|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-321 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 614.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFHLGKG------ATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKN 74
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGlfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 75 IHELKGKDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMyKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSG 154
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGL-ASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 155 GQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQT 234
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 235 ASRELYKKPLHPYTQALLTAIPIPDPdvEDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVWQEVEENHFV 314
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDP--ERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQV 318
|
....*..
gi 2570312733 315 ACHLYDR 321
Cdd:COG4608 319 ACHLAEE 325
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-321 |
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: 521.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD---QTEGEVLFNGKNIHELKGKD 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYY-RQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRtEKVHQLLEDVGLN--RDHANRYPHEFSGGQRQR 159
Cdd:COG0444 80 LRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEAR-ERAIELLERVGLPdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 240 YKKPLHPYTQALLTAIPIPDPdveDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVWQEVEENHFVACHLY 319
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP---DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLY 315
|
..
gi 2570312733 320 DR 321
Cdd:COG0444 316 EE 317
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-316 |
3.22e-159 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 448.39 E-value: 3.22e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHL--------GKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHE 77
Cdd:PRK15079 8 LLEVADLKVHFDIkdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 78 LKGKDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQR 157
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 238 ELYKKPLHPYTQALLTAIPIPDPDVEDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVWqEVEENHFVAC 316
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL-EGSFRHAVSC 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-261 |
6.52e-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: 444.35 E-value: 6.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDK 83
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYkNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIA 163
Cdd:COG1123 338 RELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLL-SRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 164 RALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
250
....*....|....*...
gi 2570312733 244 LHPYTQALLTAIPIPDPD 261
Cdd:COG1123 497 QHPYTRALLAAVPSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-321 |
2.03e-143 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 408.20 E-value: 2.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKG-----ATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHELKG 80
Cdd:PRK11308 5 LLQAIDLKKHYPVKRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG---QDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYY---RQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYkNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQR 157
Cdd:PRK11308 82 ADPEAQKllrQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSL-SAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 238 ELYKKPLHPYTQALLTAIPIPDPDveDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVWQEVEEnHFVACH 317
Cdd:PRK11308 241 QIFNNPRHPYTQALLSATPRLNPD--DRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDG-RLVACF 317
|
....
gi 2570312733 318 LYDR 321
Cdd:PRK11308 318 AVEQ 321
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-259 |
2.78e-140 |
|
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: 407.53 E-value: 2.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKG------ATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLyDQTEGEVLFNGKNIHELK 79
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 GKDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQR 159
Cdd:COG4172 354 RRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250 260
....*....|....*....|
gi 2570312733 240 YKKPLHPYTQALLTAIPIPD 259
Cdd:COG4172 514 FDAPQHPYTRALLAAAPLLE 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-233 |
6.91e-129 |
|
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: 367.22 E-value: 6.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-257 |
2.65e-121 |
|
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: 349.10 E-value: 2.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfA 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV-PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK---A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMyknkQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGL----PDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLH 245
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|..
gi 2570312733 246 PYTQALLTAIPI 257
Cdd:COG1124 233 PYTRELLAASLA 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-274 |
1.92e-96 |
|
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: 295.44 E-value: 1.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGL----YDQTEGEVLFNGKNIH 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTV-EAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 77 ELKGkdkfayyRQMQ--------MIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRtEKVHQLLEDVGLN--RDHAN 146
Cdd:COG4172 80 GLSE-------RELRrirgnriaMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAAR-ARALELLERVGIPdpERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 147 RYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:COG4172 152 AYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2570312733 227 LGHLVEQTASRELYKKPLHPYTQALLTAIPIPDPDVEDKRERIILQGE 274
Cdd:COG4172 232 QGEIVEQGPTAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEAR 279
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-277 |
3.76e-96 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 297.54 E-value: 3.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGA------TLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHE 77
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLlnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 78 LKGKDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRtEKVHQLLEDVGLNRDHANRYPHEFSGGQR 157
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAA-ARVAWLLERVGLLPEHAWRYPHEFSGGQR 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2570312733 238 ELYKKPLHPYTQALLTAIPIPDPDvEDKRERIILQGELPS 277
Cdd:PRK10261 550 AVFENPQHPYTRKLMAAVPVADPS-RQRPQRVLLSDDLPS 588
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-254 |
1.48e-90 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 271.33 E-value: 1.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFHLGKG----ATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHEL 78
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGlfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING---HKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 KGKDkFAYY-RQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQgRTEKVHQLLEDVGLNRDHANRYPHEFSGGQR 157
Cdd:COG4167 78 EYGD-YKYRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEE-REERIFATLRLVGLLPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTA 235
|
250
....*....|....*..
gi 2570312733 238 ELYKKPLHPYTQALLTA 254
Cdd:COG4167 236 EVFANPQHEVTKRLIES 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-253 |
3.65e-82 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 258.48 E-value: 3.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATLKAVD------GISFTVKKGETYGIVGESGCGKSTAGRTILGLYdQTEGEVLFNGKNIHELK 79
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKRTVDhnvvvkNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 GKDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQR 159
Cdd:PRK15134 354 RRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
250
....*....|....
gi 2570312733 240 YKKPLHPYTQALLT 253
Cdd:PRK15134 514 FAAPQQEYTRQLLA 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-317 |
6.16e-81 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 249.27 E-value: 6.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHlGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDqTEGEVL-----FNGKNIHELKG 80
Cdd:PRK11022 3 LLNVDKLSVHFG-DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKfayyRQ-----MQMIFQDPYASLNPRSTVLEIISEPMEVHgMYKNKQGRTEKVHQLLEDVGLNrDHANR---YPHEF 152
Cdd:PRK11022 81 KER----RNlvgaeVAMIFQDPMTSLNPCYTVGFQIMEAIKVH-QGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 233 QTASRELYKKPLHPYTQALLTAIPipdPDVEDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVWQEVEEnH 312
Cdd:PRK11022 235 TGKAHDIFRAPRHPYTQALLRALP---EFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAG-R 310
|
....*
gi 2570312733 313 FVACH 317
Cdd:PRK11022 311 QSKCH 315
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-317 |
9.24e-81 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 248.87 E-value: 9.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQ---TEGEVLFNGKNIHELKG 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KdKFAYYR--QMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVhQLLEDVGL--NRDHANRYPHEFSGGQ 156
Cdd:PRK09473 89 K-ELNKLRaeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESV-RMLDAVKMpeARKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTAS 236
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 237 RELYKKPLHPYTQALLTAIPIPDPDVEdkrERIILQGELPSPMNPPSGCVFRTRCAYAMEACASrKPVWQEVEENHFVAC 316
Cdd:PRK09473 247 RDVFYQPSHPYSIGLLNAVPRLDAEGE---SLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSS-APPLEEFGPGRLRAC 322
|
.
gi 2570312733 317 H 317
Cdd:PRK09473 323 F 323
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-268 |
1.85e-79 |
|
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: 250.98 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQT---EGEVLFNGKNIHELKG 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGG---DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDkfaYYRQMQMIFQDPYASLNPrSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNRdHANRYPHEFSGGQRQRI 160
Cdd:COG1123 79 AL---RGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGL--SRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
250 260
....*....|....*....|....*...
gi 2570312733 241 KKPlhpytqALLTAIPIPDPDVEDKRER 268
Cdd:COG1123 232 AAP------QALAAVPRLGAARGRAAPA 253
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-260 |
3.72e-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: 242.40 E-value: 3.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFH----LGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGK 81
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEvHGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIG 161
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYK 241
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|....*....
gi 2570312733 242 KPlHPYTQALLTAIPIPDP 260
Cdd:TIGR02769 241 FK-HPAGRNLQSAVLPEHP 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-269 |
1.37e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 233.05 E-value: 1.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAY 86
Cdd:COG1135 2 IELENLSKTFPTKGGPV-TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:COG1135 81 RRKIGMIFQH--FNLLSSRTVAENVALPLEIAGVPKAE--IRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHP 246
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
250 260
....*....|....*....|...
gi 2570312733 247 YTQALLTAIPIPDPDvEDKRERI 269
Cdd:COG1135 236 LTRRFLPTVLNDELP-EELLARL 257
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-261 |
4.53e-73 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 226.88 E-value: 4.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFH----LGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKG 80
Cdd:PRK10419 2 TLLNVSGLSHHYAhgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEvHGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRI 160
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
250 260
....*....|....*....|.
gi 2570312733 241 KKPlHPYTQALLTAIPIPDPD 261
Cdd:PRK10419 241 TFS-SPAGRVLQNAVLPAFPV 260
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-243 |
7.35e-72 |
|
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: 222.46 E-value: 7.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKV-TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDpYASLNPRsTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03258 80 ARRRIGMIFQH-FNLLSSR-TVFENVALPLEIAGVPKAE--IEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-317 |
3.76e-69 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 219.01 E-value: 3.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFHLGKGaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQ----TEGEVLFNGKNIHELKG 80
Cdd:COG4170 2 PLLDIRNLTIEIDTPQG-RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYY-RQMQMIFQDPYASLNPRSTVLEIISEPM---EVHGMY-KNKQGRTEKVHQLLEDVGLnRDHA---NRYPHEF 152
Cdd:COG4170 81 RERRKIIgREIAMIFQEPSSCLDPSAKIGDQLIEAIpswTFKGKWwQRFKWRKKRAIELLHRVGI-KDHKdimNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 233 QTASRELYKKPLHPYTQALLTAIPIPDPDVEDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACAsRKPVWQEVeENH 312
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCV-ETPRLRKI-KGH 317
|
....*
gi 2570312733 313 FVACH 317
Cdd:COG4170 318 EFACH 322
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-254 |
1.42e-68 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 215.42 E-value: 1.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFHLGKG----ATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHEL 78
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 KGKDkFAYYRQ-MQMIFQDPYASLNPRSTVLEIISEPMEVHGMYkNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQR 157
Cdd:PRK15112 78 HFGD-YSYRSQrIRMIFQDPSTSLNPRQRISQILDFPLRLNTDL-EPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*..
gi 2570312733 238 ELYKKPLHPYTQALLTA 254
Cdd:PRK15112 236 DVLASPLHELTKRLIAG 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-247 |
7.04e-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: 216.50 E-value: 7.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfA 85
Cdd:COG3842 5 ALELENVSKRY----GDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG3842 75 EKRNVGMVFQD-YA-LFPHLTVAENVAFGLRMRGV--PKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD----LSMvkqiSDRIGVMYLGHlVEQTAS-RELY 240
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGR-IEQVGTpEEIY 224
|
....*..
gi 2570312733 241 KKPLHPY 247
Cdd:COG3842 225 ERPATRF 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-230 |
6.71e-66 |
|
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: 206.96 E-value: 6.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAY 86
Cdd:cd03255 1 IELKNLSKTYGGG-GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YR-QMQMIFQDPYasLNPRSTVLEIISEPMEVHGmyKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03255 80 RRrHIGFVFQSFN--LLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKqISDRIGVMYLGHL 230
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-261 |
1.01e-65 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 215.72 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGL-------YDQteGEVLFNGKNI--- 75
Cdd:PRK15134 5 LLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvYPS--GDIRFHGESLlha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 76 --HELKGkdkfayYR--QMQMIFQDPYASLNPRSTVLEIISEPMEVH-GMYKnKQGRTEKVhQLLEDVGLnRDHANR--- 147
Cdd:PRK15134 82 seQTLRG------VRgnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHrGMRR-EAARGEIL-NCLDRVGI-RQAAKRltd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 148 YPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYL 227
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
250 260 270
....*....|....*....|....*....|....
