQDPYAsLNPTmnvfqiISEpmNIHGSYEKEEQKEIILDLLKKVGLKEeHLYRYPHEF------ 157
Cdd:TIGR02203 399 YT---LASLRRQVALVSQDVVL-FNDT------IAN--NIAYGRTEQADRAEIERALAAAYAQD-FVDKLPLGLdtpige 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 -----SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYL 232
Cdd:TIGR02203 466 ngvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDD 542
|
250
....*....|..
gi 1078707893 233 GNIVEIADSEDL 244
Cdd:TIGR02203 543 GRIVERGTHNEL 554
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-247 |
6.96e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKkyfpikkglFGRKTEQLK-AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDia 82
Cdd:PRK13650 2 SNIIEVKNLT---------FKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 dLKESELKDYRKRMQIIFQDPyaslnptMNVFQIISEPMNIHGSYEK-----EEQKEIILDLLKKVGLkEEHLYRYPHEF 157
Cdd:PRK13650 71 -LTEENVWDIRHKIGMVFQNP-------DNQFVGATVEDDVAFGLENkgiphEEMKERVNEALELVGM-QDFKEREPARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRhISDRIGVMYLGNIVE 237
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVES 220
|
250
....*....|
gi 1078707893 238 IADSEDLYTK 247
Cdd:PRK13650 221 TSTPRELFSR 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-247 |
8.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.88 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 29 QLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI-ADLKESELKDYRKRMQIIFQDPYASL 107
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 108 NPTMNVFQIISEPMNIhgSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISAL 187
Cdd:PRK13646 99 FEDTVEREIIFGPKNF--KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 188 DVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-244 |
1.25e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.81 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKKYFPikkglfGRKteqlkAVDDLSFTIKKGETFGLVGESGCGKST-----TGrsiirLHDVTSGNILFD 77
Cdd:COG1129 1 AEPLLEMRGISKSFG------GVK-----ALDGVSLELRPGEVHALLGENGAGKSTlmkilSG-----VYQPDSGEILLD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 78 GK--DIADLKESElkdyRKRMQIIFQDPyaSLNPTMNVFQII---SEPMNiHGSYEKEEQKEIILDLLKKVGLKEEhlyr 152
Cdd:COG1129 65 GEpvRFRSPRDAQ----AAGIAIIHQEL--NLVPNLSVAENIflgREPRR-GGLIDWRAMRRRARELLARLGLDID---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 yPH----EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIG 228
Cdd:COG1129 134 -PDtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVT 211
|
250
....*....|....*.
gi 1078707893 229 VMYLGNIVEIADSEDL 244
Cdd:COG1129 212 VLRDGRLVGTGPVAEL 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-225 |
1.41e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 113.71 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKkyfpikkglFGRKTEQLkaVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD 80
Cdd:PRK11831 2 QSVANLVDMRGVS---------FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADLKESELKDYRKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLK-EEHLYryPHEFSG 159
Cdd:PRK11831 71 IPAMSRSRLYTVRKRMSMLFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRgAAKLM--PSELSG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISD 225
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-240 |
1.47e-29 |
|
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: 112.30 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPikkglfgrkTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03245 3 IEFRNVSFSYP---------NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELkdyRKRMQIIFQDP---YASL--NPTMnvfqiisepmnihGSYEKEEQKeiILDLLKKVGLkEEHLYRYPHEF---- 157
Cdd:cd03245 74 ADL---RRNIGYVPQDVtlfYGTLrdNITL-------------GAPLADDER--ILRAAELAGV-TDFVNKHPNGLdlqi 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 -------SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQdiQEETGVTYLFIAHDLSMVRhISDRIGVM 230
Cdd:cd03245 135 gergrglSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRPSLLD-LVDRIIVM 211
|
250
....*....|
gi 1078707893 231 YLGNIVeiAD 240
Cdd:cd03245 212 DSGRIV--AD 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-224 |
1.99e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.22 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 27 TEQLKavdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDYRKR-MQIIFQdpYA 105
Cdd:PRK11629 22 TDVLH---NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkLGFIYQ--FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 106 SLNPTMNVFQIISEPMNIHGSYEKEEQKEIiLDLLKKVGLKEEHLYRyPHEFSGGQRQRISIARALSVKPDFILCDEPIS 185
Cdd:PRK11629 97 HLLPDFTALENVAMPLLIGKKKPAEINSRA-LEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1078707893 186 ALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHIS 224
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
6-227 |
2.21e-29 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 112.10 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPikkgLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILF--DGK--DI 81
Cdd:TIGR02324 1 LLEVEDLSKTFT----LHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVrhEGAwvDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADLKESELKDYRKRmQIIFQDPYASLNPTMNVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQ 161
Cdd:TIGR02324 77 AQASPREVLEVRRK-TIGYVSQFLRVIPRVSALEVVAEPLLERGV-PREAARARARELLARLNIPERLWHLPPATFSGGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRI 227
Cdd:TIGR02324 155 QQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-249 |
6.97e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.97 E-value: 6.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyrKRMQIIFQDpYAsLNPTMNVF 114
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQS-YA-LYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 115 QIISEPMNIHGSYEKEEQKEI-----ILDLlkkvglkeEHLY-RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:PRK11000 94 ENMSFGLKLAGAKKEEINQRVnqvaeVLQL--------AHLLdRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 189 VSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPA 249
Cdd:PRK11000 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-216 |
1.06e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 110.25 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKKYFpikkglfGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSV-------GQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADLKESELKDYR-KRMQIIFQDpyASLNPTMNVFQIISEPMNIHGSYEKEEQKEIIlDLLKKVGLkEEHLYRYPHEFSG 159
Cdd:PRK10584 74 LHQMDEEARAKLRaKHVGFVFQS--FMLIPTLNALENVELPALLRGESSRQSRNGAK-ALLEQLGL-GKRLDHLPAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHD 216
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
1.73e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLKkyfpikkglFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD 80
Cdd:PRK13648 2 EDKNSIIVFKNVS---------FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IADlkeSELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSYEkeEQKEIILDLLKKVGLKEEHLYRyPHEFSGG 160
Cdd:PRK13648 73 ITD---DNFEKLRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYD--EMHRRVSEALKQVDMLERADYE-PNALSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIAD 240
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
....*..
gi 1078707893 241 SEDLYTK 247
Cdd:PRK13648 226 PTEIFDH 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-239 |
2.70e-28 |
|
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: 108.65 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLK-KYFPikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:cd03369 7 IEVENLSvRYAP----------DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 eseLKDYRKRMQIIFQDPY---ASLNPTMNVFqiisepmnihGSYEKEEqkeiildLLKKVGLKEEHLyryphEFSGGQR 162
Cdd:cd03369 77 ---LEDLRSSLTIIPQDPTlfsGTIRSNLDPF----------DEYSDEE-------IYGALRVSEGGL-----NLSQGQR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMlqdIQEE-TGVTYLFIAHDLSMVRHIsDRIGVMYLGNIVEIA 239
Cdd:cd03369 132 QLLCLARALLKRPRVLVLDEATASIDYATDALIQKT---IREEfTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-236 |
3.26e-28 |
|
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: 108.73 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyrKRMQIIFQDpyASLNPTMNVF 114
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQE--NNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 115 QIISEPMNiHGSYEKEEQKEIILDLLKKVGLKEEHLyRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQ 194
Cdd:cd03298 89 QNVGLGLS-PGLKLTAEDRQAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1078707893 195 VVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-248 |
3.41e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.30 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 29 QLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI-ADLKESELKDYRKRMQIIFQDPYASL 107
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 108 NPTMNVFQIISEPMNIHGSyeKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISAL 187
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFS--EDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 188 DVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKP 248
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-254 |
3.55e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.74 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKglfgrkteqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTS-----GNILFDGKDI 81
Cdd:PRK14258 8 IKVNNLSFYYDTQK-----------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADlKESELKDYRKRMQIIFQDPyaSLNPtMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKEE---HLYRYPHEFS 158
Cdd:PRK14258 77 YE-RRVNLNRLRRQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEikhKIHKSALDLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 159 GGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMY-----LG 233
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIG 232
|
250 260
....*....|....*....|.
gi 1078707893 234 NIVEIADSEDLYTKPAHPYTQ 254
Cdd:PRK14258 233 QLVEFGLTKKIFNSPHDSRTR 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-236 |
5.58e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.20 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlke 86
Cdd:COG4152 2 LELKGLTKRF-------GDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selKDYR------------KRM----QIIFqdpYASLnptmnvfqiisepmniHGsYEKEEQKEIILDLLKKVGLkEEHL 150
Cdd:COG4152 68 ---EDRRrigylpeerglyPKMkvgeQLVY---LARL----------------KG-LSKAEAKRRADEWLERLGL-GDRA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 151 YRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALD-VSVQAqVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:COG4152 124 NKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVI 201
|
....*..
gi 1078707893 230 MYLGNIV 236
Cdd:COG4152 202 INKGRKV 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-249 |
7.14e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.72 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI-ADLKESELKDYRKRMQIIFQDPYASLNP 109
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TMNVFQIISEPMNIHGSyeKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PRK13634 101 ETVEKDICFGPMNFGVS--EEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 190 SVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPA 249
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-249 |
8.48e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.33 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKglfgrkTEQLKAVDDLSFTIKKGETFGLVGESGCGKST----------TGRSIIRLHDVTSGNIL 75
Cdd:PRK13631 21 ILRVKNLYCVFDEKQ------ENELVALNNISYTFEKNKIYFIIGNSGSGKSTlvthfnglikSKYGTIQVGDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 76 FDGKDIADLKESELKDY---RKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGSyeKEEQKEIILDLLKKVGLKEEHLYR 152
Cdd:PRK13631 95 NNHELITNPYSKKIKNFkelRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVK--KSEAKKLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDK 251
|
250
....*....|....*..
gi 1078707893 233 GNIVEIADSEDLYTKPA 249
Cdd:PRK13631 252 GKILKTGTPYEIFTDQH 268
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-242 |
1.68e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 106.88 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDYRKRMQIIFQDPYASLNPT 110
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 mnVFQIISEPMNIHGSyEKEEQKEIILDLLKKVGLKEEhLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVS 190
Cdd:PRK10908 96 --VYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 191 VQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-244 |
3.38e-27 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 111.76 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQD 102
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL---RRQMGVVLQE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 pyaslnptmNVFQIISEPMNIHGSYEKEEQKEIILdlLKKVGLKEEHLYRYPHEF-----------SGGQRQRISIARAL 171
Cdd:TIGR01846 540 ---------NVLFSRSIRDNIALCNPGAPFEHVIH--AAKLAGAHDFISELPQGYntevgekganlSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 172 SVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDL 244
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
28-240 |
4.34e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.50 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 28 EQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDP---Y 104
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---RRNIGYVPQDPrlfY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 ASL--NPTMNVFQIisepmnihgsyekeeQKEIILDLLKKVGLkEEHLYRYPHEF-----------SGGQRQRISIARAL 171
Cdd:TIGR03375 553 GTLrdNIALGAPYA---------------DDEEILRAAELAGV-TEFVRRHPDGLdmqigergrslSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 172 SVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRhISDRIGVMYLGNIVeiAD 240
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLD-LVDRIIVMDNGRIV--AD 680
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
34-242 |
5.28e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 106.30 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 34 DDLSFTIKKGETFGLVGESGCGKSTTGRSI--IRLHDVTSGNILFDGKDIADLKESElkdyRKRMQI--IFQDPYASlnP 109
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE----RARAGIflAFQYPVEI--P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TMNVFQIISEPMNIHGSYE---KEEQKEIiLDLLKKVGLKEEHLYRYPHE-FSGGQRQRISIARALSVKPDFILCDEPIS 185
Cdd:COG0396 91 GVSVSNFLRTALNARRGEElsaREFLKLL-KEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 186 ALDV-SVQ--AQVVNMLQDiqEETGVtyLFIAHDLSMVRHIS-DRIGVMYLGNIVEIADSE 242
Cdd:COG0396 170 GLDIdALRivAEGVNKLRS--PDRGI--LIITHYQRILDYIKpDFVHVLVDGRIVKSGGKE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-249 |
5.65e-27 |
|
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: 105.70 E-value: 5.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKe 86
Cdd:cd03218 1 LRAENLSKRY-------GKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkeEHL-YRYPHEFSGGQRQRI 165
Cdd:cd03218 69 ---MHKRARLGIGYLPQEASIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI--THLrKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 166 SIARALSVKPDFILCDEPISALD-VSVqaqvvnmlQDIQE------ETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEI 238
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDpIAV--------QDIQKiikilkDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
250
....*....|.
gi 1078707893 239 ADSEDLYTKPA 249
Cdd:cd03218 215 GTPEEIAANEL 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-236 |
6.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKKYFPikkglfgRKTEQLKavdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIa 82
Cdd:PRK13636 2 EDYILKVEELNYNYS-------DGTHALK---GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 DLKESELKDYRKRMQIIFQDPYASLNpTMNVFQIIS-EPMNIhgSYEKEEQKEIILDLLKKVGLkeEHLYRYP-HEFSGG 160
Cdd:PRK13636 71 DYSRKGLMKLRESVGMVFQDPDNQLF-SASVYQDVSfGAVNL--KLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-243 |
7.64e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.09 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKyfpikkgLFGRKTE-QLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK13651 3 IKVKNIVK-------IFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESEL---------------------KDYRKRMQIIFQ-DPYASLNPTMNVfQIISEPMNIhgSYEKEEQKEIILDLLKKV 143
Cdd:PRK13651 76 KTKEkekvleklviqktrfkkikkiKEIRRRVGVVFQfAEYQLFEQTIEK-DIIFGPVSM--GVSKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 144 GLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHI 223
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEW 231
|
250 260
....*....|....*....|
gi 1078707893 224 SDRIGVMYLGNIVEIADSED 243
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYD 251
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-227 |
1.62e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.41 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 24 GRKTEQLKAVDDLSFTIKKGEtFGLV-GESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdYRKRMQIIFQD 102
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PyASLNPTmnVFQIISEPMNIHGsyeKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDE 182
Cdd:PRK10247 90 P-TLFGDT--VYDNLIFPWQIRN---QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRI 227
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-229 |
2.52e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.34 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADL-- 84
Cdd:COG1137 4 LEAENLVKSY-------GKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 85 -KeselkdyRKRMQI--------IFQDpyaslnptMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLkeEHLYRYP- 154
Cdd:COG1137 73 hK-------RARLGIgylpqeasIFRK--------LTVEDNILAVLELRK-LSKKEREERLEELLEEFGI--THLRKSKa 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 155 HEFSGGQRQRISIARALSVKPDFILCDEPISALD-VSVqaqvvnmlQDIQEetgvtylfiahdlsMVRHISDR-IGV 229
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV--------ADIQK--------------IIRHLKERgIGV 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
34-237 |
2.81e-26 |
|
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: 108.75 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 34 DDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPyaSL-NPTmn 112
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDT--VLfNDT-- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 vfqiISEpmNIhgSYEKEE--QKEI--------ILDLLKKV-----------GLKeehlyrypheFSGGQRQRISIARAL 171
Cdd:COG5265 448 ----IAY--NI--AYGRPDasEEEVeaaaraaqIHDFIESLpdgydtrvgerGLK----------LSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 172 SVKPDFILCDEPISALDVSVQaqvvnmlQDIQEE-----TGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVE 237
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTE-------RAIQAAlrevaRGRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-265 |
3.03e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.04 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK10535 4 LLELKDIRRSYPSGE-------EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKDYRKR-MQIIFQDPY--ASLNPTMNVfqiisEPMNIHGSYEKEEQKEIILDLLKKVGLKEEHLYRyPHEFSGGQR 162
Cdd:PRK10535 77 ADALAQLRREhFGFIFQRYHllSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDlSMVRHISDRigvmylgnIVEIADSE 242
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAER--------VIEIRDGE 220
|
250 260
....*....|....*....|...
gi 1078707893 243 DLYTKPAHPYTQALLSSMPEPDP 265
Cdd:PRK10535 221 IVRNPPAQEKVNVAGGTEPVVNT 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-248 |
5.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.50 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKkyfpikkglFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRL---HDVTSGNILFDGkd 80
Cdd:PRK13640 3 DNIVEFKHVS---------FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 iADLKESELKDYRKRMQIIFQDPYaslnptmNVFQIISEPMNIHGSYE-----KEEQKEIILDLLKKVGLKEeHLYRYPH 155
Cdd:PRK13640 72 -ITLTAKTVWDIREKVGIVFQNPD-------NQFVGATVGDDVAFGLEnravpRPEMIKIVRDVLADVGMLD-YIDSEPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNI 235
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKL 221
|
250
....*....|...
gi 1078707893 236 VEIADSEDLYTKP 248
Cdd:PRK13640 222 LAQGSPVEIFSKV 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-260 |
5.87e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 104.41 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSG-----NILFDGKDIADLKEseLKDYRKRMQIIFQDPyasl 107
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRRVGMLFQRP---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 108 NP-TMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLKE---EHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:PRK14271 111 NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDavkDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 184 ISALDVSVQAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALLSSM 260
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
7-250 |
6.58e-26 |
|
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: 108.11 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLK-KYFPIKKGLfgrkteqlkaVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:TIGR03796 478 VELRNITfGYSPLEPPL----------IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELK------DyrkrmQIIFQ------DPYASLNPTMNVFQIISEPMN--IHGsyekeeqkeiilDLLKKVGLKEEHLY 151
Cdd:TIGR03796 548 REVLAnsvamvD-----QDIFLfegtvrDNLTLWDPTIPDADLVRACKDaaIHD------------VITSRPGGYDAELA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 152 RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQdiqeETGVTYLFIAHDLSMVRHiSDRIGVMY 231
Cdd:TIGR03796 611 EGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLE 685
|
250
....*....|....*....
gi 1078707893 232 LGNIVEIADSEDLYTKPAH 250
Cdd:TIGR03796 686 RGKVVQRGTHEELWAVGGA 704
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-236 |
8.33e-26 |
|
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: 102.80 E-value: 8.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIK----------KGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNIlf 76
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 77 dgkDIADLKESELKD-YRKRMQIIF-QDPYASLN-PTMNVFQIISEPMNIHGSYEKEEQKEIIlDLLKKvglkEEHLYRY 153
Cdd:cd03267 79 ---RVAGLVPWKRRKkFLRRIGVVFgQKTQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELS-ELLDL----EELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 154 PHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLG 233
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 1078707893 234 NIV 236
Cdd:cd03267 231 RLL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-244 |
1.50e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.64 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKGLfgrkteqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKe 86
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP---------ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 seLKDYRKRMQIIFQDPYAsLNPTM-NvfqiisepmNIhgSYEKEEQ---KEII--------LDLLKKVglkEEHLYRYP 154
Cdd:PRK11176 412 --LASLRNQVALVSQNVHL-FNDTIaN---------NI--AYARTEQysrEQIEeaarmayaMDFINKM---DNGLDTVI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 155 HE----FSGGQRQRISIARA-LSVKPDFILcDEPISALDVSVQAQVVNMLQDIQEETgvTYLFIAHDLSMVRHiSDRIGV 229
Cdd:PRK11176 475 GEngvlLSGGQRQRIAIARAlLRDSPILIL-DEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILV 550
|
250
....*....|....*
gi 1078707893 230 MYLGNIVEIADSEDL 244
Cdd:PRK11176 551 VEDGEIVERGTHAEL 565
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-265 |
1.86e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.16 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTE-QLKAVDDLSFTIKKGETFGLVGESGCGKSTtgrsIIRLHD-----VTSGNILFDGKDIADLKE-SELKDYRKR 95
Cdd:PRK13645 16 YAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKST----MIQLTNgliisETGQTIVGDYAIPANLKKiKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 96 MQIIFQDPYASLNPTMNVFQIISEPMNIhgSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKP 175
Cdd:PRK13645 92 IGLVFQFPEYQLFQETIEKDIAFGPVNL--GENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 176 DFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTkpahpyTQA 255
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS------NQE 243
|
250
....*....|
gi 1078707893 256 LLSSMpEPDP 265
Cdd:PRK13645 244 LLTKI-EIDP 252
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-279 |
2.07e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 104.41 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlkeSE----LKDYRKRMQIIFQDpyASLNPT 110
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD---SArgifLPPHRRRIGYVFQE--ARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQiisepmNIHGSY------EKEEQKEIILDLLkkvGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPI 184
Cdd:COG4148 92 LSVRG------NLLYGRkrapraERRISFDEVVELL---GI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 185 SALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPahpytqALLSSMPEPD 264
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP------DLLPLAGGEE 235
|
250
....*....|....*
gi 1078707893 265 PTNagkeriILEGEV 279
Cdd:COG4148 236 AGS------VLEATV 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
32-217 |
2.57e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.09 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyrkrmQIIFQDpyASLNPTM 111
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLKEEHlYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:PRK11248 86 NVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*.
gi 1078707893 192 QAQVVNMLQDIQEETGVTYLFIAHDL 217
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-235 |
2.79e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 99.81 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDY--------RKRMqiifqd 102
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKRE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 pyaSLNPTMNVFQiisepmNIhgsyekeeqkeIILDLLkkvglkeehlyryphefSGGQRQRISIARALSVKPDFILCDE 182
Cdd:cd03215 88 ---GLVLDLSVAE------NI-----------ALSSLL-----------------SGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-236 |
3.07e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 37 SFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESelkdyRKRMQIIFQDpyASLNPTMNVFQI 116
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 117 ISepMNIH-GSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQV 195
Cdd:PRK10771 92 IG--LGLNpGLKLNAAQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1078707893 196 VNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-201 |
3.64e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 100.25 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKyfpikkgLFGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:COG4133 2 MLEAENLSC-------RRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 EselkDYRKRMQIIFqdPYASLNPTMNVFQIISEPMNIHGSYEKEEQkeiILDLLKKVGLkEEHLYRYPHEFSGGQRQRI 165
Cdd:COG4133 71 E----DYRRRLAYLG--HADGLKPELTVRENLRFWAALYGLRADREA---IDEALEAVGL-AGLADLPVRQLSAGQKRRV 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1078707893 166 SIARALSVKPDFILCDEPISALDVSVQAQVVNMLQD 201
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-247 |
3.79e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNI-LFDGKDIADLKESELKDYRKRMQIIFQDPYASLNP 109
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TMNVFQIISEPMNIhgSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PRK13643 100 ETVLKDVAFGPQNF--GIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 190 SVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:PRK13643 178 KARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-302 |
5.41e-25 |
|
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: 95.55 E-value: 5.41e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 236 VEIADSEDLYTKPAHPYTQALLSSMPEPDPTNAGKERIilEGEVPSPLNSPSGCKFRTRCKFATEKC 302
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTI--PGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-230 |
9.19e-25 |
|
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: 104.29 E-value: 9.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDyrkrmQIIfqdpYASLNPT 110
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-----QIA----WVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MnVFQIISEpmNIhGSYEKEEQKEIILDLLKKVGLKE--------------EHlyryPHEFSGGQRQRISIARALSVKPD 176
Cdd:TIGR02857 407 L-FAGTIAE--NI-RLARPDASDAEIREALERAGLDEfvaalpqgldtpigEG----GAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 177 FILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSmVRHISDRIGVM 230
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA-LAALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-244 |
1.07e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 99.67 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 29 QLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyRKRMQI--------IF 100
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR----IARLGIgyvpegrrIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 101 qdpyaslnPTMNVFQiisepmNIH-GSY------EKEEQKEIILDL---LKkvglkeEHLYRYPHEFSGGQRQRISIARA 170
Cdd:COG0410 91 --------PSLTVEE------NLLlGAYarrdraEVRADLERVYELfprLK------ERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 171 LSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
33-242 |
2.09e-24 |
|
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: 97.98 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD--VTSGNILFDGKDIADLKESElkdyRKRMQIifqdpyaslnpT 110
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEE----RARLGI-----------F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MnVFQiisEPMNIHGsyekeeqkeiildllkkvgLKEEHLYRYPHE-FSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:cd03217 81 L-AFQ---YPPEIPG-------------------VKNADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 190 SVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHI-SDRIGVMYLGNIVEIADSE 242
Cdd:cd03217 138 DALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-248 |
2.25e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHeenLIEVRNLKKYFpikkglfgrkTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD 80
Cdd:PRK13652 1 MH---LIETRDLCYSY----------SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 IAdlkESELKDYRKRMQIIFQDPYASLNPTMNVFQIISEPMNIhgSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGG 160
Cdd:PRK13652 68 IT---KENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINL--GLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:PRK13652 142 EKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
....*...
gi 1078707893 241 SEDLYTKP 248
Cdd:PRK13652 222 VEEIFLQP 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
35-248 |
2.42e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.65 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlKESELKDYRKRMQIIFQDP----------- 103
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEPvlfsgsvreni 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 -YASLNPTMNVFQIISEPMNIHGSYEKEEQkeiilDLLKKVGLKEEHLyryphefSGGQRQRISIARALSVKPDFILCDE 182
Cdd:TIGR00958 576 aYGLTDTPDEEIMAAAKAANAHDFIMEFPN-----GYDTEVGEKGSQL-------SGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 183 PISALDVSVQAqvvnMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTKP 248
Cdd:TIGR00958 644 ATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-236 |
2.50e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.03 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKglfgrkteqlkAVDDLSFTIKKGeTFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:cd03264 1 LQLENLTKRYGKKR-----------ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SelkdYRKRMQIIFQDPyaSLNPTMNVFQIIsEPMNIHGSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRIS 166
Cdd:cd03264 69 K----LRRRIGYLPQEF--GVYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVtyLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-236 |
2.81e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.55 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIK----------KGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTT-----GrsIIRlhdVTS 71
Cdd:COG4586 2 IEVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltG--ILV---PTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 72 GNILFDGKDIADLKeselKDYRKRMQIIF-Q------DpyasLnPTMNVFQIISEpmnIHGSYEKEEQKEiiLDLLKKVg 144
Cdd:COG4586 77 GEVRVLGYVPFKRR----KEFARRIGVVFgQrsqlwwD----L-PAIDSFRLLKA---IYRIPDAEYKKR--LDELVEL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 145 LKEEHLYRYP-HEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHI 223
Cdd:COG4586 142 LDLGELLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250
....*....|...
gi 1078707893 224 SDRIGVMYLGNIV 236
Cdd:COG4586 222 CDRVIVIDHGRII 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
32-258 |
2.91e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.47 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV-----TSGNILFDGKDIADlKESELKDYRKRMQIIFQDPyas 106
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 107 lNP-TMNVFQIISEPMNIHGSyeKEEQKEIILDLLKKVGLKEE---HLYRYPHEFSGGQRQRISIARALSVKPDFILCDE 182
Cdd:PRK14243 101 -NPfPKSIYDNIAYGARINGY--KGDMDELVERSLRQAALWDEvkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEEtgVTYLFIAHDLSMVRHISDRI----------GVMYlGNIVEIADSEDLYTKPAHPY 252
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTaffnveltegGGRY-GYLVEFDRTEKIFNSPQQQA 254
|
....*.