gi 2570312733 228 GHLVEQTASRELYKKPLHPYTQALLTAIPIPDPD 261
Cdd:PRK15134 233 GRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-252 |
1.23e-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: 204.44 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlGKgatlKAV-DGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD 82
Cdd:COG1127 3 EPMIEVRNLTKSF--GD----RVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYYRQMQMIFQDP--YASLnprsTVLEIISEPMEVHGMYKNKQgRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRI 160
Cdd:COG1127 77 LYELRRRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAE-IRELVLEKLELVGL-PGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALD-VSVqAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 2570312733 240 YKKPlHPYTQALL 252
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-247 |
2.35e-64 |
|
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: 203.50 E-value: 2.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAY 86
Cdd:cd03261 1 IELRGLTKSF--GGRTVLK---GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDP--YASLnprsTVLEIISEPMEVHGMYKNKQgRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03261 76 RRRMGMLFQSGalFDSL----TVFENVAFPLREHTRLSEEE-IREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPl 244
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD- 228
|
...
gi 2570312733 245 HPY 247
Cdd:cd03261 229 DPL 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-266 |
1.02e-63 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 205.42 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLKKHFHlGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAYY 87
Cdd:PRK11153 3 ELKNISKVFP-QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQMIFQDpYASLNPRsTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALA 167
Cdd:PRK11153 82 RQIGMIFQH-FNLLSSR-TVFDNVALPLELAGTPKAE--IKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 168 LDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPY 247
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
250 260
....*....|....*....|
gi 2570312733 248 TQALL-TAIPIPDPDVEDKR 266
Cdd:PRK11153 237 TREFIqSTLHLDLPEDYLAR 256
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-235 |
2.44e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 200.65 E-value: 2.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAgRTILGLYDQ-TEGEVLFNGKNIHELKGKD 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKSTL-LNILGGLDRpTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KfAYYRQMQ--MIFQDPYasLNPRSTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRI 160
Cdd:COG1136 80 L-ARLRRRHigFVFQFFN--LLPELTALENVALPLLLAGVSRKE--RRERARELLERVGL-GDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSmVKQISDRIGVMYLGHLVEQTA 235
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSDER 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-225 |
9.53e-62 |
|
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: 196.15 E-value: 9.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfay 86
Cdd:cd03293 1 LEVRNVSKTYG-GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDPyaSLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03293 73 -PDRGYVFQQD--ALLPWLTVLDNVALGLELQGV--PKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-255 |
1.06e-61 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 196.75 E-value: 1.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHlgkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHeLKGKDKFA 85
Cdd:COG1126 1 MIEIENLHKSFG-----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQdpyaSLN--PRSTVLEIISE-PMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGI 162
Cdd:COG1126 75 LRRKVGMVFQ----QFNlfPHLTVLENVTLaPIKVKKM--SKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKK 242
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
250
....*....|...
gi 2570312733 243 PLHPYTQALLTAI 255
Cdd:COG1126 227 PQHERTRAFLSKV 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
3.13e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 193.77 E-value: 3.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MT-VENLLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELK 79
Cdd:COG1116 1 MSaAAPALELRGVSKRFPTGGGGV-TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 gkdkfayyRQMQMIFQDPyaSLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQR 159
Cdd:COG1116 80 --------PDRGVVFQEP--ALLPWLTVLDNVALGLELRGV--PKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLS----MvkqiSDRIGVM 225
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfL----ADRVVVL 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-243 |
5.15e-59 |
|
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: 189.76 E-value: 5.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfAY 86
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03300 71 KRPVNTVFQN-YA-LFPHLTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-317 |
2.27e-58 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 191.17 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGL----YDQTEGEVLFNGKNIHELKGK 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYY-RQMQMIFQDPYASLNPRSTVLEIISEPMEvHGMYKNK-----QGRTEKVHQLLEDVGLnRDHAN---RYPHEF 152
Cdd:PRK15093 82 ERRKLVgHNVSMIFQEPQSCLDPSERVGRQLMQNIP-GWTYKGRwwqrfGWRKRRAIELLHRVGI-KDHKDamrSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 233 QTASRELYKKPLHPYTQALLTAIPIPDPDVEDKRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVwqEVEENH 312
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRL--TGAKNH 317
|
....*
gi 2570312733 313 FVACH 317
Cdd:PRK15093 318 LYACH 322
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-256 |
1.10e-57 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 196.61 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFHlGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVL------------- 69
Cdd:PRK10261 9 ARDVLAVENLNIAFM-QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 70 -----FNGKNIHELKGKDkfayyrqMQMIFQDPYASLNPRSTVLEIISEPMEVH-GMYKNKQGRTEKvhQLLEDVGLNRD 143
Cdd:PRK10261 88 ielseQSAAQMRHVRGAD-------MAMIFQEPMTSLNPVFTVGEQIAESIRLHqGASREEAMVEAK--RMLDQVRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 144 HA--NRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDR 221
Cdd:PRK10261 159 QTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
250 260 270
....*....|....*....|....*....|....*
gi 2570312733 222 IGVMYLGHLVEQTASRELYKKPLHPYTQALLTAIP 256
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-232 |
1.61e-57 |
|
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: 185.03 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfAY 86
Cdd:cd03259 1 LELKGLSKTY----GSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03259 71 RRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGV--PKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-243 |
3.60e-57 |
|
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: 185.20 E-value: 3.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAY 86
Cdd:cd03295 1 IEFENVTKRYGGGK----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLNRDH-ANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03295 74 RRKIGYVIQQ--IGLFPHMTVEENIALVPKLLKWPKEK--IRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-255 |
8.18e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.49 E-value: 8.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA 85
Cdd:COG3638 2 MLELRNLSKRYPGGT----PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPYasLNPRSTVLE--------IISEPMEVHGMYKNKQgrTEKVHQLLEDVGLnRDHANRYPHEFSGGQR 157
Cdd:COG3638 78 LRRRIGMIFQQFN--LVPRLSVLTnvlagrlgRTSTWRSLLGLFPPED--RERALEALERVGL-ADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
250
....*....|....*...
gi 2570312733 238 ELykkplhpyTQALLTAI 255
Cdd:COG3638 233 EL--------TDAVLREI 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-244 |
1.76e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.34 E-value: 1.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFAY 86
Cdd:COG1131 1 IEVRGLTKRY----GDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:COG1131 72 RRRIGYVPQEP--ALYPDLTVRENLRFFARLYGL--PRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPL 244
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-230 |
1.92e-55 |
|
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: 179.65 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlgkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhELKGKDKFAY 86
Cdd:cd03262 1 IEIKNLHKSFG-----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpyASLNPRSTVLEIISE-PMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03262 75 RQKVGMVFQQ--FNLFPHLTVLENITLaPIKVKGM--SKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-240 |
5.42e-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: 179.80 E-value: 5.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDpYAsLNPRSTVLE-IISEPMEVHGMYKNKQGR-----TEKVHQLLEDVGLNrDHANRYPHEFSGGQRQR 159
Cdd:TIGR02315 77 LRRRIGMIFQH-YN-LIERLTVLEnVLHGRLGYKPTWRSLLGRfseedKERALSALERVGLA-DKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
.
gi 2570312733 240 Y 240
Cdd:TIGR02315 234 D 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-245 |
5.78e-55 |
|
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: 179.69 E-value: 5.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAY 86
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVLE-IISEPMEVHGMYKNKQGR-----TEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRI 160
Cdd:cd03256 77 RRQIGMIFQQF--NLIERLSVLEnVLSGRLGRRSTWRSLFGLfpkeeKQRALAALERVGL-LDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELT 233
|
....*
gi 2570312733 241 KKPLH 245
Cdd:cd03256 234 DEVLD 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-243 |
2.50e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 181.42 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:COG3839 4 LELENVSKSY----GGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:COG3839 75 -RNIAMVFQS-YA-LYPHMTVYENIAFPLKLRKV--PKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD----LSMvkqiSDRIGVMYLGHlVEQTAS-RELYK 241
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGR-IQQVGTpEELYD 223
|
..
gi 2570312733 242 KP 243
Cdd:COG3839 224 RP 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-247 |
1.96e-53 |
|
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: 176.68 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAYYRQ-MQMIFQDpYAsLNPR 104
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQS-FA-LLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 STVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:cd03294 117 RTVLENVAFGLEVQGV--PRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 185 SVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPY 247
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-231 |
1.07e-51 |
|
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: 171.38 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLkkHFHLGKGATLkavDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkFA 85
Cdd:COG1120 1 MLEAENL--SVGYGGRPVL---DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 yyRQMQMIFQDPYASLNprSTVLEIISepmevhgmyknkQGRT--------------EKVHQLLEDVGLnRDHANRYPHE 151
Cdd:COG1120 75 --RRIAYVPQEPPAPFG--LTVRELVA------------LGRYphlglfgrpsaedrEAVEEALERTGL-EHLADRPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-243 |
1.47e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 174.18 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGK----NIHELKgkd 82
Cdd:COG1118 3 IEVRNISKRF-----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 kfayyRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGmyKNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGI 162
Cdd:COG1118 75 -----RRVGFVFQH-YA-LFPHMTVAENIAFGLRVRP--PSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHlVEQTAS-RELYK 241
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR-IEQVGTpDEVYD 223
|
..
gi 2570312733 242 KP 243
Cdd:COG1118 224 RP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-247 |
1.91e-51 |
|
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: 170.60 E-value: 1.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:cd03296 3 IEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpYAsLNPRSTVLEIISEPMEVH--GMYKNKQGRTEKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03296 74 -RNVGFVFQH-YA-LFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHlVEQTAS-RELYKKP 243
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQVGTpDEVYDHP 228
|
....
gi 2570312733 244 LHPY 247
Cdd:cd03296 229 ASPF 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-229 |
8.07e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 167.64 E-value: 8.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLkkHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYY 87
Cdd:cd03225 1 ELKNL--SFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQMIFQDPYASL-NPrsTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03225 75 RKVGLVFQNPDDQFfGP--TVEEEVAFGLENLGLPEEE--IEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGH 229
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-243 |
8.20e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 168.28 E-value: 8.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGAtlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElkgKDKFAY 86
Cdd:COG1122 1 IELENL--SFSYPGGT--PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYASL-NPrsTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG1122 74 RRKVGLVFQNPDDQLfAP--TVEEDVAFGPENLGL--PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-232 |
2.99e-50 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 166.97 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQ-----TEGEVLFNGKNIHELkGK 81
Cdd:cd03260 1 IELRDLNVYY-----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDL-DV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQMQMIFQDPyaslNP-RSTVLEIISEPMEVHGMyKNKQGRTEKVHQLLEDVGLNRDHANR-YPHEFSGGQRQR 159
Cdd:cd03260 75 DVLELRRRVGMVFQKP----NPfPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-229 |
3.58e-50 |
|
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: 165.05 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKfAY 86
Cdd:cd03229 1 LELKNVSKRYG-QK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP-PL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVLEIISEPMevhgmyknkqgrtekvhqlledvglnrdhanryphefSGGQRQRIGIARAL 166
Cdd:cd03229 75 RRRIGMVFQDF--ALFPHLTVLENIALGL-------------------------------------SGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGH 229
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-243 |
3.78e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 169.12 E-value: 3.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLKKHFhlgKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAYY 87
Cdd:COG1125 3 EFENVTKRY---PDGT-VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDL---DPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQMIFQDpyASLNPRSTVLEIIsepMEVHGMYKNKQGRT-EKVHQLLEDVGLNRD-HANRYPHEFSGGQRQRIGIARA 165
Cdd:COG1125 76 RRIGYVIQQ--IGLFPHMTVAENI---ATVPRLLGWDKERIrARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:COG1125 151 LAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-235 |
4.34e-49 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 163.68 E-value: 4.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkFAY 86
Cdd:COG2884 2 IRFENVSKRYPGGR----EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE-IPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YR-QMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKQGRteKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG2884 77 LRrRIGVVFQD--FRLLPDRTVYENVALPLRVTGKSRKEIRR--RVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTA 235
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-233 |
3.85e-48 |
|
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: 161.95 E-value: 3.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlGKGatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFA 85
Cdd:COG4555 1 MIEVENLSKKY--GKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPYasLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG4555 72 ARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL--FDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-232 |
9.31e-48 |
|
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: 160.21 E-value: 9.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKfA 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDT-RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNER-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGmyKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:TIGR02211 79 KLRNKKLGFIYQFHHLLPDFTALENVAMPLLIGK--KSVKEAKERAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVE 232
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-230 |
1.17e-47 |
|
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: 158.33 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlGKGatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFAY 86
Cdd:cd03230 1 IEVRNLSKRY--GKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVLEIIsepmevhgmyknkqgrtekvhqlledvglnrdhanryphEFSGGQRQRIGIARAL 166
Cdd:cd03230 72 KRRIGYLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-235 |
1.12e-46 |
|
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: 157.42 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:cd03301 1 VELENVTKRF-----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMYKNKQgrTEKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03301 72 -RDIAMVFQN-YA-LYPHMTVYDNIAFGLKLRKVPKDEI--DERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGhLVEQTA 235
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG-QIQQIG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-247 |
2.51e-46 |
|
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: 166.93 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAY 86
Cdd:COG2274 474 IELENV--SFRYPGDSPP-VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYasLNPRsTVLEIISepmevhgmyknkQGRT----EKVHQLLEDVGLNRD---HANRYPHE-------F 152
Cdd:COG2274 548 RRQIGVVLQDVF--LFSG-TIRENIT------------LGDPdatdEEIIEAARLAGLHDFieaLPMGYDTVvgeggsnL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVE 232
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVE 689
|
250
....*....|....*
gi 2570312733 233 QTASRELYKKPLHPY 247
Cdd:COG2274 690 DGTHEELLARKGLYA 704
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-230 |
1.38e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.20 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGatlkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfAY 86
Cdd:COG4619 1 LELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYAslnPRSTVLEIISEPMEvhgmYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:COG4619 73 RRQVAYVPQEPAL---WGGTVRDNLPFPFQ----LRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-178 |
2.12e-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: 151.65 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkGKDKFAYYRQMQMIFQDPyaSLNPRST 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT---DDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 107 VLEIISEPMEVHGMYK-NKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEP 178
Cdd:pfam00005 76 VRENLRLGLLLKGLSKrEKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-228 |
4.24e-45 |
|
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: 154.43 E-value: 4.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdk 83
Cdd:COG0411 2 DPLLEVRGLTKRF----GG-LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fAYYR-QMQMI--FQDPyaSLNPRSTVLE-------------IISEPMEVHGMYKNKQGRTEKVHQLLEDVGLnRDHANR 147
Cdd:COG0411 73 -PHRIaRLGIArtFQNP--RLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGL-ADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 148 YPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYL 227
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
.
gi 2570312733 228 G 228
Cdd:COG0411 229 G 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-225 |
4.69e-45 |
|
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: 151.38 E-value: 4.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAY 86
Cdd:cd03228 1 IEFKNV--SFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL---DLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYasLNPRsTVLEIIsepmevhgmyknkqgrtekvhqlledvglnrdhanrypheFSGGQRQRIGIARAL 166
Cdd:cd03228 75 RKNIAYVPQDPF--LFSG-TIRENI----------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVM 225
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVL 167
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-255 |
4.74e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 153.80 E-value: 4.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:TIGR00968 1 IEIANISKRF-----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpYAsLNPRSTVLEIISEPMEVhgMYKNKQGRTEKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIARAL 166
Cdd:TIGR00968 72 -RKIGFVFQH-YA-LFKHLTVRDNIAFGLEI--RKHPKAKIKARVEELLELVQLEG-LGDRYPNQLSGGQRQRVALARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHP 246
Cdd:TIGR00968 146 AVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANP 225
|
....*....
gi 2570312733 247 YTQALLTAI 255
Cdd:TIGR00968 226 FVMSFLGEV 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-228 |
1.30e-44 |
|
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: 152.59 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhelKGKDKFAY 86
Cdd:cd03219 1 LEVRGLTKRF----GG-LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQ-MQMIFQDPyaSLNPRSTVLEII--------SEPMEVHGMYKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQR 157
Cdd:cd03219 73 ARLgIGRTFQIP--RLFPELTVLENVmvaaqartGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLG 228
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-254 |
1.36e-44 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 153.32 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLY----DQTEGEVLFNGKNIH--ELKGkdkfayyRQMQMIFQDPYAS 100
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVApcALRG-------RKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 101 LNPRSTVLEIISEPMEVHGmyknKQGRTEKVHQLLEDVGLNRDH--ANRYPHEFSGGQRQRIGIARALALDPEFIIADEP 178
Cdd:PRK10418 92 FNPLHTMHTHARETCLALG----KPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 179 ISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQALLTA 254
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-243 |
1.68e-44 |
|
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: 152.49 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKK---HFHLgkgatlkavDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgKDK 83
Cdd:cd03299 1 LKVENLSKdwkEFKL---------KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fayyRQMQMIFQDpYAsLNPRSTVLEIISepmevHGMYKNKQGRTE---KVHQLLEDVGLnrDHA-NRYPHEFSGGQRQR 159
Cdd:cd03299 71 ----RDISYVPQN-YA-LFPHMTVYKNIA-----YGLKKRKVDKKEierKVLEIAEMLGI--DHLlNRKPETLSGGEQQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
....
gi 2570312733 240 YKKP 243
Cdd:cd03299 218 FKKP 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-233 |
2.01e-44 |
|
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: 150.28 E-value: 2.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLkkHFHLGKGatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD---KF 84
Cdd:cd03214 1 EVENL--SVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElarKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 AYyrqmqmifqdpyaslnprstvleiisepmevhgmyknkqgrtekVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03214 76 AY--------------------------------------------VPQALELLGL-AHLADRPFNELSGGERQRVLLAR 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-249 |
3.85e-44 |
|
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: 155.01 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHEL-KGKDKFAYYRQMQMIFQDpyASLNP 103
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRRKKIGMVFQQ--FALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 RSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:TIGR01186 85 HMTILQNTSLGPELLGW--PEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 184 VSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQ 249
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVE 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
1.14e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLkkHFHLGKgatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelKG 80
Cdd:COG1121 1 MMMMPAIELENL--TVSYGG---RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYYRQmqmifqdpYASLNPR--STVLEIISepMevhGMYK--------NKQGRtEKVHQLLEDVGLnRDHANRYPH 150
Cdd:COG1121 74 RRRIGYVPQ--------RAEVDWDfpITVRDVVL--M---GRYGrrglfrrpSRADR-EAVDEALERVGL-EDLADRPIG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 151 EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRigVMYL 227
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDR--VLLL 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-253 |
1.22e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 150.57 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLkkHFHLGKgatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-----QTEGEVLFNGKNIHEl 78
Cdd:COG1117 9 EPKIEVRNL--NVYYGD---KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIYD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 KGKDKFAYYRQMQMIFQDPyaslNP-RSTVLEIISEPMEVHGMyKNKQGRTEKVHQLLEDVGL-----NRDHANryPHEF 152
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGI-KSKSELDEIVEESLRKAALwdevkDRLKKS--ALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALD-VSVqAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250 260
....*....|....*....|..
gi 2570312733 232 EQTASRELYKKPLHPYTQALLT 253
Cdd:COG1117 233 EFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-233 |
2.15e-42 |
|
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: 145.82 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlgkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfay 86
Cdd:cd03268 1 LKTNDLTKTYG-----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDP--YASLNPRstvleiisEPMEVHGMYKnkQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03268 71 LRRIGALIEAPgfYPNLTAR--------ENLRLLARLL--GIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-242 |
3.77e-42 |
|
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: 153.76 E-value: 3.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGATlkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaY 86
Cdd:COG4988 337 IELEDV--SFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYasLnPRSTVLEIIsepmevhGMYKNKQGRTEkVHQLLEDVGLNrDHANRYPH-------E----FSGG 155
Cdd:COG4988 410 RRQIAWVPQNPY--L-FAGTIRENL-------RLGRPDASDEE-LEAALEAAGLD-EFVAALPDgldtplgEggrgLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTA 235
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
....*..
gi 2570312733 236 SRELYKK 242
Cdd:COG4988 555 HEELLAK 561
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-280 |
6.57e-42 |
|
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: 148.03 E-value: 6.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 42 IVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfAYYRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMy 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-----PHLRHINMVFQS-YA-LFPHMTVEENVAFGLKMRKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 122 kNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEK 201
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 202 GLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQALLTAIPIPD-PDVEDKRERIILQGELPSPMN 280
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEaTVIERKSEQVVLAGVEGRRCD 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-243 |
1.20e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 146.06 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAYYRQMQMIFQDPYASLNPR 104
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEHQLFEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 sTVLE-IISEPMEvhgMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:TIGR04521 99 -TVYKdIAFGPKN---LGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 184 VSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-231 |
2.10e-41 |
|
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: 141.80 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgkdkfay 86
Cdd:cd03216 1 LELRGITKRF----GGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yrqmqmiFQDPYASLNprstvleiisepmevHGMyknkqgrtEKVHQLledvglnrdhanryphefSGGQRQRIGIARAL 166
Cdd:cd03216 66 -------FASPRDARR---------------AGI--------AMVYQL------------------SVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-243 |
5.73e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 147.02 E-value: 5.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKg 80
Cdd:PRK09452 9 SSLSPLVELRGISKSF-----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 kdkfAYYRQMQMIFQDpYAsLNPRSTVLEIISepmevHGMYKNKQGRTE---KVHQLLEDVGLNrDHANRYPHEFSGGQR 157
Cdd:PRK09452 83 ----AENRHVNTVFQS-YA-LFPHMTVFENVA-----FGLRMQKTPAAEitpRVMEALRMVQLE-EFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD----LSMvkqiSDRIGVMYLGHlVEQ 233
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGR-IEQ 225
|
250
....*....|.
gi 2570312733 234 TAS-RELYKKP 243
Cdd:PRK09452 226 DGTpREIYEEP 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-229 |
6.88e-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: 140.46 E-value: 6.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLKKHFHLGKgatlkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfAYY 87
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE---ELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQMIFQdpyaslnprstvleiisepmevhgmyknkqgrtekvhqlledvglnrdhanrypheFSGGQRQRIGIARALA 167
Cdd:cd00267 73 RRIGYVPQ--------------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570312733 168 LDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGH 229
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-252 |
1.60e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 142.15 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniheLKGKDKFA 85
Cdd:PRK09493 1 MIEFKNVSKHF----GPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQ----MIFQDPYasLNPRSTVLE-IISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRI 160
Cdd:PRK09493 71 DERLIRqeagMVFQQFY--LFPHLTALEnVMFGPLRVRGA--SKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
250
....*....|..