gi 1078707893 253 TQALLS 258
Cdd:PRK14243 255 TRDYVS 260
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-245 |
4.59e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.23 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNL-KKYfpikkglfGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTgRSII-RLHDVTSGNILFDGKDIADL 84
Cdd:COG4604 2 IEIKNVsKRY--------GGKV----VLDDVSLTIPKGGITALIGPNGAGKSTL-LSMIsRLLPPDSGEVLVDGLDVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 85 KESELKdyrKRMQIIFQDPyaSLNPTMNVFQIISepmniHGSYE------KEEQKEIILDLLKKVGLKE-EHlyRYPHEF 157
Cdd:COG4604 69 PSRELA---KRLAILRQEN--HINSRLTVRELVA-----FGRFPyskgrlTAEDREIIDEAIAYLDLEDlAD--RYLDEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV- 236
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVa 216
|
250
....*....|....*..
gi 1078707893 237 -----EIADSE---DLY 245
Cdd:COG4604 217 qgtpeEIITPEvlsDIY 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-236 |
7.26e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIkkglfGRKTEQlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKE 86
Cdd:COG1101 2 LELKNLSKTFNP-----GTVNEK-RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SelkdyrKRMQII---FQDPYASLNPTMNVFQIIS------EPMNIHGSYEKEEqKEIILDLLKKVGL--------KEEH 149
Cdd:COG1101 76 Y------KRAKYIgrvFQDPMMGTAPSMTIEENLAlayrrgKRRGLRRGLTKKR-RELFRELLATLGLglenrldtKVGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 150 LyryphefSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:COG1101 149 L-------SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIM 221
|
....*..
gi 1078707893 230 MYLGNIV 236
Cdd:COG1101 222 MHEGRII 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
32-244 |
1.04e-23 |
|
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: 96.83 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyRKRMQI--------IFqdp 103
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RARAGIayvpqgreIF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 yaslnPTMNVfqiisepmnihgsyekEEQKEIILDLLKKVGLK-EEHLY-RYP--HEF--------SGGQRQRISIARAL 171
Cdd:TIGR03410 88 -----PRLTV----------------EENLLTGLAALPRRSRKiPDEIYeLFPvlKEMlgrrggdlSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 172 SVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-262 |
1.22e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkeSELKDYRKRMQIIFQDPyaslnPTM 111
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF--SKLQGIRKLVGIVFQNP-----ETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFQIISE-----PMNIhgSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISA 186
Cdd:PRK13644 90 FVGRTVEEdlafgPENL--CLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 187 LDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVrHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALLSSMPE 262
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIE 240
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
37-240 |
1.85e-23 |
|
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: 96.08 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 37 SFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlkeSELKDYRKRMQIIFQDpyASLNPTMNVFQI 116
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-----TGLAPYQRPVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 117 ISepMNIHGSYE-KEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQV 195
Cdd:TIGR01277 91 IG--LGLHPGLKlNAEQQEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1078707893 196 VNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIAD 240
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-235 |
2.15e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 94.59 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdYRKRMQIIFQDpyaslnptMN 112
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDHVGYLPQD--------DE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 VFQ-IISEpmNIhgsyekeeqkeiildllkkvglkeehlyrypheFSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:cd03246 87 LFSgSIAE--NI---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1078707893 192 QAQVVNMLQDIQEEtGVTYLFIAHDLSMVRhISDRIGVMYLGNI 235
Cdd:cd03246 132 ERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-247 |
2.83e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQD 102
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQAISVVSQR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PY---ASLNPTMnvfqIISEPmnihgsyekEEQKEIILDLLKKVGLkeEHLYRYPH-----------EFSGGQRQRISIA 168
Cdd:PRK11160 423 VHlfsATLRDNL----LLAAP---------NASDEALIEVLQQVGL--EKLLEDDKglnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 169 RALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetGVTYLFIAHDLSMVRHIsDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-244 |
3.03e-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: 100.20 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPYASLNPT 110
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQEPYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQIisepmnihGSYEKEEQKEI--------ILDLLKKV--GLKEEhLYRYPHEFSGGQRQRISIARALSVKPDFILC 180
Cdd:TIGR01193 565 LENLLL--------GAKENVSQDEIwaaceiaeIKDDIENMplGYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQEEtgvTYLFIAHDLSmVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-222 |
5.59e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 99.72 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDgkDIADLKE 86
Cdd:PTZ00265 383 IQFKNVRFHYDTRK--------DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQDPYASLNPTMN------------------------------------------VFQIISEPMNIH 124
Cdd:PTZ00265 453 INLKWWRSKIGVVSQDPLLFSNSIKNnikyslyslkdlealsnyynedgndsqenknkrnscrakcagDLNDMSNTTDSN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 125 GSYEKEEQKEII-----LDLLKKVgLKEEHLYRYPHEF-----------SGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:PTZ00265 533 ELIEMRKNYQTIkdsevVDVSKKV-LIHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
250 260 270
....*....|....*....|....*....|....
gi 1078707893 189 VSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRH 222
Cdd:PTZ00265 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
26-236 |
1.01e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 26 KTEQLKA-------VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKdyrKRMQI 98
Cdd:PRK11231 4 RTENLTVgygtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 99 IFQDPyasLNPT-MNVFQIIS---EPMNIHGSYEKEEQKEIILDLLKKVGLkeEHLYRYP-HEFSGGQRQRISIARALSV 173
Cdd:PRK11231 81 LPQHH---LTPEgITVRELVAygrSPWLSLWGRLSAEDNARVNQAMEQTRI--NHLADRRlTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 174 KPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-249 |
1.27e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGR--SIIRLHDVTSGNILFDGKDI 81
Cdd:PRK13549 3 EYLLEMKNITKTFG-----------GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 --ADLKESElkdyRKRMQIIFQDpyASLNPTMNVFQII---SEP-----MNIHGSYEKEEQkeiildLLKKVGLkEEHLY 151
Cdd:PRK13549 72 qaSNIRDTE----RAGIAIIHQE--LALVKELSVLENIflgNEItpggiMDYDAMYLRAQK------LLAQLKL-DINPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 152 RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVmy 231
Cdd:PRK13549 139 TPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICV-- 215
|
250
....*....|....*...
gi 1078707893 232 lgniveIADSEDLYTKPA 249
Cdd:PRK13549 216 ------IRDGRHIGTRPA 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-245 |
1.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.77 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 26 KTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDiadLKESELKDYRKRMQIIFQDPYA 105
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWNLRRKIGMVFQNPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 106 SLnPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLkeEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPIS 185
Cdd:PRK13642 93 QF-VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 186 ALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLY 245
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
33-236 |
1.79e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSI---IRlhdVTSGNILFDGKDIADLKESELKDYRKRM-QiifqdpYASLN 108
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLS---PDSGEVRLNGRPLADWSPAELARRRAVLpQ------HSSLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 109 PTMNVFQIISepMN-IHGSYEKEEQKEIILDLLKKVGLkeEHL-YRYPHEFSGGQRQRISIARAL------SVKPDFILC 180
Cdd:PRK13548 89 FPFTVEEVVA--MGrAPHGLSRAEDDALVAAALAQVDL--AHLaGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
31-236 |
2.87e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDI-ADLKESELKDYRKRMQIIFQDPYASLNP 109
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TMNVFQIISEPMNIHGSyeKEEQKEIILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVS--QEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1078707893 190 SVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK13649 179 KGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
32-217 |
3.07e-22 |
|
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: 97.05 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPYaslnptm 111
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAH------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 nVFQI-ISEPMNIHgsyEKEEQKEIILDLLKKVGLkEEHLYRYPH-----------EFSGGQRQRISIARALSVKPDFIL 179
Cdd:TIGR02868 420 -LFDTtVRENLRLA---RPDATDEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 1078707893 180 CDEPISALDVSVQAQVVNMLQDIQEETGVtyLFIAHDL 217
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALSGRTV--VLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-237 |
5.68e-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: 90.84 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESelkdYRKRMQIIFQD 102
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PYAsLNPTmnvfqiisepmnihgsyekeeqkeiildLLKKVGLKeehlyrypheFSGGQRQRISIARALSVKPDFILCDE 182
Cdd:cd03247 84 PYL-FDTT----------------------------LRNNLGRR----------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEETgvTYLFIAHDLSMVRHIsDRIGVMYLGNIVE 237
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
38-254 |
6.53e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 91.84 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 38 FTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDiADLKESELKDYRKRMQIIFQDPyaslnptMNVFQ-I 116
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-PGKGWRHIGYVPQRHEFAWDFP-------ISVAHtV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 117 ISEPMNIHGSYEKEEQKEIIL--DLLKKVGLkeEHLYRYP-HEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQA 193
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADFAAvrDALRRVGL--TELADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 194 QVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIgVMYLGNIveIADSEDLYTKPAHPYTQ 254
Cdd:TIGR03771 151 LLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRV--IADGTPQQLQDPAPWMT 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
35-235 |
1.16e-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: 91.38 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKEselKDYRKRMQIIFQDP----------- 103
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH---KYLHSKVSLVGQEPvlfarslqdni 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 -YASLNPTMNVFQIISEPMNIHgSYEKEEQKEIILDllkkVGLKEEHLyryphefSGGQRQRISIARALSVKPDFILCDE 182
Cdd:cd03248 109 aYGLQSCSFECVKEAAQKAHAH-SFISELASGYDTE----VGEKGSQL-------SGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEETgvTYLFIAHDLSMVRHiSDRIGVMYLGNI 235
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-244 |
5.30e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.57 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:PRK13647 2 DNIIEVEDLHFRYK----------DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESELkdyRKRMQIIFQDPYASLNpTMNVFQIIS-EPMNIhgSYEKEEQKEIILDLLKKVGLKEeHLYRYPHEFSGGQR 162
Cdd:PRK13647 72 ENEKWV---RSKVGLVFQDPDDQVF-SSTVWDDVAfGPVNM--GLDKDEVERRVEEALKAVRMWD-FRDKPPYHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
..
gi 1078707893 243 DL 244
Cdd:PRK13647 224 LL 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-227 |
2.42e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.58 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTeQLKAVDdlsFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKEselkDYRkrmqIIFQD 102
Cdd:PRK11247 22 YGERT-VLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE----DTR----LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 pyASLNPTMNVfqIISEPMNIHGSYekeeqKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDE 182
Cdd:PRK11247 90 --ARLLPWKKV--IDNVGLGLKGQW-----RDAALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRI 227
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-264 |
4.71e-20 |
|
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: 90.27 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGR--SIIRLHDVTSGNILFDGkdiAD 83
Cdd:TIGR02633 1 LLEMKGIVKTF-----------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSG---SP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESELKDY-RKRMQIIFQDpyASLNPTMNVFQIISEPMNIHGSYEKEEQKEIIL---DLLKKVGLKEEHLYRYPHEFSG 159
Cdd:TIGR02633 67 LKASNIRDTeRAGIVIIHQE--LTLVPELSVAENIFLGNEITLPGGRMAYNAMYLrakNLLRELQLDADNVTRPVGDYGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 160 GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVmylgniveIA 239
Cdd:TIGR02633 145 GQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICV--------IR 215
|
250 260
....*....|....*....|....*
gi 1078707893 240 DSEDLYTKPAhpytqallSSMPEPD 264
Cdd:TIGR02633 216 DGQHVATKDM--------STMSEDD 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-247 |
4.83e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 90.25 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkglfgrktEQLKAVDDLSFTIKKGETFGLVGESGCGKS--------------TTGRSIIRLH----- 67
Cdd:TIGR03269 1 IEVKNLTKKF-----------DGKEVLKNISFTIEEGEVLGILGRSGAGKSvlmhvlrgmdqyepTSGRIIYHVAlcekc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 68 ---DVTSgnilFDGK--------------DIADLKESELKDYRKRMQIIFQDPYAsLNPTMNVFQIISEPMNIHGsYEKE 130
Cdd:TIGR03269 70 gyvERPS----KVGEpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIG-YEGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 131 EQKEIILDLLKKVGLKEE--HLYRyphEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGV 208
Cdd:TIGR03269 144 EAVGRAVDLIEMVQLSHRitHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGI 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 1078707893 209 TYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-238 |
5.54e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.82 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKGLFGRKTEQLK-----------AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNIL 75
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGIlgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 76 FDGKDIADLkeselkdyrkrmqiifqDPYASLNPTM----NVFqiisepMN--IHGsYEKEEQKEIILDLLKKVGLkEEH 149
Cdd:cd03220 81 VRGRVSSLL-----------------GLGGGFNPELtgreNIY------LNgrLLG-LSRKEIDEKIDEIIEFSEL-GDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 150 LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeETGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:cd03220 136 IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALV 214
|
....*....