gi 2570312733 241 KKPLHPYTQALL 252
Cdd:PRK09493 225 KNPPSQRLQEFL 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-222 |
2.57e-40 |
|
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: 140.75 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelKGKDKFAYYRQmqmifqdpYASLNPRS 105
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--KERKRIGYVPQ--------RRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 --TVLEIIS---EPMEVHGMYKNKQGRtEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPIS 180
Cdd:cd03235 84 piSVRDVVLmglYGHKGLFRRLSKADK-AKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2570312733 181 ALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRI 222
Cdd:cd03235 162 GVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-238 |
2.75e-40 |
|
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: 141.03 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 2 TVENLLEVRNLKKHFHLGKGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkGK 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGE-LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQMQM--IFQdpyaS--LNPRSTVLEIISEPMEVHGMyKNKQGRTEkvhQLLEDVGL-NR-DHanrYPHEFSGG 155
Cdd:COG4181 82 DARARLRARHVgfVFQ----SfqLLPTLTALENVMLPLELAGR-RDARARAR---ALLERVGLgHRlDH---YPAQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTA 235
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
...
gi 2570312733 236 SRE 238
Cdd:COG4181 230 ATA 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-255 |
1.75e-39 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 140.06 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGK-----NI 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 76 HELKGKDkfayyRQMQM------IFQDPYASLNPRSTVLEIISEPMEVHGMykNKQGRT-EKVHQLLEDVGLNRDHANRY 148
Cdd:PRK11701 76 YALSEAE-----RRRLLrtewgfVHQHPRDGLRMQVSAGGNIGERLMAVGA--RHYGDIrATAGDWLERVEIDAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 149 PHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLG 228
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|....*..
gi 2570312733 229 HLVEQTASRELYKKPLHPYTQALLTAI 255
Cdd:PRK11701 229 RVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-243 |
1.76e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 139.94 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD---K 83
Cdd:COG4598 9 LEVRDLHKSF--GDLEVLK---GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQ-------MIFQdpyaSLN--PRSTVLE-IISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFS 153
Cdd:COG4598 84 PADRRQLQrirtrlgMVFQ----SFNlwSHMTVLEnVIEAPVHVLGR--PKAEAIERAEALLAKVGL-ADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 154 GGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRigVMYL--GHLV 231
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSH--VVFLhqGRIE 233
|
250
....*....|..
gi 2570312733 232 EQTASRELYKKP 243
Cdd:COG4598 234 EQGPPAEVFGNP 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-243 |
1.94e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.05 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHlGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfA 85
Cdd:PRK11607 19 LLEIRNLTKSFD-GQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDpYAsLNPRSTVLEIISepmevHGMYKNKQGRTE---KVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGI 162
Cdd:PRK11607 89 YQRPINMMFQS-YA-LFPHMTVEQNIA-----FGLKQDKLPKAEiasRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 163 ARALALDPEFIIADEPISALDVSV----QAQVVNLMKRLqkekGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRE 238
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
....*
gi 2570312733 239 LYKKP 243
Cdd:PRK11607 237 IYEHP 241
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-252 |
3.32e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.11 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFHlgkGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTIlGLYDQTE------GEVLFNG-KNIHE 77
Cdd:PRK11264 2 SAIEVKNLVKKFH---GQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTaRSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 78 LKGKDKfAYYRQMQMIFQDpyASLNPRSTVLE-IISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQ 156
Cdd:PRK11264 76 QKGLIR-QLRQHVGFVFQN--FNLFPHRTVLEnIIEGPVIVKGE--PKEEATARARELLAKVGLA-GKETSYPRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKgLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTAS 236
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
250
....*....|....*.
gi 2570312733 237 RELYKKPLHPYTQALL 252
Cdd:PRK11264 229 KALFADPQQPRTRQFL 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-253 |
6.81e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 138.56 E-value: 6.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD- 82
Cdd:PRK10619 3 ENKLNVIDLHKRY--GEHEVLK---GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 --KFAYYRQMQ-------MIFQdpYASLNPRSTVLEIISE-PMEVHGMykNKQGRTEKVHQLLEDVGLNRDHANRYPHEF 152
Cdd:PRK10619 78 qlKVADKNQLRllrtrltMVFQ--HFNLWSHMTVLENVMEaPIQVLGL--SKQEARERAVKYLAKVGIDERAQGKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250 260
....*....|....*....|.
gi 2570312733 233 QTASRELYKKPLHPYTQALLT 253
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQFLK 253
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-255 |
9.28e-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: 138.04 E-value: 9.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATlkavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLF--NGKNIHEL----K 79
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCR-----DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimRSGAELELyqlsE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 GKDKFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRtEKVHQLLEDVGLNRDHANRYPHEFSGGQRQR 159
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIR-ATAQDWLEEVEIDPTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQV 236
|
250
....*....|....*.
gi 2570312733 240 YKKPLHPYTQALLTAI 255
Cdd:TIGR02323 237 LDDPQHPYTQLLVSSI 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-242 |
1.07e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.54 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGAtlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAY 86
Cdd:COG1132 340 IEFENV--SFSYPGDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYasLNPRsTVLEIISepmevhgmYKNKQGRTEKVHQLLEDVGLnrdhanrypHEF-------------- 152
Cdd:COG1132 413 RRQIGVVPQDTF--LFSG-TIRENIR--------YGRPDATDEEVEEAAKAAQA---------HEFiealpdgydtvvge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 -----SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYL 227
Cdd:COG1132 473 rgvnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDD 549
|
250 260
....*....|....*....|.
gi 2570312733 228 GHLVEQ------TASRELYKK 242
Cdd:COG1132 550 GRIVEQgtheelLARGGLYAR 570
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-222 |
2.44e-38 |
|
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: 135.61 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdKFAY 86
Cdd:cd03292 1 IEFINVTKTY----PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR-AIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQ-MQMIFQDpyASLNPRSTVLEIISEPMEVhgMYKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:cd03292 76 LRRkIGVVFQD--FRLLPDRNVYENVAFALEV--TGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQISDRI 222
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRV 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-241 |
2.56e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.45 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihELKGKDK 83
Cdd:PRK13635 3 EEIIRVEHISFRY---PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQdpyaslNPR-----STVLEIISEPMEVHGMYKNKQgrTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQ 158
Cdd:PRK13635 77 WDVRRQVGMVFQ------NPDnqfvgATVQDDVAFGLENIGVPREEM--VERVDQALRQVGM-EDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRE 238
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE 226
|
...
gi 2570312733 239 LYK 241
Cdd:PRK13635 227 IFK 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-243 |
2.93e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 139.06 E-value: 2.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:PRK10851 3 IEIANIKKSF----GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMYK--NKQGRTEKVHQLLEDVGLnrDH-ANRYPHEFSGGQRQRIGIA 163
Cdd:PRK10851 74 -RKVGFVFQH-YA-LFRHMTVFDNIAFGLTVLPRRErpNAAAIKAKVTQLLEMVQL--AHlADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 164 RALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-265 |
6.03e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 136.83 E-value: 6.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElKGKDKF--AYYRQMQMIFQDPYASLN 102
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKYirPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 103 PRSTVLEIISEPMEVhGMykNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISAL 182
Cdd:PRK13646 100 EDTVEREIIFGPKNF-KM--NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 183 DVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPlhpyTQALLTAIPIPD--- 259
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK----KKLADWHIGLPEivq 252
|
....*...
gi 2570312733 260 --PDVEDK 265
Cdd:PRK13646 253 lqYDFEQK 260
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-231 |
7.22e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.78 E-value: 7.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElKGKDKFAY 86
Cdd:COG4152 2 LELKGLTKRF-----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 -------YRQM----QMIFqdpYASLnprstvleiisepmevHGMYKnKQGRtEKVHQLLEDVGLNrDHANRYPHEFSGG 155
Cdd:COG4152 76 lpeerglYPKMkvgeQLVY---LARL----------------KGLSK-AEAK-RRADEWLERLGLG-DRANKKVEELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALD-VSvqaqvVNLMKRL---QKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDpVN-----VELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-239 |
1.32e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.15 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgkdk 83
Cdd:COG1129 2 EPLLEMRGISKSF----GGV-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQ-----MIFQDPyaSLNPRSTVLEII---SEPMEvHGMYKNKQGRtEKVHQLLEDVGLNRDhanryPH----E 151
Cdd:COG1129 70 FRSPRDAQaagiaIIHQEL--NLVPNLSVAENIflgREPRR-GGLIDWRAMR-RRARELLARLGLDID-----PDtpvgD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
....*...
gi 2570312733 232 EQTASREL 239
Cdd:COG1129 220 GTGPVAEL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
25-228 |
2.08e-37 |
|
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: 132.77 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElkgKDKfayYRQMQMIFQDPYASLNpR 104
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KER---RKSIGYVMQDVDYQLF-T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 STVLEiisepmEVHGMYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:cd03226 87 DSVRE------ELLLGLKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2570312733 185 SVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRigVMYLG 228
Cdd:cd03226 160 KNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDR--VLLLA 200
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
27-260 |
3.94e-37 |
|
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: 136.66 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLY--DQTEGEVLFNGKNIHELKgkdkfAYYRQMQMIFQDpYAsLNPR 104
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVkaAGLTGRIAIADRDLTHAP-----PHKRGLALLFQN-YA-LFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 STVLEIISepmevHGMYKNKQGRT---EKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISA 181
Cdd:TIGR03258 94 LKVEDNVA-----FGLRAQKMPKAdiaERVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 182 LDVSVQAQVVNLMKRLQKE-KGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQALLTAIPIPDP 260
Cdd:TIGR03258 168 LDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-232 |
4.38e-37 |
|
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: 139.17 E-value: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFN--------GKNI 75
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 76 HELKGKDKfayyRQMQMIFQDpyASLNPRSTVLEIISEPMEVHgmYKNKQGRTEKVHqLLEDVGLNRDHA----NRYPHE 151
Cdd:TIGR03269 357 PDGRGRAK----RYIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVI-TLKMVGFDEEKAeeilDKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
.
gi 2570312733 232 E 232
Cdd:TIGR03269 508 K 508
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-253 |
6.49e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 133.11 E-value: 6.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRT---ILGLYDQ--TEGEVLFNGKNIHELk 79
Cdd:PRK14247 2 NKIEIRDLKVSF-----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDIFKM- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 gkDKFAYYRQMQMIFQDPYASlnPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLNRDHANRY---PHEFSGGQ 156
Cdd:PRK14247 76 --DVIELRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTAS 236
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
250
....*....|....*..
gi 2570312733 237 RELYKKPLHPYTQALLT 253
Cdd:PRK14247 230 REVFTNPRHELTEKYVT 246
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-211 |
2.52e-36 |
|
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: 129.91 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHlgkGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFA 85
Cdd:COG4133 2 MLEAENLSCRRG---ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFqdPYASLNPRSTVLEIIsepmEVHGMYKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG4133 73 YRRRLAYLG--HADGLKPELTVRENL----RFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTyLFIAHD 211
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-243 |
5.41e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.31 E-value: 5.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFhlGKGATlkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhelkg 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRF--GSNTV---IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYYRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRI 160
Cdd:PRK11432 71 THRSIQQRDICMVFQS-YA-LFPHMSLGENVGYGLKMLGV--PKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
...