gi 1078707893 230 MYLGNIVEI 238
Cdd:cd03220 215 LEKGKIRFD 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-248 |
5.65e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.16 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPY------- 104
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPFlfsdtva 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 ---ASLNPTMNVFQI--ISEPMNIHgsyekeeqkEIILDL----LKKVGLKEEHLyryphefSGGQRQRISIARALSVKP 175
Cdd:PRK10789 407 nniALGRPDATQQEIehVARLASVH---------DDILRLpqgyDTEVGERGVML-------SGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 176 DFILCDEPISALDVSVQAQVVNMLQdiQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTKP 248
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
33-247 |
6.13e-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: 90.10 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGkdiADLKESELKDYRKRMQIIFQDpyaslnptMN 112
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQWDRETFGKHIGYLPQD--------VE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 VFQ-IISEpmNIhGSYEKEEQKEIILDLLKKVGLKEEHLyRYPHEF-----------SGGQRQRISIARALSVKPDFILC 180
Cdd:TIGR01842 403 LFPgTVAE--NI-ARFGENADPEKIIEAAKLAGVHELIL-RLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHIsDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEVLAK 543
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-247 |
7.33e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.57 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPYA-SLNPTMNVf 114
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLfSGTVRFNL- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 115 qiisEPMNIHG------SYEKEEQKEIILDllKKVGLKEEhLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:PLN03130 1334 ----DPFNEHNdadlweSLERAHLKDVIRR--NSLGLDAE-VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 189 VSVQAqvvnMLQD-IQEE-TGVTYLFIAHDLSMVrhI-SDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:PLN03130 1407 VRTDA----LIQKtIREEfKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-280 |
7.57e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 87.25 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKD---------IADLKESELKDYRkrmqiifqd 102
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalqknlVAYVPQSEEVDWS--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 pyaslnptmnvFQIISEPMNIHGSY--------EKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVK 174
Cdd:PRK15056 93 -----------FPVLVEDVVMMGRYghmgwlrrAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 175 PDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIgVMYLGNIVEIADSEDLYTkpAHPYTQ 254
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFT--AENLEL 236
|
250 260
....*....|....*....|....*.
gi 1078707893 255 AlLSSMPEPDPTNAGKERIILEGEVP 280
Cdd:PRK15056 237 A-FSGVLRHVALNGSEESIITDDERP 261
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-244 |
9.94e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 31 KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyRKRMQIIFQDPYASLNPT 110
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA----RARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQIISEPMNIHGSYEKEEQKEIILDLLKKVGLkeEHLY-RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALD- 188
Cdd:PRK10895 93 LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLRdSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDp 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 189 VSVQ--AQVVNMLQDiqeeTGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:PRK10895 171 ISVIdiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-230 |
1.09e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.58 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFpikKGLFgrkteqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLK 85
Cdd:PRK11300 5 LLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 ESELKdyRKRMQIIFQDpyASLNPTMNVFQ--IISEPMN-----IHG-----SYEKEEQK--EIILDLLKKVGLKEeHLY 151
Cdd:PRK11300 74 GHQIA--RMGVVRTFQH--VRLFREMTVIEnlLVAQHQQlktglFSGllktpAFRRAESEalDRAATWLERVGLLE-HAN 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 152 RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-243 |
1.17e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 5 NLIEVRNLKKYFPI--------KKGLFGRK---TEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGN 73
Cdd:COG1134 3 SMIEVENVSKSYRLyhepsrslKELLLRRRrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 74 ILFDGKdIADLKEselkdyrkrmqiiFQdpyASLNPTM----NVFqiisepMN--IHGsYEKEEQKEIILDLLKKVGLkE 147
Cdd:COG1134 83 VEVNGR-VSALLE-------------LG---AGFHPELtgreNIY------LNgrLLG-LSRKEIDEKFDEIVEFAEL-G 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 148 EHLY----RYphefSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHI 223
Cdd:COG1134 138 DFIDqpvkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|
gi 1078707893 224 SDRIGVMYLGNIVEIADSED 243
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEE 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
33-274 |
3.11e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKdyrKRMQIIFQDpyASLNPTMN 112
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQD--TSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 VFQIISEPMNIHGS---YEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PRK09536 94 VRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 190 SVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKP-------------AHPYTQA- 255
Cdd:PRK09536 173 NHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlraafdartavgTDPATGAp 251
|
250
....*....|....*....
gi 1078707893 256 LLSSMPEPDPTNAGKERII 274
Cdd:PRK09536 252 TVTPLPDPDRTEAAADTRV 270
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
33-217 |
4.85e-19 |
|
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: 84.75 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGN--ILFD----GKDIADLkeselkdyRKRMQIIFQDPYAS 106
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGerrgGEDVWEL--------RKRIGLVSPALQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 107 LNPTMNVFQ-IISEPMNIHGSYEK--EEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:COG1119 91 FPRDETVLDvVLSGFFDSIGLYREptDEQRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190
....*....|....*....|....*....|....
gi 1078707893 184 ISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDL 217
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-277 |
6.19e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKST-----TGrsiirLHDVTSGNILFD 77
Cdd:COG3845 2 MPPALELRGITKRFG-----------GVVANDDVSLTVRPGEIHALLGENGAGKSTlmkilYG-----LYQPDSGEILID 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 78 GK--DIADLKESelkdyRKR---MqiIFQDPyaSLNPTMNVFQ-II--SEPMNiHGSYEKEEQKEIILDLLKKVGLKEEh 149
Cdd:COG3845 66 GKpvRIRSPRDA-----IALgigM--VHQHF--MLVPNLTVAEnIVlgLEPTK-GGRLDRKAARARIRELSERYGLDVD- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 150 LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALdvSVQ--AQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRI 227
Cdd:COG3845 135 PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 228 GVMYLGNIVEIADSEDLytkpahpyTQALLSSM---------PEPDPTNAGKERIILEG 277
Cdd:COG3845 212 TVLRRGKVVGTVDTAET--------SEEELAELmvgrevllrVEKAPAEPGEVVLEVEN 262
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-234 |
1.07e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 9 VRNLKKYFPIKKgLFgrkteqlkavDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNI-------------- 74
Cdd:COG0488 1 LENLSKSFGGRP-LL----------DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsipkglrigylpqe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 75 --LFDGKDIADLKES---ELKDYRKRMQIIFQDPyASLNPTMNVFQIISEPMNIHGSYEKEEQKEIILDLLkkvGLKEEH 149
Cdd:COG0488 70 ppLDDDLTVLDTVLDgdaELRALEAELEELEAKL-AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGL---GFPEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 150 LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDvsvqAQVVNMLQD-IQEETGvTYLFIAHDLSMVRHISDRI- 227
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSHDRYFLDRVATRIl 220
|
250
....*....|...
gi 1078707893 228 ------GVMYLGN 234
Cdd:COG0488 221 eldrgkLTLYPGN 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-236 |
1.11e-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: 83.09 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 25 RKTEQLKAVDDLSFTIKKGETFGLVGESGCGKST-----TGRsiIRLHDVTSGNILFDGKdiadlkESELKDYRKRMQII 99
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaiSGR--VEGGGTTSGQILFNGQ------PRKPDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 100 FQDPYasLNPTMNVFQIISEPMNIHGSYEK-EEQKEIILDLlkkVGLKEEHLYRYPHEF----SGGQRQRISIARALSVK 174
Cdd:cd03234 87 RQDDI--LLPGLTVRETLTYTAILRLPRKSsDAIRKKRVED---VLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 175 PDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-235 |
1.17e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFpikkglfgRKTEQLKAVDdlsFTIKKGETFGLVGESGCGKST---------TGRSIIRLHDVTSGN- 73
Cdd:PRK09984 2 QTIIRVEKLAKTF--------NQHQALHAVD---LNIHHGEMVALLGPSGSGKSTllrhlsgliTGDKSAGSHIELLGRt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 74 ILFDGKDIADLKESelkdyRKRMQIIFQ--DPYASLNPTMNVF--QIISEPM-NIHGSYEKEEQKEIILDLLKKVGLKEe 148
Cdd:PRK09984 71 VQREGRLARDIRKS-----RANTGYIFQqfNLVNRLSVLENVLigALGSTPFwRTCFSWFTREQKQRALQALTRVGMVH- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 149 HLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIG 228
Cdd:PRK09984 145 FAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
....*..
gi 1078707893 229 VMYLGNI 235
Cdd:PRK09984 225 ALRQGHV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
33-215 |
1.71e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILF-DGKDIadlkeselkdyrkrmqiIF--QDPY---AS 106
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------------LFlpQRPYlplGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 107 LnptmnvFQIISEPmNIHGSYEKEEqkeiILDLLKKVGLkeEHL-------YRYPHEFSGGQRQRISIARALSVKPDFIL 179
Cdd:COG4178 442 L------REALLYP-ATAEAFSDAE----LREALEAVGL--GHLaerldeeADWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*.
gi 1078707893 180 CDEPISALDVSVQAQVVNMLQdiQEETGVTYLFIAH 215
Cdd:COG4178 509 LDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-244 |
2.19e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 10 RNLKKYFPIKKGLFGR---KTEQL---KAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIad 83
Cdd:COG1129 239 RELEDLFPKRAAAPGEvvlEVEGLsvgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 lkesELKDYRKRMQ--IIfqdpYAS-------LNPTMNVFQIISepMNIHGSYEK------EEQKEIILDLLKKVGLKEE 148
Cdd:COG1129 317 ----RIRSPRDAIRagIA----YVPedrkgegLVLDLSIRENIT--LASLDRLSRgglldrRRERALAEEYIKRLRIKTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 149 HLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIG 228
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRIL 465
|
250
....*....|....*.
gi 1078707893 229 VMYLGNIVEIADSEDL 244
Cdd:COG1129 466 VMREGRIVGELDREEA 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-244 |
3.73e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKdyRKRMQIIFQDPYASlnpTMNVFQ 115
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA--RKVAYLPQQLPAAE---GMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 116 IIS---EPMniHGSYEK--EEQKEIILDLLKKVGLKEeHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVS 190
Cdd:PRK10575 105 LVAigrYPW--HGALGRfgAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 191 VQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDL 244
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-262 |
4.88e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 85.03 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPyASLNPTMNvFQ 115
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQSP-VLFSGTVR-FN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 116 IisEPMNIHGSYE--KEEQKEIILDLLKK--VGLKEEhLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:PLN03232 1330 I--DPFSEHNDADlwEALERAHIKDVIDRnpFGLDAE-VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 192 QAQVVNMLQdiQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALLSSMPE 262
Cdd:PLN03232 1407 DSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-244 |
7.58e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 20 KGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLkeselkDYRKRMQ-- 97
Cdd:COG3845 261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL------SPRERRRlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 98 --IIFQDPYAS-LNPTMNVFQiisepmN-IHGSYEKEE-QKEIILDLlKKVGLKEEHL---Y--RYPHE------FSGGQ 161
Cdd:COG3845 335 vaYIPEDRLGRgLVPDMSVAE------NlILGRYRRPPfSRGGFLDR-KAIRAFAEELieeFdvRTPGPdtparsLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADS 241
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPA 486
|
...
gi 1078707893 242 EDL 244
Cdd:COG3845 487 AEA 489
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-236 |
8.82e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKdyrKRMQIIFQD 102
Cdd:PRK10253 17 YGKYT----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 pyASLNPTMNVFQIISEPMNIHG---SYEKEEQKEIILDLLKKVGLKeeHLYRYPHE-FSGGQRQRISIARALSVKPDFI 178
Cdd:PRK10253 90 --ATTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGIT--HLADQSVDtLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 179 LCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-243 |
9.57e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTtgrsiirLHDVTS---------GNILF 76
Cdd:NF040905 1 ILEMRGITKTFP-----------GVKALDDVNLSVREGEIHALCGENGAGKST-------LMKVLSgvyphgsyeGEILF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 77 DGKDIA--DLKESElkdyRKRMQIIFQD----PYASlnptmnvfqiISEpmNI--------HGSYEKEEQKEIILDLLKK 142
Cdd:NF040905 63 DGEVCRfkDIRDSE----ALGIVIIHQElaliPYLS----------IAE--NIflgnerakRGVIDWNETNRRARELLAK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 143 VGLKEEhlyryPHEFSG----GQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLS 218
Cdd:NF040905 127 VGLDES-----PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLN 200
|
250 260
....*....|....*....|....*
gi 1078707893 219 MVRHISDRIGVMYLGNIVEIADSED 243
Cdd:NF040905 201 EIRRVADSITVLRDGRTIETLDCRA 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-215 |
3.06e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.58 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNIlfdgkdiadlkeselkDYRKRMQIIF--QDPYASLnpt 110
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------GMPEGEDLLFlpQRPYLPL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 mnvfqiisepmnihGSyekeeqkeiildllkkvgLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVS 190
Cdd:cd03223 78 --------------GT------------------LREQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....*
gi 1078707893 191 VQAQVVNMLQdiqeETGVTYLFIAH 215
Cdd:cd03223 126 SEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-235 |
3.09e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKEselkdyRKRMQI-------------IFQ 101
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST------AQRLARglvylpedrqssgLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 102 DpyASLnpTMNVfqiISEPMNIHGSYEKEEQKEIILDLLKK-VGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILC 180
Cdd:PRK15439 355 D--APL--AWNV---CALTHNRRGFWIKPARENAVLERYRRaLNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
6.89e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.53 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 1 MHEENLIEVRNLK---KYFPIKKGLfgrkteqlkavddlSFTIKKGETFGLVGESGCGKSTTGRsIIRLH---DVTSGNI 74
Cdd:CHL00131 2 NKNKPILEIKNLHasvNENEILKGL--------------NLSINKGEIHAIMGPNGSGKSTLSK-VIAGHpayKILEGDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 75 LFDGKDIADLKESElkdyRKRMQII--FQDPYASlnPTMNVFQIISEPMNI-HGSYEKEEQK-----EIILDLLKKVGLK 146
Cdd:CHL00131 67 LFKGESILDLEPEE----RAHLGIFlaFQYPIEI--PGVSNADFLRLAYNSkRKFQGLPELDpleflEIINEKLKLVGMD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 147 EEHLYRYPHE-FSGGQRQRISIARALSVKPDFILCDEPISALDVS---VQAQVVNMLQDIQEetgvTYLFIAHDLSMVRH 222
Cdd:CHL00131 141 PSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITHYQRLLDY 216
|
250 260
....*....|....*....|.