gi 2570312733 241 KKP 243
Cdd:PRK11432 226 RQP 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-240 |
1.04e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 130.62 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHELKGKDK 83
Cdd:PRK13650 2 SNIIEVKNLTFKYK--EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQDPYASLnPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIA 163
Cdd:PRK13650 77 WDIRHKIGMVFQNPDNQF-VGATVEDDVAFGLENKGI--PHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 164 RALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKqISDRIGVMYLGHlVEQTAS-RELY 240
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTSTpRELF 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-211 |
2.03e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.21 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhELKGKDKfay 86
Cdd:COG4525 4 LTVRHVSVRYP-GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yrqmQMIFQDpyASLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:COG4525 79 ----GVVFQK--DALLPWLNVLDNVAFGLRLRGV--PKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD 211
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
30-233 |
2.44e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNI---HELKGKDKFAYYRQMQMIFQDpYaSLNPRST 106
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ-Y-NLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VLE-IISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVS 185
Cdd:PRK11124 99 VQQnLIEAPCRVLGL--SKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2570312733 186 VQAQVVNLMKRLQkEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-222 |
3.05e-35 |
|
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: 127.94 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVenLLEVRNLKKHF--HLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKN---- 74
Cdd:COG4778 1 MTT--LLEVENLSKTFtlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 75 --------IHELKgKDKFAYYRQmqmiFqdpyasLN--PRSTVLEIISEPMEVHGMyKNKQGRtEKVHQLLEDVGLNRDH 144
Cdd:COG4778 79 laqaspreILALR-RRTIGYVSQ----F------LRviPRVSALDVVAEPLLERGV-DREEAR-ARARELLARLNLPERL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 145 ANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRI 222
Cdd:COG4778 146 WDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRV 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-242 |
3.44e-35 |
|
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: 127.73 E-value: 3.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfAYYRQMQMIFQDPYasLNPRs 105
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK---SLRSMIGVVLQDTF--LFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 TVLEIISepmevhgmYKNKQGRTEKVHQLLEDVGLN---RDHANRYPHE-------FSGGQRQRIGIARALALDPEFIIA 175
Cdd:cd03254 92 TIMENIR--------LGRPNATDEEVIEAAKEAGAHdfiMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 176 DEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKK 242
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-231 |
3.55e-35 |
|
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: 127.41 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHfhlgKGATLKavdgISFTVKkGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNG-------KNIHELK 79
Cdd:cd03297 2 LCVDIEKRL----PDFTLK----IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 GKDKFAYyrqmqmIFQDpyASLNPRSTVLEIIsepmeVHGMYKNKQG-RTEKVHQLLEDVGLnrDH-ANRYPHEFSGGQR 157
Cdd:cd03297 73 QQRKIGL------VFQQ--YALFPHLNVRENL-----AFGLKRKRNReDRISVDELLDLLGL--DHlLNRYPAQLSGGEK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:cd03297 138 QRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-257 |
5.33e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 10 RNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD-KFAYYR 88
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 89 QMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALAL 168
Cdd:PRK10070 107 KIAMVFQS--FALMPHMTVLDNTAFGMELAGINAEE--RREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 169 DPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYT 248
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
....*....
gi 2570312733 249 QALLTAIPI 257
Cdd:PRK10070 262 RTFFRGVDI 270
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-243 |
6.42e-35 |
|
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: 133.74 E-value: 6.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaY 86
Cdd:COG4987 334 LELEDV--SFRYP-GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---L 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPY---ASL-------NPRSTvleiisepmevhgmyknkqgrTEKVHQLLEDVGLnRDHANRYPH------ 150
Cdd:COG4987 408 RRRIAVVPQRPHlfdTTLrenlrlaRPDAT---------------------DEELWAALERVGL-GDWLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 151 -E----FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLtyLFIAHDLSMVKQIsDRIGVM 225
Cdd:COG4987 466 gEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVL 542
|
250
....*....|....*...
gi 2570312733 226 YLGHLVEQTASRELYKKP 243
Cdd:COG4987 543 EDGRIVEQGTHEELLAQN 560
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-233 |
7.85e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 126.85 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA 85
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQT-DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YY-RQMQMIFQdpYASLNPRSTVLEIISEPMEVHGmyKNKQGRTEKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIAR 164
Cdd:PRK11629 84 LRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGK--KKPAEINSRALEMLAAVGLEH-RANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGvMYLGHLVEQ 233
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-233 |
1.46e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 125.47 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgKDKFAY 86
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 -------YRQMQMIFQDPY-ASLnprstvleiisepmevHGMykNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQ 158
Cdd:cd03269 75 lpeerglYPKMKVIDQLVYlAQL----------------KGL--KKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVsVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-253 |
1.64e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 126.88 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLkkHFHLGKGATLKAVDgisFTVKKGETYGIVGESGCGKSTAGRTILGLYD-----QTEGEVLFNGKNIHEL 78
Cdd:PRK14267 2 KFAIETVNL--RVYYGSNHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 KgKDKFAYYRQMQMIFQdpYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGL---NRDHANRYPHEFSGG 155
Cdd:PRK14267 77 D-VDPIEVRREVGMVFQ--YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTA 235
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
250
....*....|....*...
gi 2570312733 236 SRELYKKPLHPYTQALLT 253
Cdd:PRK14267 232 TRKVFENPEHELTEKYVT 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-239 |
1.66e-34 |
|
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: 125.56 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFAY 86
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVleiiSEPMEVHGM---YKNKQgRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIA 163
Cdd:cd03265 72 RRRIGIVFQDL--SVDDELTG----WENLYIHARlygVPGAE-RRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 164 RALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-231 |
4.92e-34 |
|
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: 124.40 E-value: 4.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFA 85
Cdd:cd03266 1 MITADALTKRFRDVKK-TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKQ-GRTEKVHQLLEdvglNRDHANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03266 76 ARRRLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDELtARLEELADRLG----MEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-240 |
1.52e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 124.82 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKkhFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihELKGKD 82
Cdd:PRK13642 1 MNKILEVENLV--FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYYRQMQMIFQDPYASLnPRSTVLEIISEPMEVHGMYKNKQgrTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGI 162
Cdd:PRK13642 76 VWNLRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGIPREEM--IKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-242 |
1.66e-33 |
|
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: 123.42 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLkkHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYY 87
Cdd:cd03249 2 EFKNV--SFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQMIFQDP---YASL--N-----PRSTVLEIIsEPMEVHGMYKNKQGRTEKVHQLLEDVGLnrdhanryphEFSGGQR 157
Cdd:cd03249 77 SQIGLVSQEPvlfDGTIaeNirygkPDATDEEVE-EAAKKANIHDFIMSLPDGYDTLVGERGS----------QLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVS----VQAQVVNLMkrlqkeKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQ 233
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAEseklVQEALDRAM------KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
....*....
gi 2570312733 234 TASRELYKK 242
Cdd:cd03249 219 GTHDELMAQ 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-242 |
1.95e-33 |
|
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: 123.49 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYYRQMQMIFQDPY------ 98
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQIGLVSQDVFlfndtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 ----ASLNPRSTVLEIIS--EPMEVHGMYKNKQgrtEKVHQLLEDVGLNrdhanrypheFSGGQRQRIGIARALALDPEF 172
Cdd:cd03251 93 aeniAYGRPGATREEVEEaaRAANAHEFIMELP---EGYDTVIGERGVK----------LSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 173 IIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKK 242
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-233 |
2.85e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.20 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlgkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNI---HELKGKDK 83
Cdd:COG4161 3 IQLKNINCFYG-----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQDpYaSLNPRSTVLE-IISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGI 162
Cdd:COG4161 78 RLLRQKVGMVFQQ-Y-NLWPHLTVMEnLIEAPCKVLGL--SKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQkEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
6-222 |
3.14e-33 |
|
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: 122.50 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHF--HLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNgkniHELKGKD- 82
Cdd:TIGR02324 1 LLEVEDLSKTFtlHQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVR----HEGAWVDl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 ------KFAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQ 156
Cdd:TIGR02324 77 aqasprEVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGV--PREAARARARELLARLNIPERLWHLPPATFSGGE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRI 222
Cdd:TIGR02324 155 QQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRV 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-243 |
1.23e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 124.19 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlGKgatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:PRK11650 4 LKLQAVRKSYD-GK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpYAsLNPRSTVLEIISEPMEVHGMYKNK-QGRTEKVHQLLEDVGLnrdhANRYPHEFSGGQRQRIGIARA 165
Cdd:PRK11650 76 -RDIAMVFQN-YA-LYPHMSVRENMAYGLKIRGMPKAEiEERVAEAARILELEPL----LDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDlsmvkQI-----SDRIGVMYLGHlVEQTAS-REL 239
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-----QVeamtlADRVVVMNGGV-AEQIGTpVEV 222
|
....
gi 2570312733 240 YKKP 243
Cdd:PRK11650 223 YEKP 226
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
229-318 |
3.47e-32 |
|
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: 115.54 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 229 HLVEQTASRELYKKPLHPYTQALLTAIPIP-DPDvedkRERIILQGELPSPMNPPSGCVFRTRCAYAMEACASRKPVWQE 307
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIkKRD----RKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVE 76
|
90
....*....|.
gi 2570312733 308 VEENHFVACHL 318
Cdd:TIGR01727 77 IAEGHRVACHL 87
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-244 |
3.84e-32 |
|
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: 119.96 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHEL----KGKD 82
Cdd:cd03218 1 LRAENLSKRY-----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYYRQMQMIFQdpyaslnpRSTVLEIISEPMEVHgmYKNKQGRTEKVHQLLEDVGLnrDH-ANRYPHEFSGGQRQRIG 161
Cdd:cd03218 76 GIGYLPQEASIFR--------KLTVEENILAVLEIR--GLSKKEREEKLEELLEEFHI--THlRKSKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 162 IARALALDPEFIIADEPISALD-VSVQaQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
....
gi 2570312733 241 KKPL 244
Cdd:cd03218 222 ANEL 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-239 |
5.78e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.75 E-value: 5.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihELKGKD- 82
Cdd:COG3845 3 PPALELRGITKRF----GG-VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYYRQMQMIFQDPyaSLNPRSTVLE-II--SEPmeVHGMYKNKQGRTEKVHQLLEDVGLNRDhANRYPHEFSGGQRQR 159
Cdd:COG3845 75 RDAIALGIGMVHQHF--MLVPNLTVAEnIVlgLEP--TKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALdvsVQAQVVNL---MKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV----- 231
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVL---TPQEADELfeiLRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVgtvdt 225
|
....*...
gi 2570312733 232 EQTASREL 239
Cdd:COG3845 226 AETSEEEL 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-242 |
7.43e-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: 119.13 E-value: 7.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHELKGKDKFAYYRQMQMIFQ---------- 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQVGVVLQenvlfnrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 96 DPYASLNPRSTVLEIIsEPMEVHGMYKNKQGRTEKVHQLLEDVGLNrdhanrypheFSGGQRQRIGIARALALDPEFIIA 175
Cdd:cd03252 94 DNIALADPGMSMERVI-EAAKLAGAHDFISELPEGYDTIVGEQGAG----------LSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 176 DEPISALDVSVQAQVVNLMKRLQkeKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKK 242
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-258 |
1.56e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 119.10 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLkkHFHLGKgatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKG 80
Cdd:PRK11831 2 QSVANLVDMRGV--SFTRGN---RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYYRQMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKQGRTeKVHQLLEDVGLnRDHANRYPHEFSGGQRQRI 160
Cdd:PRK11831 77 SRLYTVRKRMSMLFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHS-TVMMKLEAVGL-RGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
250 260
....*....|....*....|.