gi 1078707893 223 IS-DRIGVMYLGNIVEIADSE 242
Cdd:CHL00131 217 IKpDYVHVMQNGKIIKTGDAE 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-244 |
1.12e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPIkkglfgrkteqLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAD 83
Cdd:PRK09700 3 TPYISMAGIGKSFGP-----------VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 LKESElkDYRKRMQIIFQD------------PYASLNPTMNVFQIisepmNIHGSYEKEEQKEIildLLKKVGLKEEhLY 151
Cdd:PRK09700 72 LDHKL--AAQLGIGIIYQElsvideltvlenLYIGRHLTKKVCGV-----NIIDWREMRVRAAM---MLLRVGLKVD-LD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 152 RYPHEFSGGQRQRISIARALSVKPDFILCDEPISAL-DVSVQAQVVNMLQDIQEETGVTYlfIAHDLSMVRHISDRIGVM 230
Cdd:PRK09700 141 EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVY--ISHKLAEIRRICDRYTVM 218
|
250
....*....|....
gi 1078707893 231 YLGNIVEIADSEDL 244
Cdd:PRK09700 219 KDGSSVCSGMVSDV 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-215 |
1.66e-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: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 22 LFG--RKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKD--YRKrmq 97
Cdd:COG2401 33 AFGveLRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDaiGRK--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 98 iifQDPYASLNptmnvfqiisepmnihgsyekeeqkeiildLLKKVGLKEEHLY-RYPHEFSGGQRQRISIARALSVKPD 176
Cdd:COG2401 110 ---GDFKDAVE------------------------------LLNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1078707893 177 FILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAH 215
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-230 |
1.69e-16 |
|
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: 79.79 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDYrkrmqIIF--QDPyaSLNP- 109
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-----IGYlpQDV--ELFDg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TmnvfqiISEpmNIHGSYEKEEQKeiILDLLKKVGLkeehlyrypHEF-------------------SGGQRQRISIARA 170
Cdd:COG4618 421 T------IAE--NIARFGDADPEK--VVAAAKLAGV---------HEMilrlpdgydtrigeggarlSGGQRQRIGLARA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 171 LSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHiSDRIGVM 230
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVL 539
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-229 |
2.73e-16 |
|
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: 77.06 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 39 TIKKGETFGLVGESGCGKSTtgrsIIRLhdvTSGNILFDGKDIadlkESELKDyrkrmqIIFQDPYASLNPTMNVFQIIS 118
Cdd:cd03237 21 SISESEVIGILGPNGIGKTT----FIKM---LAGVLKPDEGDI----EIELDT------VSYKPQYIKADYEGTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 119 EPMNIHG--SYEKEEqkeiILDLLKKVGLKEEHLyrypHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVV 196
Cdd:cd03237 84 SITKDFYthPYFKTE----IAKPLQIEQILDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|...
gi 1078707893 197 NMLQDIQEETGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-229 |
2.82e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 39 TIKKGETFGLVGESGCGKSTtgrsIIRLhdvTSGNILFDGKDIadlkESELKdyrkrmqIIFQDPYASLNPTMNVFQIIS 118
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTT----FAKL---LAGVLKPDEGEV----DPELK-------ISYKPQYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 119 E-PMNIHGSYEKEEqkeiildLLKKVGLkeEHLY-RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVV 196
Cdd:PRK13409 423 SiTDDLGSSYYKSE-------IIKPLQL--ERLLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170 180 190
....*....|....*....|....*....|...
gi 1078707893 197 NMLQDIQEETGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-244 |
3.27e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTtgrsiirLHDVTS------GNILFDGKdiaDLKESELKDYRKRMQIIFQDP---YAS 106
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTS-------LLNALLgflpyqGSLKINGI---ELRELDPESWRKHLSWVGQNPqlpHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 107 L--NPTMNVFQIisepmnihgsyeKEEQkeiILDLLKKVGLKeEHLYRYPH-----------EFSGGQRQRISIARALSV 173
Cdd:PRK11174 439 LrdNVLLGNPDA------------SDEQ---LQQALENAWVS-EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 174 KPDFILCDEPISALDVSVQAQVVNMLQdiQEETGVTYLFIAHDLSMVRHIsDRIGVMYLGNIVEIADSEDL 244
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-188 |
3.53e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKyfpikkgLFGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlke 86
Cdd:PRK13537 8 IDFRNVEK-------RYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SELKDYRKRMQIIFQdpYASLNPTMNVfqiiSEPMNIHGSY---EKEEQKEIILDLLKKVGLKEEHLYRYpHEFSGGQRQ 163
Cdd:PRK13537 73 SRARHARQRVGVVPQ--FDNLDPDFTV----RENLLVFGRYfglSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKR 145
|
170 180
....*....|....*....|....*
gi 1078707893 164 RISIARALSVKPDFILCDEPISALD 188
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
47-247 |
4.16e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 47 GLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIaDLKESELKDYRKRMQIIFQDPYASLNPTmNVFQIISEPMNIHGS 126
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPEQQIFYT-DIDSDIAFSLRNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 127 YEKEEQKEI--ILDLLKKVGLKEEHLYRYPHefsgGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQE 204
Cdd:PRK13638 109 PEAEITRRVdeALTLVDAQHFRHQPIQCLSH----GQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1078707893 205 EtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:PRK13638 185 Q-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-237 |
4.38e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 25 RKTEQLKA-VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlkeSELKDYRKRMQIIFQdp 103
Cdd:PRK13536 48 SKSYGDKAvVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLARARIGVVPQ-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 YASLNPTMNVfqiiSEPMNIHGSY---EKEEQKEIILDLLKKVGLKEEHLYRYPhEFSGGQRQRISIARALSVKPDFILC 180
Cdd:PRK13536 122 FDNLDLEFTV----RENLLVFGRYfgmSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLG-NIVE 237
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-235 |
1.33e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.17 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 2 HE--ENLIEVRNLKKYFPIKKglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD-VTSGNILFDG 78
Cdd:TIGR02633 251 HEigDVILEARNLTCWDVINP--------HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 79 KDIA--------DLKESELKDYRKRMQIIfQDPYASLNPTMNVFQIISEPMNIHGsyEKEEQkeIILDLLKKVGLKEEHL 150
Cdd:TIGR02633 323 KPVDirnpaqaiRAGIAMVPEDRKRHGIV-PILGVGKNITLSVLKSFCFKMRIDA--AAELQ--IIGSAIQRLKVKTASP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 151 YRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVM 230
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
....*
gi 1078707893 231 YLGNI 235
Cdd:TIGR02633 477 GEGKL 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-227 |
1.42e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 23 FGRKteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdiadlkeselkdyrkrMQIIFQD 102
Cdd:PRK09544 14 FGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------------LRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PYASLNPTMNVfqIISEPMNIHGSYEKEEqkeiILDLLKKVglKEEHLYRYP-HEFSGGQRQRISIARALSVKPDFILCD 181
Cdd:PRK09544 74 QKLYLDTTLPL--TVNRFLRLRPGTKKED----ILPALKRV--QAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1078707893 182 EPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRI 227
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-200 |
1.51e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlkesELKDYRKRMQiifqdpYAS----LNPT 110
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACH------YLGhrnaMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQIISEPMNIHGSYEKEeqkeiILDLLKKVGLKE-EHL-YRYpheFSGGQRQRISIARALSVK-PDFILcDEPISAL 187
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEELD-----IAAALEAVGLAPlAHLpFGY---LSAGQKRRVALARLLVSNrPIWIL-DEPTAAL 158
|
170
....*....|...
gi 1078707893 188 DVSVQAQVVNMLQ 200
Cdd:PRK13539 159 DAAAVALFAELIR 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
35-229 |
1.66e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDV--------------------------------------------- 69
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 70 ---------TSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPYASlnpTMNVFQIISepmnihgsYEKEEQKEIILDLL 140
Cdd:PTZ00265 1266 sgedstvfkNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPMLF---NMSIYENIK--------FGKEDATREDVKRA 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 141 KKVGLKEEHLYRYPHEF-----------SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVT 209
Cdd:PTZ00265 1332 CKFAAIDEFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKT 1411
|
250 260
....*....|....*....|
gi 1078707893 210 YLFIAHDLSMVRHiSDRIGV 229
Cdd:PTZ00265 1412 IITIAHRIASIKR-SDKIVV 1430
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-236 |
3.99e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.72 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTgrsIIRLHDVTS--GNILFDGKDIADLKESELKDYRK--RMQiifQDPYASlnptM 111
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPgqGEILLNGRPLSDWSAAELARHRAylSQQ---QSPPFA----M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFQIISepMNIHGSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARAL-----SVKPD--FILCDEPI 184
Cdd:COG4138 85 PVFQYLA--LHQPAGASSEAVEQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 185 SALDVsvqAQVVNMLQDIQE--ETGVTYLFIAHDLSM-VRHiSDRIGVMYLGNIV 236
Cdd:COG4138 162 NSLDV---AQQAALDRLLRElcQQGITVVMSSHDLNHtLRH-ADRVWLLKQGKLV 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-236 |
4.22e-15 |
|
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: 72.58 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYfpIKKGLFGRKTEQLKavdDLSFTIKKGETFGLVGESGCGKST-----TGRsIIRLHdvTSGNILFDGKDi 81
Cdd:cd03213 4 LSFRNLTVT--VKSSPSKSGKQLLK---NVSGKAKPGELTAIMGPSGAGKSTllnalAGR-RTGLG--VSGEVLINGRP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 adlkeSELKDYRKRMQIIFQDPYasLNPTMNVFQIISEPMNIHGsyekeeqkeiildllkkvglkeehlyrypheFSGGQ 161
Cdd:cd03213 75 -----LDKRSFRKIIGYVPQDDI--LHPTLTVRETLMFAAKLRG-------------------------------LSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeETGVTYLFIAHDLS-MVRHISDRIGVMYLGNIV 236
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
35-244 |
5.94e-15 |
|
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: 75.75 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPY---ASLNPTM 111
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVlfsGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFqiisepmnihGSYEkEEQKEIILDLLKKVGLKEEHLYRYPHE-------FSGGQRQRISIARALSVKPDFILCDEPI 184
Cdd:TIGR00957 1381 DPF----------SQYS-DEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 185 SALDVS----VQAQVVNMLQDiqeetgVTYLFIAHDLSMVRHISdRIGVMYLGNIVEIADSEDL 244
Cdd:TIGR00957 1450 AAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-236 |
6.34e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 29 QLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESElkdyrkrmqiIFQDPYASLN 108
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK----------IMREAVAIVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 109 PTMNVFQ--IISEPMNIHGSYEKEEQK----EIILDLLKKvgLKEEHLYRyPHEFSGGQRQRISIARALSVKPDFILCDE 182
Cdd:PRK11614 87 EGRRVFSrmTVEENLAMGGFFAERDQFqeriKWVYELFPR--LHERRIQR-AGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 183 PISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-243 |
1.45e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYfpikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAd 83
Cdd:PRK09700 263 ETVFEVRNVTSR-------------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 84 lKESELKDYRKRMQIIFQD-------PYASLNPTMNVFQIISEPmNIHGSY----EKEEQKeIILDLLKKVGLKEEHLYR 152
Cdd:PRK09700 329 -PRSPLDAVKKGMAYITESrrdngffPNFSIAQNMAISRSLKDG-GYKGAMglfhEVDEQR-TAENQRELLALKCHSVNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 153 YPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYL 232
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCE 484
|
250
....*....|.
gi 1078707893 233 GNIVEIADSED 243
Cdd:PRK09700 485 GRLTQILTNRD 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-229 |
3.98e-14 |
|
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: 72.89 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 39 TIKKGETFGLVGESGCGKSTtgrsIIRLhdvTSGNILFDGKDIadlkESELKdyrkrmqIIFQDPYASLNPTMNVFQIIS 118
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT----FAKI---LAGVLKPDEGEV----DEDLK-------ISYKPQYISPDYDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 119 E--PMNIHGSYEKEEqkeiildLLKKVGLkeEHLY-RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQV 195
Cdd:COG1245 424 SanTDDFGSSYYKTE-------IIKPLGL--EKLLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180 190
....*....|....*....|....*....|....
gi 1078707893 196 VNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-255 |
7.31e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.44 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIK-----KGET--FGLvgeSGCGKST------------TGRsiIRLhdvtSGNILFD-GKDIAdlkeseLKDYRK 94
Cdd:PRK11144 12 DLCLTVNltlpaQGITaiFGR---SGAGKTSlinaisgltrpqKGR--IVL----NGRVLFDaEKGIC------LPPEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 95 RMQIIFQDpyASLNPTMNVfqiisePMNIHGSYEKE--EQKEIILDLLkkvGLkEEHLYRYPHEFSGGQRQRISIARALS 172
Cdd:PRK11144 77 RIGYVFQD--ARLFPHYKV------RGNLRYGMAKSmvAQFDKIVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 173 VKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPA-HP 251
Cdd:PRK11144 145 TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRP 224
|
....
gi 1078707893 252 YTQA 255
Cdd:PRK11144 225 WLPK 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-227 |
8.51e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPIKKgLFgrkteqlkavDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNIlfdgkdiadlk 85
Cdd:COG0488 315 VLELEGLSKSYGDKT-LL----------DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 eselkDYRKRMQIIF--QDpYASLNPTMNVFQIISEpmnihGSYEKEEQKeiILDLLKKVGLKEEHLYRYPHEFSGGQRQ 163
Cdd:COG0488 373 -----KLGETVKIGYfdQH-QEELDPDKTVLDELRD-----GAPGGTEQE--VRGYLGRFLFSGDDAFKPVGVLSGGEKA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 164 RISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeetGvTYLFIAHDLSMVRHISDRI 227
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRI 499
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-227 |
8.67e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTgrsIIRLHDVT--SGNILFDGKDIADLKESELKdyRKRMQIIFQDPYASLnptMNV 113
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMAGLLpgSGSIQFAGQPLEAWSAAELA--RHRAYLSQQQTPPFA---MPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 114 FQIISepMNIHGSYEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARA-LSVKPD------FILCDEPISA 186
Cdd:PRK03695 87 FQYLT--LHQPDKTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPMNS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1078707893 187 LDVsvqAQVVNMLQDIQE--ETGVTYLFIAHDLSMVRHISDRI 227
Cdd:PRK03695 164 LDV---AQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRV 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-230 |
9.75e-14 |
|
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: 69.28 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 27 TEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdIADLKESELKDYRKRMQIIF--QDPY 104
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAYaaQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 AsLNPTMNVFQIISEPMNihgsyeKEEQKEII--------LDLL-----KKVGLKEEHLyryphefSGGQRQRISIARAL 171
Cdd:cd03290 90 L-LNATVEENITFGSPFN------KQRYKAVTdacslqpdIDLLpfgdqTEIGERGINL-------SGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 172 SVKPDFILCDEPISALDVSV-----QAQVVNMLQDIQEetgvTYLFIAHDLSMVRHiSDRIGVM 230
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAM 214
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
40-253 |
1.07e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 69.94 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 40 IKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKeseLKDYRKRMQIIFQDPYaslnptmnvfqIISE 119
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPI-----------LFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 120 PMNIHGSYEKEEQKEIILDLLKKVGLK----------EEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:cd03288 110 SIRFNLDPECKCTDDRLWEALEIAQLKnmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 190 SVQaqvvNMLQDI-----QEETGVTylfIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTKPAHPYT 253
Cdd:cd03288 190 ATE----NILQKVvmtafADRTVVT---IAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-230 |
1.69e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 68.26 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 18 IKKGLFG---RKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdIAdlkeselkdyrk 94
Cdd:cd03250 3 VEDASFTwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IA------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 95 rmqiifqdpYAS-----LNPTmnvfqiISEpmNI--HGSYEKEEQKEII--------LDLLKK-----VGLKEEHLyryp 154
Cdd:cd03250 70 ---------YVSqepwiQNGT------IRE--NIlfGKPFDEERYEKVIkacalepdLEILPDgdlteIGEKGINL---- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 155 hefSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLqdIQEE--TGVTYLFIAHDLSMVRHiSDRIGVM 230
Cdd:cd03250 129 ---SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLllNNKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-227 |
4.57e-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: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFPIKKgLFgrkteqlkavDDLSFTIKKGETFGLVGESGCGKSTtgrsiirlhdvtsgnilfdgkdiadlke 86
Cdd:cd03221 1 IELENLSKTYGGKL-LL----------KDISLTINPGDRIGLVGRNGAGKST---------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 selkdyrkrmqiifqdpyaslnptmnVFQIISEPMnihgsyeKEEQKEIILDLLKKVGlkeehlyrYPHEFSGGQRQRIS 166
Cdd:cd03221 42 --------------------------LLKLIAGEL-------EPDEGIVTWGSTVKIG--------YFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078707893 167 IARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQeetGvTYLFIAHDLSMVRHISDRI 227
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP---G-TVILVSHDRYFLDQVATKI 137
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-271 |
6.03e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.81 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQIIFQDPY---ASLNPTMN 112
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPVlfdGTVRQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 VFQiisepmnihgsyekEEQKEIILDLLKKVGLKEehlyRYPHE--------------FSGGQRQRISIARALSVK-PDF 177
Cdd:PTZ00243 1406 PFL--------------EASSAEVWAALELVGLRE----RVASEsegidsrvleggsnYSVGQRQLMCMARALLKKgSGF 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 178 ILCDEPIS----ALDVSVQAQVVNMLqdiqeeTGVTYLFIAHDLSMVRHIsDRIGVMYLGNIVEIADSEDLYTKPahpyt 253
Cdd:PTZ00243 1468 ILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR----- 1535
|
250
....*....|....*...
gi 1078707893 254 QALLSSMPEPDPTNAGKE 271
Cdd:PTZ00243 1536 QSIFHSMVEALGRSEAKR 1553
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-236 |
8.90e-13 |
|
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: 66.13 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 22 LFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVT---SGNILFDGKDIADLKEselkdyRKRMQI 98
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE------KYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 99 IFQDPYASLNPTMNVFQIISEPMNIHGSyekeeqkeiilDLLKKVglkeehlyryphefSGGQRQRISIARALSVKPDFI 178
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRCKGN-----------EFVRGI--------------SGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 179 LCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLS-MVRHISDRIGVMYLGNIV 236
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-221 |
1.37e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.33 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILF-DGKDIADL-KESELKDyrkRMQIIFQDPYaslnp 109
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVpQRSEVPD---SLPLTVRDLV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 TMNVFQiisePMNIHGSYEKEEQKEIIlDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:NF040873 79 AMGRWA----RRGLWRRLTRDDRAAVD-DALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|..
gi 1078707893 190 SVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVR 221
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-242 |
1.59e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlkeSELKDYRKRMQIIFQDpyaslnptm 111
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYRKLFSAVFTD--------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 nvFQIISEPMNIHGSYEKEEQKEIILDLLK---KVGLKEEHLYRYphEFSGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:PRK10522 406 --FHLFDQLLGPEGKPANPALVEKWLERLKmahKLELEDGRISNL--KLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 189 VSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSE 242
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELTGEE 534
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
33-250 |
1.62e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSI-------IRLHDVT-SGNILFDGKDIADLKESELKDYRKRMQIIFQDPY 104
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltggGAPRGARvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 AslnptMNVFQIIS---EPMNIHGSYEKEEQKEIILDLLKKVGlKEEHLYRYPHEFSGGQRQRISIARALS--------- 172
Cdd:PRK13547 97 A-----FSAREIVLlgrYPHARRAGALTHRDGEIAWQALALAG-ATALVGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 173 VKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTkPAH 250
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-235 |
2.16e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPIKKGLfgrkteqlKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSII-RLHDVTSGNILFDGKD-- 80
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHI--------KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPvk 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 81 -----------IADLKESelkdyRKRMQIIFQDPYASlNPTMNVFQIISEPMNIHGSyekEEQKeIILDLLKKVGLKEEH 149
Cdd:PRK13549 329 irnpqqaiaqgIAMVPED-----RKRDGIVPVMGVGK-NITLAALDRFTGGSRIDDA---AELK-TILESIQRLKVKTAS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 150 LYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLV 477
|
....*.
gi 1078707893 230 MYLGNI 235
Cdd:PRK13549 478 MHEGKL 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-244 |
2.78e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 3 EENLIEV---RNLKKYFP---IKKGLFGRKTEQLKA--VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNI 74
Cdd:PRK10762 230 EDSLIEMmvgRKLEDQYPrldKAPGEVRLKVDNLSGpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 75 LFDGKDIADLKESELKDY--------RKRMQIIFQdpyaslnptMNVfqiiSEPMNI---------HGSYEKEEQKEIIL 137
Cdd:PRK10762 310 TLDGHEVVTRSPQDGLANgivyisedRKRDGLVLG---------MSV----KENMSLtalryfsraGGSLKHADEQQAVS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 138 DLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDL 217
Cdd:PRK10762 377 DFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEM 455
|
250 260 270
....*....|....*....|....*....|..
gi 1078707893 218 SMVRHISDRIGVMYLGNI-----VEIADSEDL 244
Cdd:PRK10762 456 PEVLGMSDRILVMHEGRIsgeftREQATQEKL 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-243 |
8.36e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFPikkglfgrKTEQLKAVDdlsFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLk 85
Cdd:PRK15439 11 LLCARSISKQYS--------GVEVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 eSELKDYRKRMQIIFQDPYasLNPTMNVFQIISEPMNIH-GSYEKEEQK----EIILDLLKKVGLKEEhlyryphefsgG 160
Cdd:PRK15439 79 -TPAKAHQLGIYLVPQEPL--LFPNLSVKENILFGLPKRqASMQKMKQLlaalGCQLDLDSSAGSLEV-----------A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALdvsVQAQVVNMLQDIQE--ETGVTYLFIAHDLSMVRHISDRIGVMYLGNIV-- 236
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIAls 221
|
....*...
gi 1078707893 237 -EIADSED 243
Cdd:PRK15439 222 gKTADLST 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-202 |
8.45e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 20 KGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKST-----TGRSiirLHDVT-SGNILFDGKDIadlkesELKDYR 93
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRS---PKGVKgSGSVLLNGMPI------DAKEMR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 94 KRMQIIFQDpyaSLN-PTMNVFQ--IISEPMNIHGSYEKEEQKEIILDLLKKVGLKE--------EHLYRyphEFSGGQR 162
Cdd:TIGR00955 99 AISAYVQQD---DLFiPTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcantrigvPGRVK---GLSGGER 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDI 202
Cdd:TIGR00955 173 KRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
36-217 |
9.14e-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: 63.15 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlkesELKDYRKRmQIIFQDPYASLNPTMNVFQ 115
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHE-NILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 116 IISEPMNIHGSyekeEQKEIiLDLLKKVGLKE-EHLyryP-HEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQA 193
Cdd:TIGR01189 93 NLHFWAAIHGG----AQRTI-EDALAAVGLTGfEDL---PaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|....