gi 2570312733 241 KKPlHPYTQALLTAI---PIP 258
Cdd:PRK11831 233 ANP-DPRVRQFLDGIadgPVP 252
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-211 |
1.93e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.20 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlgkGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD---QTEGEVLFNGKNIHELKgkdk 83
Cdd:COG4136 2 LSLENLTITLG---GRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fAYYRQMQMIFQDPYasLNPRSTVLE--IISEPMEVhgmykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIG 161
Cdd:COG4136 73 -AEQRRIGILFQDDL--LFPHLSVGEnlAFALPPTI-----GRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD 211
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-243 |
2.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhELKGKDKFA 85
Cdd:PRK13639 1 ILETRDLKYSYPDGT----EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPYASLNPRSTVLEIISEPMEvhgMYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARA 165
Cdd:PRK13639 76 VRKTVGIVFQNPDDQLFAPTVEEDVAFGPLN---LGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-242 |
2.57e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFHLGKGATLKAVdgiSFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElkg 80
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASFTLKDV---SFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 kDKFAYYRQ-MQMIFQDPYASLnPRSTVLEIISEPMEVHGM-YKNKQgrtEKVHQLLEDVGLnRDHANRYPHEFSGGQRQ 158
Cdd:PRK13648 76 -DNFEKLRKhIGIVFQNPDNQF-VGSIVKYDVAFGLENHAVpYDEMH---RRVSEALKQVDM-LERADYEPNALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRE 238
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTE 228
|
....
gi 2570312733 239 LYKK 242
Cdd:PRK13648 229 IFDH 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-233 |
3.77e-31 |
|
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: 116.52 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlGKGatlKAVDGISFTVKKGeTYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhelkGKDKFAY 86
Cdd:cd03264 1 LQLENLTKRY--GKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPyaSLNPRSTVLEIISEPMEVHGMykNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:cd03264 71 RRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGI--PSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-241 |
4.36e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.61 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFHLgkgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD 82
Cdd:PRK13637 5 IENLTHIYMEGTPFEK------KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYyRQMQMIFQDPYASLNPRSTVLEIISEPMEVhGMykNKQGRTEKVHQLLEDVGLNRD-HANRYPHEFSGGQRQRIG 161
Cdd:PRK13637 79 SDIR-KKVGLVFQYPEYQLFEETIEKDIAFGPINL-GL--SEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYK 241
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-239 |
6.35e-31 |
|
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: 122.52 E-value: 6.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD 82
Cdd:TIGR02203 327 ARGDVEFRNVTFRY---PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 ---KFAYYRQMQMIFQDPYASlNPRSTVLEIISEpmevhgmyknkqgrtEKVHQLLEDVGLnRDHANRYPHEF------- 152
Cdd:TIGR02203 404 lrrQVALVSQDVVLFNDTIAN-NIAYGRTEQADR---------------AEIERALAAAYA-QDFVDKLPLGLdtpigen 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 153 ----SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLG 228
Cdd:TIGR02203 467 gvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDG 543
|
250
....*....|.
gi 2570312733 229 HLVEQTASREL 239
Cdd:TIGR02203 544 RIVERGTHNEL 554
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-228 |
7.96e-31 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 116.41 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElKGKDKFayyrqmqMIFQDpyASLNPRST 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRM-------VVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSV 186
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2570312733 187 QAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLG 228
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-252 |
9.26e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 9.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlgkGATLKAvdgiSFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfAY 86
Cdd:COG3840 2 LRLDDLTYRYG---DFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpyASLNPRSTVLEIIS---EPmevhGMYKNKQGRtEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIA 163
Cdd:COG3840 70 ERPVSMLFQE--NNLFPHLTVAQNIGlglRP----GLKLTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 164 RALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
....*....
gi 2570312733 244 LHPYTQALL 252
Cdd:COG3840 222 PPPALAAYL 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-242 |
1.17e-30 |
|
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: 116.18 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 14 KHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAYYRQMQMI 93
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 94 FQDP------------YAslNPRSTVLEII--SEPMEVHGMYKN-KQGRTEKVHQLledvGLnrdhanryphEFSGGQRQ 158
Cdd:cd03253 81 PQDTvlfndtigynirYG--RPDATDEEVIeaAKAAQIHDKIMRfPDGYDTIVGER----GL----------KLSGGEKQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRE 238
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
....
gi 2570312733 239 LYKK 242
Cdd:cd03253 222 LLAK 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-242 |
1.62e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.73 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGATLK-AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNG------KNIH 76
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 77 ELKGKdkfayyrqMQMIFQDPYASLnprstVLEIISEPM----EVHGMyKNKQGRtEKVHQLLEDVGLN--RDHAnryPH 150
Cdd:PRK13633 82 DIRNK--------AGMVFQNPDNQI-----VATIVEEDVafgpENLGI-PPEEIR-ERVDESLKKVGMYeyRRHA---PH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 151 EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHL 230
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
250
....*....|..
gi 2570312733 231 VEQTASRELYKK 242
Cdd:PRK13633 223 VMEGTPKEIFKE 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-231 |
1.93e-30 |
|
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: 114.99 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAY 86
Cdd:cd03245 3 IEFRNVSFSY---PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDP---YASLnpRSTVleiisepmevhgMYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEF----------- 152
Cdd:cd03245 77 RRNIGYVPQDVtlfYGTL--RDNI------------TLGAPLADDERILRAAELAGVT-DFVNKHPNGLdlqigergrgl 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 153 SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVkQISDRIGVMYLGHLV 231
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-241 |
2.74e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFAYYRQ-MQMIFQdpyaslNPR 104
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLKEIRKkIGIIFQ------NPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 -----STVLEIISEPMEvhgmykNKQGRTEKVHQLLED----VGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIA 175
Cdd:PRK13632 94 nqfigATVEDDIAFGLE------NKKVPPKKMKDIIDDlakkVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 176 DEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYK 241
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-260 |
3.87e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.26 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 24 LKAVDGISFTVKKGETYGIVGESGCGKST------------AGRTILGLYdqtegEVLFNGKNIHELKgkdkfAYYRQMQ 91
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTmiqltngliiseTGQTIVGDY-----AIPANLKKIKEVK-----RLRKEIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 92 MIFQDPYASLNPRSTVLEIISEPMEvhgMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPE 171
Cdd:PRK13645 94 LVFQFPEYQLFQETIEKDIAFGPVN---LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 172 FIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKkplhpyTQAL 251
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS------NQEL 244
|
....*....
gi 2570312733 252 LTAIPIPDP 260
Cdd:PRK13645 245 LTKIEIDPP 253
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
15-242 |
3.91e-30 |
|
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: 120.19 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 15 HFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYYRQMQMIF 94
Cdd:TIGR02204 344 NFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE---LRARMALVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 95 QDP---YASL-------NPRSTVLEII--SEPMEVHGMYKnkqGRTEKVHQLLEDVGLNrdhanrypheFSGGQRQRIGI 162
Cdd:TIGR02204 421 QDPvlfAASVmenirygRPDATDEEVEaaARAAHAHEFIS---ALPEGYDTYLGERGVT----------LSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 163 ARALALDPEFIIADEPISALDVS----VQAQVVNLMkrlqkeKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRE 238
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAEseqlVQQALETLM------KGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAE 560
|
....
gi 2570312733 239 LYKK 242
Cdd:TIGR02204 561 LIAK 564
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-231 |
4.12e-30 |
|
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: 120.74 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 20 KGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAYYRQMQMIFQDP-- 97
Cdd:TIGR03375 474 PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI---DPADLRRNIGYVPQDPrl 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 -YASLNprstvlEIIsepmevhgMYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEF-----------SGGQRQRIGIARA 165
Cdd:TIGR03375 551 fYGTLR------DNI--------ALGAPYADDEEILRAAELAGVT-EFVRRHPDGLdmqigergrslSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 166 LALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVkQISDRIGVMYLGHLV 231
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-247 |
4.74e-30 |
|
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: 117.14 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHE-LKGKDKFAYYRQMQMIFQDpyASLNPRSTVL 108
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsRKGIFLPPEKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIIsepmeVHGMYK----NKQGRTEKVHQLLedvglNRDH-ANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:TIGR02142 94 GNL-----RYGMKRarpsERRISFERVIELL-----GIGHlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 184 VSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPY 247
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-249 |
8.27e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 114.37 E-value: 8.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTI---LGLYD---QTEGEVLFNGKNIHELkgkDKFAYYRQMQMIFQDPYASlnP 103
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDskiKVDGKVLYFGKDIFQI---DAIKLRKEVGMVFQQPNPF--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 RSTVLEIISEPMEVHGMyKNKQGRTEKVHQLLEDVGLNR---DHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPIS 180
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGI-KEKREIKKIVEECLRKVGLWKevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 181 ALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQ 249
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-231 |
1.32e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.05 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAYYRQMQMIFQDPYASLNpr 104
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 STVLEIISEPMEVHGMYKNKQGRteKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRR--RVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2570312733 185 SVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK10908 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-239 |
1.36e-29 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 113.24 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGL--YDQTEGEVLFNGKNIHEL------ 78
Cdd:COG0396 1 LEIKNL--HVSVEGKEILK---GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELspdera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 -KGkdkfayyrqMQMIFQDP------------YASLNPRStvlEIISEPMEVHgmyknkqgrtEKVHQLLEDVGLNRDHA 145
Cdd:COG0396 76 rAG---------IFLAFQYPveipgvsvsnflRTALNARR---GEELSAREFL----------KLLKEKMKELGLDEDFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 146 NRYPHE-FSGGQRQRIGIARALALDPEFIIADEPISALDV-SVQ--AQVVNLMkrlqKEKGLTYLFIAHDLSMVKQIS-D 220
Cdd:COG0396 134 DRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRivAEGVNKL----RSPDRGILIITHYQRILDYIKpD 209
|
250
....*....|....*....
gi 2570312733 221 RIGVMYLGHLVEqTASREL 239
Cdd:COG0396 210 FVHVLVDGRIVK-SGGKEL 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-225 |
1.90e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.16 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlgkGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdKFA 85
Cdd:PRK11300 5 LLSVSGLMMRF----GGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH-QIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 yyrQMQMI--FQDpyASLNPRSTVLE--IISEPMEV-----HGMYKNKQGR------TEKVHQLLEDVGLnRDHANRYPH 150
Cdd:PRK11300 79 ---RMGVVrtFQH--VRLFREMTVIEnlLVAQHQQLktglfSGLLKTPAFRraeseaLDRAATWLERVGL-LEHANRQAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 151 EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-243 |
2.12e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.74 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLY---DQTEGEVLFNGKNIHElk 79
Cdd:PRK13640 2 KDNIVEFKHVSFTY---PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 gKDKFAYYRQMQMIFQDPYASLnPRSTVLEIISEPMEVHGMYKNKQGRTekVHQLLEDVGLnRDHANRYPHEFSGGQRQR 159
Cdd:PRK13640 77 -KTVWDIREKVGIVFQNPDNQF-VGATVGDDVAFGLENRAVPRPEMIKI--VRDVLADVGM-LDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASREL 239
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
....
gi 2570312733 240 YKKP 243
Cdd:PRK13640 231 FSKV 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-231 |
2.35e-29 |
|
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: 112.21 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFAY 86
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpyASLNPRSTVLEIisepMEVHGMYK--NKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIAR 164
Cdd:cd03263 74 RQSLGYCPQF--DALFDELTVREH----LRFYARLKglPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-242 |
3.01e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLkkHFHLGKGAtlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhELKGKDK 83
Cdd:PRK13636 3 DYILKVEEL--NYNYSDGT--HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQgrtEKVHQLLEDVGLnrDHANRYP-HEFSGGQRQRIGI 162
Cdd:PRK13636 78 MKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVR---KRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKK 242
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-222 |
5.55e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 112.08 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlGKGATLKAVDgisFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfay 86
Cdd:PRK11247 13 LLLNAVSKRY--GERTVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yRQMQMIFQDpyASLNPRSTVLEIISepMEVHGMYKnkqgrtEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL 166
Cdd:PRK11247 81 -EDTRLMFQD--ARLLPWKKVIDNVG--LGLKGQWR------DAALQALAAVGLA-DRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRI 222
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRV 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-211 |
6.54e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.02 E-value: 6.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHfhLGKGA-TLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELK 79
Cdd:PRK10584 1 MPAENIVEVHHLKKS--VGQGEhELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 GKDKFAYY-RQMQMIFQDpyASLNPRSTVLEIISEPMEVHGMyKNKQGRTEKVhQLLEDVGLNR--DHanrYPHEFSGGQ 156
Cdd:PRK10584 79 EEARAKLRaKHVGFVFQS--FMLIPTLNALENVELPALLRGE-SSRQSRNGAK-ALLEQLGLGKrlDH---LPAQLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD 211
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-242 |
1.11e-28 |
|
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: 109.54 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGL--YDQTEGEVLFNGKNIHELKGKDKF 84
Cdd:cd03217 1 LEIKDL--HVSVGGKEILK---GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 AyyRQMQMIFQdpyaslnprstvleiisEPMEVHGMyknkqgrteKVHQLLEDVGLNrdhanrypheFSGGQRQRIGIAR 164
Cdd:cd03217 76 R--LGIFLAFQ-----------------YPPEIPGV---------KNADFLRYVNEG----------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQI-SDRIGVMYLGHLVEqTASRELYKK 242
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK-SGDKELALE 194
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-233 |
1.32e-28 |
|
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: 110.31 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkhfHLGKGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDK--- 83
Cdd:TIGR03410 1 LEVSNL----NVYYGQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 -FAYYRQMQMIFqdpyaslnPRSTVLEIISEPMEVHGmyKNKQGRTEKVHQL---LEDVgLNRDHANrypheFSGGQRQR 159
Cdd:TIGR03410 76 gIAYVPQGREIF--------PRLTVEENLLTGLAALP--RRSRKIPDEIYELfpvLKEM-LGRRGGD-----LSGGQQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVAS 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-233 |
1.98e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLkkHFHLGkGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdKFA 85
Cdd:PRK13548 2 MLEARNL--SVRLG-GRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPA-ELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQM--QmifqdpYASLNPRSTVLEIISepMEVHGMYKNKQGRTEKVHQLLEDVGLnrDH-ANRYPHEFSGGQRQRIGI 162
Cdd:PRK13548 76 RRRAVlpQ------HSSLSFPFTVEEVVA--MGRAPHGLSRAEDDALVAAALAQVDL--AHlAGRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 163 ARALA------LDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-243 |
2.63e-28 |
|
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: 115.44 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKkhFHLGKGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGlYDQTE-GEVLFNGKnihELKGKDKFA 85
Cdd:TIGR03797 452 IEVDRVT--FRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG-FETPEsGSVFYDGQ---DLAGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDpyASLNPrSTVLEIIS--------EPMEVHGMyknkQGRTEKV-------HQLLEDVGLNrdhanryph 150
Cdd:TIGR03797 525 VRRQLGVVLQN--GRLMS-GSIFENIAggapltldEAWEAARM----AGLAEDIrampmgmHTVISEGGGT--------- 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 151 eFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQkekgLTYLFIAHDLSMVKQiSDRIGVMYLGHL 230
Cdd:TIGR03797 589 -LSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRV 662
|
250
....*....|...
gi 2570312733 231 VEQTASRELYKKP 243
Cdd:TIGR03797 663 VQQGTYDELMARE 675
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-233 |
2.91e-28 |
|
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: 109.18 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 31 SFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfAYYRQMQMIFQDpyASLNPRSTVLEI 110
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 111 ISepMEVHGMYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQV 190
Cdd:TIGR01277 91 IG--LGLHPGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2570312733 191 VNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-253 |
4.81e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.48 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTvENLLEVRNLkkHFHLGKGatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-----QTEGEVLFNGKNI 75
Cdd:PRK14239 1 MT-EPILQVSDL--SVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 76 HELKgKDKFAYYRQMQMIFQDPyaslNPRS-TVLEIISEPMEVHGMyKNKQGRTEKVHQLLEDVGL---NRDHANRYPHE 151
Cdd:PRK14239 75 YSPR-TDTVDLRKEIGMVFQQP----NPFPmSIYENVVYGLRLKGI-KDKQVLDEAVEKSLKGASIwdeVKDRLHDSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250 260
....*....|....*....|..
gi 2570312733 232 EQTASRELYKKPLHPYTQALLT 253
Cdd:PRK14239 227 EYNDTKQMFMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-243 |
6.59e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEG------EVLFNGKNIHELKGKDKfayyrQMQMIFQDPY 98
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNKKLKPLRK-----KVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 ASLNpRSTVLEIIS-EPMEVhGMYKNKQgrTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADE 177
Cdd:PRK13634 96 HQLF-EETVEKDICfGPMNF-GVSEEDA--KQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 178 PISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-243 |
6.69e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.66 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 10 RNLKKHFhlgkGATLKAVDgISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfayyRQ 89
Cdd:PRK11000 7 RNVTKAY----GDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 90 MQMIFQDpYAsLNPRSTVLEIISEPMEVHGmyKNKQGRTEKVHQLLEDVGLnrDHA-NRYPHEFSGGQRQRIGIARALAL 168
Cdd:PRK11000 77 VGMVFQS-YA-LYPHLSVAENMSFGLKLAG--AKKEEINQRVNQVAEVLQL--AHLlDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 169 DPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-231 |
2.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.02 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAY 86
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 Y---------------------RQMQMIFQDPYASLNpRSTVLE-IISEPMEvhgMYKNKQGRTEKVHQLLEDVGLNRDH 144
Cdd:PRK13651 83 VleklviqktrfkkikkikeirRRVGVVFQFAEYQLF-EQTIEKdIIFGPVS---MGVSKEEAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 145 ANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGV 224
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIF 237
|
....*..
gi 2570312733 225 MYLGHLV 231
Cdd:PRK13651 238 FKDGKII 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-239 |
3.12e-27 |
|
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: 106.36 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkhfHLGKGAtLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKF-- 84
Cdd:cd03224 1 LEVENL----NAGYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 --AYYRQMQMIFqdpyaslnPRSTVLEIIsepmEVhGMYKnkqGRTEKVHQLLEDVgLN-----RDHANRYPHEFSGGQR 157
Cdd:cd03224 76 giGYVPEGRRIF--------PELTVEENL----LL-GAYA---RRRAKRKARLERV-YElfprlKERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
..
gi 2570312733 238 EL 239
Cdd:cd03224 218 EL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-262 |
5.01e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.40 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngkNIHELKGKDKFA 85
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-----QVGDIYIGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQ------------------MQMIFQDPYASLNPRSTVLEIISEPMEVhGMYKNKQGRTEKVHqlLEDVGLNRDHANR 147
Cdd:PRK13631 96 NHELitnpyskkiknfkelrrrVSMVFQFPEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFY--LNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 148 YPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRlQKEKGLTYLFIAHDLSMVKQISDRIGVMYL 227
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
250 260 270
....*....|....*....|....*....|....*
gi 2570312733 228 GHLVEQTASRELYkkplhpYTQALLTAIPIPDPDV 262
Cdd:PRK13631 252 GKILKTGTPYEIF------TDQHIINSTSIQVPRV 280
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-225 |
5.76e-27 |
|
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: 110.84 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYYRQMQMIFQDPYAslnPR 104
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQIAWVPQHPFL---FA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 STVLEIIsepmevhGMYKNKQGRTEkVHQLLEDVGLNRDHANR----------YPHEFSGGQRQRIGIARALALDPEFII 174
Cdd:TIGR02857 410 GTIAENI-------RLARPDASDAE-IREALERAGLDEFVAALpqgldtpigeGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2570312733 175 ADEPISALDVSVQAQVVNLMKRLQkeKGLTYLFIAHDLSmVKQISDRIGVM 225
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-256 |
6.39e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 111.35 E-value: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHLGKGaTLKAVDGISFTVKKGETYGIVGESGCGKSTAgRTILGLYDQ-TEGEVLFNGKNIHELKGkDKF 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEE-QVEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLDKpTSGTYRVAGQDVATLDA-DAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 AYYRQMQM--IFQDPYasLNPRSTVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGI 162
Cdd:PRK10535 81 AQLRREHFgfIFQRYH--LLSHLTAAQNVEVPAVYAGLERKQ--RLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQkEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRElyKK 242
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE--KV 231
|
250
....*....|....
gi 2570312733 243 PLHPYTQALLTAIP 256
Cdd:PRK10535 232 NVAGGTEPVVNTAS 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-224 |
7.90e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.40 E-value: 7.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQT--EGEVLFNGKNIH----- 76
Cdd:PRK13549 3 EYLLEMKNITKTF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQasnir 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 77 --ELKGkdkfayyrqMQMIFQDpyASLNPRSTVLEII---SEPMEVHGMYKNKQgrTEKVHQLLEDVGLNRDHANRYpHE 151
Cdd:PRK13549 78 dtERAG---------IAIIHQE--LALVKELSVLENIflgNEITPGGIMDYDAM--YLRAQKLLAQLKLDINPATPV-GN 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGV 224
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICV 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-258 |
9.54e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.81 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKkhfHLGKGaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNG-----KNIHELK 79
Cdd:PRK13652 2 HLIETRDLC---YSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 gkdkfayyRQMQMIFQDPYASLNPRSTVLEIISEPMEvhgMYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQR 159
Cdd:PRK13652 78 --------KFVGLVFQNPDDQIFSPTVEQDIAFGPIN---LGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
250
....*....|....*....
gi 2570312733 240 YKKPlHPYTQALLTAIPIP 258
Cdd:PRK13652 226 FLQP-DLLARVHLDLPSLP 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-266 |
1.07e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLKKHFhlgkGATlKAVDGISFTVKKGETYGIVGESGCGKST----AGRtilgLYDQTEGEVLFNGKNIHELKGKDk 83
Cdd:COG4604 3 EIKNVSKRY----GGK-VVLDDVSLTIPKGGITALIGPNGAGKSTllsmISR----LLPPDSGEVLVDGLDVATTPSRE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 faYYRQMQMIFQDPyaSLNPRSTVLEIISepmevHGMYKNKQGR-----TEKVHQLLEDVGLNrDHANRYPHEFSGGQRQ 158
Cdd:COG4604 73 --LAKRLAILRQEN--HINSRLTVRELVA-----FGRFPYSKGRltaedREIIDEAIAYLDLE-DLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVsvqAQVVNLMKRLQK---EKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTA 235
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDM---KHSVQMMKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
250 260 270
....*....|....*....|....*....|....