gi 1078707893 194 QVVNMLQDIQEETGVTYLFIAHDL 217
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-231 |
1.07e-11 |
|
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: 63.92 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 41 KKGETFGLVGESGCGKSTTGRsiIRLHDVTSGNILFDGKD-----IADLKESELKDYRKRM-----QIIFQDPYASLNP- 109
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALK--ILAGKLKPNLGKFDDPPdwdeiLDEFRGSELQNYFTKLlegdvKVIVKPQYVDLIPk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 110 --TMNVFQIISEPmnihgsyEKEEQKEIILDLLKKVGLKEEHLyrypHEFSGGQRQRISIARALSVKPDFILCDEPISAL 187
Cdd:cd03236 102 avKGKVGELLKKK-------DERGKLDELVDQLELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1078707893 188 DVSvqaQVVNMLQDIQE--ETGVTYLFIAHDLSMVRHISDRIGVMY 231
Cdd:cd03236 171 DIK---QRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-188 |
1.09e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKYFpikkGLFgrkTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNI-LF----DGKDI 81
Cdd:NF033858 267 IEARGLTMRF----GDF---T----AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFgqpvDAGDI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 82 ADlkeselkdyRKR---MQIIFqdpyaSLNPTMNVFQiisepmN--IHG---SYEKEEQKEIILDLLKKVGLkEEHLYRY 153
Cdd:NF033858 336 AT---------RRRvgyMSQAF-----SLYGELTVRQ------NleLHArlfHLPAAEIAARVAEMLERFDL-ADVADAL 394
|
170 180 190
....*....|....*....|....*....|....*
gi 1078707893 154 PHEFSGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:NF033858 395 PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-229 |
2.47e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 8 EVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGkdiadlKES 87
Cdd:PRK11288 6 SFDGIGKTFP-----------GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 88 ELKDYRKRMQ----IIFQDpyASLNPTMNVFQiisepmNI--------HGSYEKEEQKEIILDLLKKVGLKEEhlyryPH 155
Cdd:PRK11288 69 RFASTTAALAagvaIIYQE--LHLVPEMTVAE------NLylgqlphkGGIVNRRLLNYEAREQLEHLGVDID-----PD 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 156 ----EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGV 229
Cdd:PRK11288 136 tplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-237 |
3.05e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGET--------------FGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELkdyRKRMQ 97
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 98 IIFQDPyASLNPTMnvFQIISEPMNIhgsyeKEEQkeiILDLLKKVGLKE------EHLYRYPHE----FSGGQRQRISI 167
Cdd:PRK10790 419 MVQQDP-VVLADTF--LANVTLGRDI-----SEEQ---VWQALETVQLAElarslpDGLYTPLGEqgnnLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 168 ARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETgvTYLFIAHDLSMVRHiSDRIGVMYLGNIVE 237
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-231 |
3.94e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 39 TIKKGETFGLVGESGCGKSTtgrsIIRlhdVTSGNI---LFDGKDIADLKE-------SELKDYrkrmqiiFQDPY---- 104
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKST----ALK---ILSGELkpnLGDYDEEPSWDEvlkrfrgTELQDY-------FKKLAngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 -ASLNPTMnVFQIisePMNIHGS----YEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFIL 179
Cdd:COG1245 161 kVAHKPQY-VDLI---PKVFKGTvrelLEKVDERGKLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 180 CDEPISALDVSvqaQVVNMLQDIQE--ETGVTYLFIAHDLSMVRHISDRIGVMY 231
Cdd:COG1245 236 FDEPSSYLDIY---QRLNVARLIRElaEEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-230 |
5.30e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIA- 82
Cdd:PRK10762 2 QALLQLKGIDKAFP-----------GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 -DLKESElkdyRKRMQIIFQDpyasLN--PTMNVFQII---SEPMNIHGSYEKEEQKEIILDLLKKVGLKEeHLYRYPHE 156
Cdd:PRK10762 71 nGPKSSQ----EAGIGIIHQE----LNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRF-SSDKLVGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 157 FSGGQRQRISIARALSVKPDFILCDEPISAL-DVSVQA--QVVNMLQDiqEETGVTYlfIAHDLSMVRHISDRIGVM 230
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESlfRVIRELKS--QGRGIVY--ISHRLKEIFEICDDVTVF 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-236 |
5.70e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 20 KGLFGRKteqLKAvdDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGK--DIADLKES---------E 88
Cdd:PRK11288 261 DGLKGPG---LRE--PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAiragimlcpE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 89 lkDyRKRMQIIfqdPYASLNPTMNvfqiISEPMN-------IHGSYEKEEQKEIIldllKKVGLKEEHLYRYPHEFSGGQ 161
Cdd:PRK11288 336 --D-RKAEGII---PVHSVADNIN----ISARRHhlragclINNRWEAENADRFI----RSLNIKTPSREQLIMNLSGGN 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 162 RQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIV 236
Cdd:PRK11288 402 QQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-247 |
7.24e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 24 GRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdiadlkeselkdyrkrMQIIFQDp 103
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAIS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 yASLNPTMNVFQIISEPMNIHGsYEKEEQKEIILDLLKKVGLKEeHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEp 183
Cdd:PRK13546 94 -AGLSGQLTGIENIEFKMLCMG-FKRKEIKAMTPKIIEFSELGE-FIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 184 isALDVSVQAQVVNMLQDIQE--ETGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTK 247
Cdd:PRK13546 170 --ALSVGDQTFAQKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-227 |
8.29e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 34 DDLSFTIKKGETFGLVGESGCGKSTtgrsiirLHDVTSGNILFD-GKDI--ADLKESelkdyrkRMQiifQDPyaSLNPT 110
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKST-------LMKILNGEVLLDdGRIIyeQDLIVA-------RLQ---QDP--PRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 111 MNVFQIISEPMNIHGSYEKE----------EQKEIILDLLKKVGLKEEH--LYRY--------------PH----EFSGG 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRyhdishlvetDPSEKNLNELAKLQEQLDHhnLWQLenrinevlaqlgldPDaalsSLSGG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1078707893 161 QRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEetgvTYLFIAHDLSMVRHISDRI 227
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-264 |
1.22e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIAdlkeSELKDYRKRMQIIFQdpYASLNPTM 111
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQNMGYCPQ--FDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFQIISEPMNIHGSYEKEEQKeIILDLLKKVGLKeehLY--RYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:TIGR01257 2028 TGREHLYLYARLRGVPAEEIEK-VANWSIQSLGLS---LYadRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1078707893 190 SVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALLSSMPEPD 264
Cdd:TIGR01257 2104 QARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDD 2177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-287 |
1.32e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 10 RNLKKYFPikkglfgrkteQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIaDLKES-- 87
Cdd:PRK10982 2 SNISKSFP-----------GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSke 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 88 -----------ELKDYRKR------------MQIIFQDPYASLNPTMNVFqiisepmnihgsyekeEQKEIILDLLKKVG 144
Cdd:PRK10982 70 alengismvhqELNLVLQRsvmdnmwlgrypTKGMFVDQDKMYRDTKAIF----------------DELDIDIDPRAKVA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 145 lkeehlyryphEFSGGQRQRISIARALSVKPDFILCDEPISAL---DVSVQAQVVNMLQdiqeETGVTYLFIAHDLSMVR 221
Cdd:PRK10982 134 -----------TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLK----ERGCGIVYISHKMEEIF 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 222 HISDRIGVMYLGNIVEiadsedlyTKPAHPYTQALLSSMPE--------PDPTNAGKErIILEGEVPSPLNSPS 287
Cdd:PRK10982 199 QLCDEITILRDGQWIA--------TQPLAGLTMDKIIAMMVgrsltqrfPDKENKPGE-VILEVRNLTSLRQPS 263
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
33-222 |
1.60e-10 |
|
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: 62.07 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILfdgkdiadlkeselKDYRKRMQIIFQDPYASLNPTMN 112
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT--------------KPAKGKLFYVPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 vfQII----SEPMNIHGSYEKEEQKeiILDLLKKVGLKEEH-----LYRYPHEFSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:TIGR00954 534 --QIIypdsSEDMKRRGLSDKDLEQ--ILDNVQLTHILEREggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|....*....
gi 1078707893 184 ISALDVSVQAQVVNMLQDIqeetGVTYLFIAHDLSMVRH 222
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREF----GITLFSVSHRKSLWKY 644
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-231 |
2.34e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 39 TIKKGETFGLVGESGCGKSTtgrsIIRlhdVTSGNIL-----FDGKDIAD--LKE---SELKDYrkrmqiiFQDPY---- 104
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTT----AVK---ILSGELIpnlgdYEEEPSWDevLKRfrgTELQNY-------FKKLYngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 105 -ASLNPTMnVFQIisePMNIHGS----YEKEEQKEIILDLLKKVGLkEEHLYRYPHEFSGGQRQRISIARALSVKPDFIL 179
Cdd:PRK13409 161 kVVHKPQY-VDLI---PKVFKGKvrelLKKVDERGKLDEVVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 180 CDEPISALDVSVQAQVVNMLQDIQEETGVtyLFIAHDLSMVRHISDRIGVMY 231
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHDLAVLDYLADNVHIAY 285
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-244 |
2.69e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 2 HEE---NLIEVRNLKK----YFPIKKGLFGRKTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNI 74
Cdd:TIGR00957 616 HEElepDSIERRTIKPgegnSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 75 LFDGKDIADLKESELKDYRKRMQIIFQDPyasLNPtmNVFQIISEPMNIHGSYE---KEEQKEIildllkkvGLKEEHLy 151
Cdd:TIGR00957 696 HMKGSVAYVPQQAWIQNDSLRENILFGKA---LNE--KYYQQVLEACALLPDLEilpSGDRTEI--------GEKGVNL- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 152 ryphefSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVV-NMLQDIQEETGVTYLFIAHDLSMVRHIsDRIGVM 230
Cdd:TIGR00957 762 ------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVM 834
|
250
....*....|....
gi 1078707893 231 YLGNIVEIADSEDL 244
Cdd:TIGR00957 835 SGGKISEMGSYQEL 848
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-235 |
2.86e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.57 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 9 VRNLKKYFPIkkglFGRKteqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlkESE 88
Cdd:TIGR01257 931 VKNLVKIFEP----SGRP-----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETN 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 89 LKDYRKRMqiifqdpyaSLNPTMNVF---QIISEPMNIHGSYEKEEQKEIILD---LLKKVGLKEEHlYRYPHEFSGGQR 162
Cdd:TIGR01257 998 LDAVRQSL---------GMCPQHNILfhhLTVAEHILFYAQLKGRSWEEAQLEmeaMLEDTGLHHKR-NEEAQDLSGGMQ 1067
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 163 QRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLqdIQEETGVTYLFIAHDLSMVRHISDRIGVMYLGNI 235
Cdd:TIGR01257 1068 RKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-188 |
4.75e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 6 LIEVRNLKKYFP-----IKKGLFGRKTEQLKAV-DDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDvTSGNILFDGk 79
Cdd:TIGR01271 1202 VIENPHAQKCWPsggqmDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG- 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 80 diADLKESELKDYRKRMQIIFQDPYAsLNPTmnvFQIISEPmniHGSYEKEEqkeiILDLLKKVGLKEEhLYRYPHE--- 156
Cdd:TIGR01271 1280 --VSWNSVTLQTWRKAFGVIPQKVFI-FSGT---FRKNLDP---YEQWSDEE----IWKVAEEVGLKSV-IEQFPDKldf 1345
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1078707893 157 --------FSGGQRQRISIARALSVKPDFILCDEPISALD 188
Cdd:TIGR01271 1346 vlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-221 |
8.03e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIadlkESELKDYRKrmQIIFQDPYASLNPTMN 112
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK--QLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 113 VFQiiSEPMNIHGSYEKEEQKEIIldllkkVGLKEEHLYRYP-HEFSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:PRK13540 91 LRE--NCLYDIHFSPGAVGITELC------RLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180 190
....*....|....*....|....*....|
gi 1078707893 192 QAQVVNMLQDIQEETGVTYLFIAHDLSMVR 221
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-227 |
1.13e-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: 59.18 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 4 ENLIEVRNLKKyfpikkgLFGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILF-DGKDIA 82
Cdd:TIGR03719 320 DKVIEAENLTK-------AFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 83 DLKESElkdyrkrmqiifqdpyASLNPTMNVFQIISEPMNIH--GSYEKEEQKEIIL------DLLKKVGlkeehlyryp 154
Cdd:TIGR03719 389 YVDQSR----------------DALDPNKTVWEEISGGLDIIklGKREIPSRAYVGRfnfkgsDQQKKVG---------- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1078707893 155 hEFSGGQRQRISIARALSVKPDFILCDEPISALDV-SVQAqvvnmLQDIQEETGVTYLFIAHDlsmvRHISDRI 227
Cdd:TIGR03719 443 -QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA-----LEEALLNFAGCAVVISHD----RWFLDRI 506
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-224 |
1.35e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 34 DDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKEselkDYRkrmqiifQDP-----YASLN 108
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----EYH-------QDLlylghQPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 109 PTMNVFQIISEPMNIHGSYEKEEqkeiILDLLKKVGLKE-EHLyryP-HEFSGGQRQRISIAR-ALSVKPDFILcDEPIS 185
Cdd:PRK13538 87 TELTALENLRFYQRLHGPGDDEA----LWEALAQVGLAGfEDV---PvRQLSAGQQRRVALARlWLTRAPLWIL-DEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1078707893 186 ALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSM----VRHIS 224
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVasdkVRKLR 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
35-278 |
2.45e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDgKDIADL-KESELKDYRKRMQIIFQDP--YASLNPTM 111
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVpQQAWIMNATVRGNILFFDEedAARLADAV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFQIISEPMNIHGSYEKEeqkeiildllkkVGLKEEHLyryphefSGGQRQRISIARALSVKPDFILCDEPISALDVSV 191
Cdd:PTZ00243 757 RVSQLEADLAQLGGGLETE------------IGEKGVNL-------SGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 192 QAQVVnmlqdiqEE------TGVTYLFIAHDLSMVRHiSDRIGVMYLGNIVEIADSEDLYTKPAHPYTQALLssMPEPDP 265
Cdd:PTZ00243 818 GERVV-------EEcflgalAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAAEL--KENKDS 887
|
250
....*....|...
gi 1078707893 266 TNAGKERIILEGE 278
Cdd:PTZ00243 888 KEGDADAEVAEVD 900
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
36-240 |
2.69e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHD--VTSGNILFDGKDIADLKESELKDyrKRMQIIFQDPyASLNPTMNV 113
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAG--EGIFMAFQYP-VEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 114 FqIISEPMNIHGSYEKEEQ------KEIILDLLKKVGLKEEHLYRYPHE-FSGGQRQRISIARALSVKPDFILCDEPISA 186
Cdd:PRK09580 97 F-FLQTALNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1078707893 187 LDV---SVQAQVVNMLQDIQEetgvTYLFIAHDLSMVRHIS-DRIGVMYLGNIVEIAD 240
Cdd:PRK09580 176 LDIdalKIVADGVNSLRDGKR----SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
156-231 |
4.51e-09 |
|
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: 54.89 E-value: 4.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 156 EFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSMVRHISDRIGVMY 231
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
158-244 |
1.39e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLqdIQEE-TGVTYLFIAHDLSMVRHIsDRIGVMYLGNIV 236
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKC--IKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
....*...
gi 1078707893 237 EIADSEDL 244
Cdd:PLN03130 819 EEGTYEEL 826
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-227 |
4.31e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 42 KGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFdgkdiadlkeselkdyrkrmqiifqdpyasLNPTMNVFQIISEpm 121
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------IDGEDILEEVLDQ-- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 122 nihgsyekeeqkeiildllkkvgLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQV-----V 196
Cdd:smart00382 49 -----------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeL 105
|
170 180 190
....*....|....*....|....*....|....*.
gi 1078707893 197 NMLQDIQEETGVTYLFIAHDLSM-----VRHISDRI 227
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDlgpalLRRRFDRR 141
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-227 |
4.33e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDG--------KDIADLKESELkDYrkrmqIIFQD-P 103
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPAL-EY-----VIDGDrE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 YASLNPTMNVFQIISEPMNI---HGSYEKEEQKEI---ILDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDF 177
Cdd:PRK10636 91 YRQLEAQLHDANERNDGHAIatiHGKLDAIDAWTIrsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1078707893 178 ILCDEPISALDVSVqaqVVNMLQDIQEETGvTYLFIAHDLSMVRHISDRI 227
Cdd:PRK10636 171 LLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
36-227 |
4.42e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.50 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESelkdYRKRMQIIFQDPyaSLNPTMNVFQ 115
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS----IARGLLYLGHAP--GIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 116 iisepmNIHgSYEKEEQKEIILDLLKKVGLKE-EHlyRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQ 194
Cdd:cd03231 93 ------NLR-FWHADHSDEQVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 1078707893 195 VVNMLQDIQEETGVTYLFIAHDLSMVRHISDRI 227
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-202 |
7.17e-08 |
|
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: 51.86 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 10 RNLKKYFPIKKGlfgrkTEQLkaVDDLSFTIKKGETFGLVGESGCGKST-----TGRSIIrlhDVTSGNILFDGKDIAdl 84
Cdd:cd03232 7 KNLNYTVPVKGG-----KRQL--LNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTA---GVITGEILINGRPLD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 85 keselKDYRKRMQiifqdpYASLNPTMNVFQIISEPMNIHGsyekeeqkeiildLLKkvGLKEEhlyryphefsggQRQR 164
Cdd:cd03232 75 -----KNFQRSTG------YVEQQDVHSPNLTVREALRFSA-------------LLR--GLSVE------------QRKR 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 1078707893 165 ISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDI 202
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-199 |
1.11e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 25 RKTEQLKAVDDLSFTIKKGETFGLVGESGCGKST-----TGRsiIRLHDVTsGNILFDGKDIAdlkeselKDYRKRMQII 99
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTllnalAGR--IQGNNFT-GTILANNRKPT-------KQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 100 FQD----PYASLNPTMNVFQIISEPmnihGSYEKEEQKEIILDLLKKVGLKEEHLYRYPHEF----SGGQRQRISIARAL 171
Cdd:PLN03211 146 TQDdilyPHLTVRETLVFCSLLRLP----KSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEM 221
|
170 180
....*....|....*....|....*...
gi 1078707893 172 SVKPDFILCDEPISALDVSVQAQVVNML 199
Cdd:PLN03211 222 LINPSLLILDEPTSGLDATAAYRLVLTL 249
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-188 |
1.30e-07 |
|
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: 52.16 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 20 KGLFGRKTEQLKAV-DDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDvTSGNILFDGkdiADLKESELKDYRKRMQI 98
Cdd:cd03289 6 KDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG---VSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 99 IFQdpyaslnptmNVFqIISEP--MNI--HGSYEKEEqkeiILDLLKKVGLKEEhLYRYPHE-----------FSGGQRQ 163
Cdd:cd03289 82 IPQ----------KVF-IFSGTfrKNLdpYGKWSDEE----IWKVAEEVGLKSV-IEQFPGQldfvlvdggcvLSHGHKQ 145
|
170 180
....*....|....*....|....*
gi 1078707893 164 RISIARALSVKPDFILCDEPISALD 188
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-246 |
3.05e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 20 KGLFGR--KTEQLKAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIrlhDVTSGNilfdgKDIADLKESElkdyrKRMQ 97
Cdd:PRK13545 25 KDLFFRskDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIA---GVTMPN-----KGTVDIKGSA-----ALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 98 IifqdpYASLNPTMNVFQIIsEPMNIHGSYEKEEQKEIILDLLKKVGLKEeHLYRYPHEFSGGQRQRISIARALSVKPDF 177
Cdd:PRK13545 92 I-----SSGLNGQLTGIENI-ELKGLMMGLTKEKIKEIIPEIIEFADIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 178 ILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSEDLYT 246
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
158-247 |
3.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVN--MLQDIQEETGVTYLFIAHDLSMVRHI---SDRIgVMYL 232
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTRVLVTNQLHFLPLMDRIilvSEGM-IKEE 820
|
90
....*....|....*
gi 1078707893 233 GNIVEIADSEDLYTK 247
Cdd:PLN03232 821 GTFAELSKSGSLFKK 835
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
36-104 |
7.24e-07 |
|
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: 50.57 E-value: 7.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADlkeSELKDYRKRMQIIFQDPY 104
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAYRQLFSAVFSDFH 416
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
35-195 |
1.46e-06 |
|
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: 49.08 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdiadlkeselkdyrkrmqIIFQDPYASLNPTMnvf 114
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------------ISFSSQFSWIMPGT--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 115 qiISEPMNIHGSYEKEEQKEIIldllkKVGLKEEHLYRYPHE-----------FSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:cd03291 114 --IKENIIFGVSYDEYRYKSVV-----KACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170
....*....|..
gi 1078707893 184 ISALDVSVQAQV 195
Cdd:cd03291 187 FGYLDVFTEKEI 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-242 |
1.49e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESE--------LKDYRKRMQIifqdp 103
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTGI----- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 YASLNPTMNvfQIISEPMNIHGSYEKEEQKEIILD---LLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILC 180
Cdd:PRK10982 338 YAYLDIGFN--SLISNIRNYKNKVGLLDNSRMKSDtqwVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1078707893 181 DEPISALDVSVQAQVVNMLQDI-QEETGVtyLFIAHDLSMVRHISDRIGVMYLGNIVEIADSE 242
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLVAGIVDTK 476
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
35-227 |
1.98e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTtgrsiirlhdvtsgnILFDGkdiadLKESELKDYRKRMqiifqdPYASLNPTMNVF 114
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKST---------------LVNEG-----LYASGKARLISFL------PKFSRNKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 115 QiisepmnihgsyekeeqkeiiLDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPD---FILcDEPISALDVSV 191
Cdd:cd03238 67 Q---------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtlFIL-DEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 1078707893 192 QAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHiSDRI 227
Cdd:cd03238 125 INQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWI 158
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-189 |
3.22e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 7 IEVRNLKKyfpikkgLFGRKTeqlkAVDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNIlfdgkdiaDLKE 86
Cdd:PRK11819 325 IEAENLSK-------SFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI--------KIGE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 87 SelkdyrkrMQIIFQDPY-ASLNPTMNVFQIIS---EPMNIhGSYE--------------KEEQkeiildllKKVGlkee 148
Cdd:PRK11819 386 T--------VKLAYVDQSrDALDPNKTVWEEISgglDIIKV-GNREipsrayvgrfnfkgGDQQ--------KKVG---- 444
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1078707893 149 hlyryphEFSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PRK11819 445 -------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-282 |
3.52e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 10 RNLKKYFPIKKGlfgRKTEQLKAVDDLsftIKKGETFGLVGESGCGKSTTGRSI----IRLHDVTSGNILFDGKDIADLK 85
Cdd:TIGR00956 60 RGFRKLKKFRDT---KTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 86 EselkdyRKRMQIIfqdpYASLN----PTMNVFQII------SEPMNIHGSYEKEEQKEIILDL-LKKVGLKEEHLYRYP 154
Cdd:TIGR00956 134 K------HYRGDVV----YNAETdvhfPHLTVGETLdfaarcKTPQNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 155 HEF----SGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEETGVTYLFIAHDLSM-VRHISDRIGV 229
Cdd:TIGR00956 204 NDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIV 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078707893 230 MYLGNIVEIADS-------EDL-YTKPAHPYTQALLSSMPEPdptnagKERIILEG-EVPSP 282
Cdd:TIGR00956 284 LYEGYQIYFGPAdkakqyfEKMgFKCPDRQTTADFLTSLTSP------AERQIKPGyEKKVP 339
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
157-189 |
8.54e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 8.54e-06
10 20 30
....*....|....*....|....*....|...
gi 1078707893 157 FSGGQRQRISIARALSVKPDFILCDEPISALDV 189
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-195 |
1.62e-05 |
|
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: 46.83 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 35 DLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdiadlkeselkdyrkrmqIIFQDPYASLNPTMnvf 114
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------------ISFSPQTSWIMPGT--- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 115 qiISEPMNIHGSYEKEEQKEIIldllkKVGLKEEHLYRYPHE-----------FSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:TIGR01271 503 --IKDNIIFGLSYDEYRYTSVI-----KACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|..
gi 1078707893 184 ISALDVSVQAQV 195
Cdd:TIGR01271 576 FTHLDVVTEKEI 587
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-216 |
5.41e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 33 VDDLSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKdiadlkeselkdyrkrMQIIFQDPY-ASLNPTM 111
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----------------LEVAYFDQHrAELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 112 NVFQiisepmNIhgsyeKEEQKEIIldllkkVGLKEEHLYRYPHEF--------------SGGQRQRISIARaLSVKP-D 176
Cdd:PRK11147 399 TVMD------NL-----AEGKQEVM------VNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPsN 460
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1078707893 177 FILCDEPISALDVsvqaQVVNMLQDIQEETGVTYLFIAHD 216
Cdd:PRK11147 461 LLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-188 |
9.05e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 36 LSFTIKKGETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFDGKDIADLKESELKDYRKRMqiifqdpyASLNPTMNVFQ 115
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHL--------PGLKADLSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1078707893 116 IISEPMNIHGSYEKEEQKeiilDLLKKVGLK--EEHLYRyphEFSGGQRQRISIARA-LSVKPDFILcDEPISALD 188
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMPG----SALAIVGLAgyEDTLVR---QLSAGQKKRLALARLwLSPAPLWLL-DEPYANLD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
158-216 |
2.09e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 2.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDvsvqAQVVNML-QDIQEETGvTYLFIAHD 216
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLeRHLQEYPG-TVVAVTHD 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
138-250 |
2.78e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 138 DLLKKVGLKEEhLYRYPHEFSGGQRQRISIARALSVKPDFILCDEPISALDVSVQAQVVNMLQDIQEEtGVTYLFIAHDL 217
Cdd:NF000106 127 ELLERFSLTEA-AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYM 204
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1078707893 218 SMVRHISDRIGVMYLGNIVEIADSEDLYTK---------PAH 250
Cdd:NF000106 205 EEAEQLAHELTVIDRGRVIADGKVDELKTKvggrtlqirPAH 246
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-275 |
5.45e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 37 SFTIKKGETFGLVGESGCGKSTTGRSIirlhdvtSGN-ILFDGKDIADLKESELKDYRKRMQIIfQDPYASLNPTMnvfq 115
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGElPLLSGERQSQFSHITRLSFEQLQKLV-SDEWQRNNTDM---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 116 iISEPMNIHGsyekEEQKEIILDLLKKVGLKEE--------HLYRYPHEF-SGGQRQRISIARALSVKPDFILCDEPISA 186
Cdd:PRK10938 91 -LSPGEDDTG----RTTAEIIQDEVKDPARCEQlaqqfgitALLDRRFKYlSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 187 LDVSVQAQVVNMLQDIQEEtGVTYLFIAHDLSMVRHISDRIGVMYLGNIVEIADSED-----LYTKPAHPYTQALLsSMP 261
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEilqqaLVAQLAHSEQLEGV-QLP 243
|
250 260
....*....|....*....|
gi 1078707893 262 EPDPTNA------GKERIIL 275
Cdd:PRK10938 244 EPDEPSArhalpaNEPRIVL 263
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-225 |
5.90e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 43 GETFGLVGESGCGKSTTGRSIIRLHDVTSGNILFD-GKDIADLKESEL--KDYR-------------KRMQ---IIFQDP 103
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQFafEEFTvldtvimghtelwEVKQerdRIYALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 104 YASLNPTMNVFQIISEPMNIHGsYEKEEQKEiilDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPDFILCDEP 183
Cdd:PRK15064 107 EMSEEDGMKVADLEVKFAEMDG-YTAEARAG---ELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1078707893 184 ISALDVSvqaqVVNMLQDIQEETGVTYLFIAHD---LSMV-RHISD 225
Cdd:PRK15064 183 TNNLDIN----TIRWLEDVLNERNSTMIIISHDrhfLNSVcTHMAD 224
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
137-221 |
7.42e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.68 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 137 LDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSvKPD-----FILcDEPISALDVSVQAQVVNMLQDIQEEtGVTYL 211
Cdd:cd03271 150 LQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELS-KRStgktlYIL-DEPTTGLHFHDVKKLLEVLQRLVDK-GNTVV 226
|
90
....*....|
gi 1078707893 212 FIAHDLSMVR 221
Cdd:cd03271 227 VIEHNLDVIK 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-183 |
8.21e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 32 AVDDLSFTIKKGETFGLVGESGCGKST-----TGRSIIRlhdvtSGNILFDGKDIADlkeselKDYRKRM--QIIF--QD 102
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSllsliAGARKIQ-----QGRVEVLGGDMAD------ARHRRAVcpRIAYmpQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 103 PYASLNPTMNVFQiisepmNI--------HGSYEKEEQkeiILDLLKKVGLkeehlyrypHEF--------SGGQRQRIS 166
Cdd:NF033858 85 LGKNLYPTLSVFE------NLdffgrlfgQDAAERRRR---IDELLRATGL---------APFadrpagklSGGMKQKLG 146
|
170
....*....|....*..
gi 1078707893 167 IARALSVKPDFILCDEP 183
Cdd:NF033858 147 LCCALIHDPDLLILDEP 163
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-227 |
1.27e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 137 LDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSVKPD---FILcDEPISALDVSVQAQVVNMLQDIQeETGVTYLFI 213
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvlYVL-DEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVV 195
|
90
....*....|....
gi 1078707893 214 AHDLSMVRHiSDRI 227
Cdd:cd03270 196 EHDEDTIRA-ADHV 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
158-216 |
6.88e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.18 E-value: 6.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 158 SGGQRQRISIARALSVKPDFILCDEPISALDvsvqAQVVNML-QDIQEETGvTYLFIAHD 216
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLeQFLHDYPG-TVVAVTHD 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-221 |
7.89e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078707893 137 LDLLKKVGLKEEHLYRYPHEFSGGQRQRISIARALSvKPD-----FILcDEPISALDVSVQAQVVNMLQDIQEEtGVTYL 211
Cdd:TIGR00630 810 LQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELS-KRStgrtlYIL-DEPTTGLHFDDIKKLLEVLQRLVDK-GNTVV 886
|
90
....*....|
gi 1078707893 212 FIAHDLSMVR 221
Cdd:TIGR00630 887 VIEHNLDVIK 896
|
|
| |