gi 2570312733 236 SRELykkplhpYTQALLTAI---PIPDPDVEDKR 266
Cdd:COG4604 220 PEEI-------ITPEVLSDIydtDIEVEEIDGKR 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-243 |
1.68e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIH-ELKGKDKFAYYRQMQMIFQDPYASLNp 103
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQFPEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 RSTVLEIISEPMEVHGMYKNKQgrTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEA--KEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 184 VSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-225 |
3.70e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 102.29 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKkhFHLGkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDK--- 83
Cdd:cd03246 1 LEVENVS--FRYP-GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELgdh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQDpyaslnprsTVLEIIsepmevhgmyknkqgrtekvhqlledvglnrdhanrypheFSGGQRQRIGIA 163
Cdd:cd03246 78 VGYLPQDDELFSG---------SIAENI----------------------------------------LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570312733 164 RALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQiSDRIGVM 225
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVL 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-203 |
9.75e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.80 E-value: 9.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlGKgatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHEL-------K 79
Cdd:COG1137 4 LEAENLVKSY--GK---RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrarL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 GkdkFAYYRQMQMIFQDpyasLnprsTVLEIISEPMEVHGmyKNKQGRTEKVHQLLEDVGLNRdHANRYPHEFSGGQRQR 159
Cdd:COG1137 79 G---IGYLPQEASIFRK----L----TVEDNILAVLELRK--LSKKEREERLEELLEEFGITH-LRKSKAYSLSGGERRR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2570312733 160 IGIARALALDPEFIIADEPISALD-VSV---QAQVVNLmkrlqKEKGL 203
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDpIAVadiQKIIRHL-----KERGI 187
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-233 |
1.34e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.80 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 31 SFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfayyRQMQMIFQDpyASLNPRSTVLEI 110
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQE--NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 111 ISEPMeVHGMYKNKQGRtEKVHQLLEDVGLNRDHAnRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQV 190
Cdd:cd03298 91 VGLGL-SPGLKLTAEDR-QAIEVALARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2570312733 191 VNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQ 233
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
26-212 |
2.01e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhELKGKDKfayyrqmQMIFQDpyASLNPRS 105
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER-------GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 TVLEIISEPMEVHGMYKNKqgRTEKVHQLLEDVGLNRDHAnRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVS 185
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQ--RLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*..
gi 2570312733 186 VQAQVVNLMKRLQKEKGLTYLFIAHDL 212
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-243 |
2.37e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.73 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAYYRQMQMIFQDPyasLNPRSTVL 108
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHRQVALVGQEP---VLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIIS---------EPMEVHGMYKNKQGRTEKVHQLLEDVGlnrDHANryphEFSGGQRQRIGIARALALDPEFIIADEPI 179
Cdd:TIGR00958 573 ENIAygltdtpdeEIMAAAKAANAHDFIMEFPNGYDTEVG---EKGS----QLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 180 SALDVSVQAQVVNLMKRlqkeKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:TIGR00958 646 SALDAECEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-230 |
2.44e-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: 100.20 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHfhlgkgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDk 83
Cdd:cd03215 2 EPVLEVRGLSVK---------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fAYYRQMQMIFQDPYAS-LNPRSTVLEIISepmevhgmyknkqgrtekVHQLLedvglnrdhanryphefSGGQRQRIGI 162
Cdd:cd03215 72 -AIRAGIAYVPEDRKREgLVLDLSVAENIA------------------LSSLL-----------------SGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-239 |
2.93e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAgrtiLGL----YDQTEGEVLFNGKNIHELKGKdkfAYYRQMQMIFQDpyASL 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLlqrvFDPQSGRILIDGTDIRTVTRA---SLRRNIAVVFQD--AGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 102 NPRStvleiISEPMEVhgmyknkqGRTEKVHQLLEDvGLNRDHAnrypHEF-------------------SGGQRQRIGI 162
Cdd:PRK13657 421 FNRS-----IEDNIRV--------GRPDATDEEMRA-AAERAQA----HDFierkpdgydtvvgergrqlSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQkeKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASREL 239
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-266 |
3.59e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.48 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEG-----EVLFNGKNIHELKgkDKFAYYRQMQMIFQDPyasl 101
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR--DVLEFRRRVGMLFQRP---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 102 NP-RSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEdVGL---NRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADE 177
Cdd:PRK14271 111 NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTE-VGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 178 PISALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQALLTAIpi 257
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL-- 265
|
....*....
gi 2570312733 258 pDPDVEDKR 266
Cdd:PRK14271 266 -SGDVKDAK 273
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-239 |
3.79e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 31 SFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNiHELKGKDKfayyRQMQMIFQDpyASLNPRSTVLEI 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSR----RPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 111 ISepMEVH-GMYKNKQGRtEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQ 189
Cdd:PRK10771 92 IG--LGLNpGLKLNAAQR-EKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570312733 190 VVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-233 |
4.28e-25 |
|
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: 99.69 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGkdkfAY 86
Cdd:cd03247 1 LSINNV--SFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----AL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYASlnprSTVLeiisepmevhgmyknkqgrtekvhqlLEDVGLnrdhanryphEFSGGQRQRIGIARAL 166
Cdd:cd03247 74 SSLISVLNQRPYLF----DTTL--------------------------RNNLGR----------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQIsDRIGVMYLGHLVEQ 233
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
27-243 |
8.91e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 105.03 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGK---DKFAYYRQMQMIFQdpyaslnp 103
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlaNSVAMVDQDIFLFE-------- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 rSTVLEIIS--------EPME-------VHGMYKNKQGRTEkvHQLLEDvGLNrdhanrypheFSGGQRQRIGIARALAL 168
Cdd:TIGR03796 567 -GTVRDNLTlwdptipdADLVrackdaaIHDVITSRPGGYD--AELAEG-GAN----------LSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 169 DPEFIIADEPISALDVSVQAQVV-NLMKRlqkekGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKKP 243
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDdNLRRR-----GCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-231 |
1.51e-24 |
|
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: 99.27 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 17 HLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQ---TEGEVLFNGKNIHELKGKDKFAYYRQmqmi 93
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYVRQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 94 fQDPYAS-LNPRSTVLEIISEPMEVHGMYKNKQGRTEKVhqLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEF 172
Cdd:cd03234 89 -DDILLPgLTVRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 173 IIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
27-242 |
1.80e-24 |
|
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: 104.05 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHELKGKDKFAYYRQMQMIFQDPYasLNPRSt 106
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDG---VDLAIADPAWLRRQMGVVLQENV--LFSRS- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VLEIISEpmevhgmyKNKQGRTEKVHQLLEDVGLNrDHANRYPHEF-----------SGGQRQRIGIARALALDPEFIIA 175
Cdd:TIGR01846 547 IRDNIAL--------CNPGAPFEHVIHAAKLAGAH-DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 176 DEPISALDVSVQAQVVNLMKRLQkeKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKK 242
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREIC--RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLAL 681
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-230 |
2.86e-24 |
|
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: 103.20 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 19 GKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGkniHELKGKDKFAYYRQMQMIFQDpy 98
Cdd:TIGR01842 329 GKKPTLR---GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQWDRETFGKHIGYLPQD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 ASLNPrSTVLEIIS------EPMEVHgmyknKQGRTEKVHQLLE------DVGLNRDHANrypheFSGGQRQRIGIARAL 166
Cdd:TIGR01842 401 VELFP-GTVAENIArfgenaDPEKII-----EAAKLAGVHELILrlpdgyDTVIGPGGAT-----LSGGQRQRIALARAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQIsDRIGVMYLGHL 230
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-239 |
3.79e-24 |
|
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: 103.28 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAYYRQMQMIFQDPYASlnpR 104
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYLPQEPYIF---S 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 STVLEIIsepmevhgMYKNKQGRT-EKVHQLLEDVGLNRDHANrYPHEF-----------SGGQRQRIGIARALALDPEF 172
Cdd:TIGR01193 562 GSILENL--------LLGAKENVSqDEIWAACEIAEIKDDIEN-MPLGYqtelseegssiSGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 173 IIADEPISALDVSVQAQVV-NLMKRLQKekglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASREL 239
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVnNLLNLQDK----TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-242 |
4.07e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.79 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKG---KDKFAYYRQMQMIFQD------ 96
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLaslRNQVALVSQNVHLFNDtianni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 97 PYASlNPRSTVLEIISEPMEVHGMyknkqGRTEKVHQLLEDV-GLNrdhanryPHEFSGGQRQRIGIARALALDPEFIIA 175
Cdd:PRK11176 438 AYAR-TEQYSREQIEEAARMAYAM-----DFINKMDNGLDTViGEN-------GVLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 176 DEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASRELYKK 242
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-238 |
4.57e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 14 KHFHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfAYYRQMQMI 93
Cdd:PRK11231 6 ENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 94 FQDPyasLNPRS-TVLEIIS---EPmevhgmYKNKQGR-----TEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIAR 164
Cdd:PRK11231 82 PQHH---LTPEGiTVRELVAygrSP------WLSLWGRlsaedNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRE 238
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-225 |
5.67e-24 |
|
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: 100.56 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 41 GIVGESGCGKSTAGRTILGLyDQTE-------GEVLFNGKNIHELKgkdkfAYYRQMQMIFQDpyASLNPRSTVLEiise 113
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGL-ERPDsgrirlgGEVLQDSARGIFLP-----PHRRRIGYVFQE--ARLFPHLSVRG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 114 pmevhgmykN---------KQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:COG4148 97 ---------NllygrkrapRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2570312733 185 SVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLL 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-231 |
1.08e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 97.40 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 14 KHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGknihELKGKDKFAYYRQMQMI 93
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 94 FqdpyaslNPRSTVLEIISePME----VHGMYKNKQGR-TEKVHQLLE--DVGLNRDHANRyphEFSGGQRQRIGIARAL 166
Cdd:cd03267 100 F-------GQKTQLWWDLP-VIDsfylLAAIYDLPPARfKKRLDELSEllDLEELLDTPVR---QLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-249 |
1.30e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 23 TLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-----QTEGEVLFNGKNIHELKgKDKFAYYRQMQMIFQDP 97
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERR-VNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 yaSLNPRStVLEIISEPMEVHGmYKNKQGRTEKVHQLLEDVGL-----NRDHANRYphEFSGGQRQRIGIARALALDPEF 172
Cdd:PRK14258 98 --NLFPMS-VYDNVAYGVKIVG-WRPKLEIDDIVESALKDADLwdeikHKIHKSAL--DLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 173 IIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMY-----LGHLVEQTASRELYKKPLHPY 247
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHDSR 251
|
..
gi 2570312733 248 TQ 249
Cdd:PRK14258 252 TR 253
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-212 |
1.41e-23 |
|
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: 97.46 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVL------FNGKNIHELKGK------DKFAYYRqmqmif 94
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELRKRiglvspALQLRFP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 95 qdpyaslnPRSTVLE-IISEPMEVHGMYKN---KQgrTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDP 170
Cdd:COG1119 93 --------RDETVLDvVLSGFFDSIGLYREptdEQ--RERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2570312733 171 EFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDL 212
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-250 |
1.47e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-----QTEGEVLFNGKNIHEl 78
Cdd:PRK14243 8 ETVLRTENLNVYY----GSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 KGKDKFAYYRQMQMIFQDPYASlnPRStVLEIISEPMEVHGMyknKQGRTEKVHQLLEDVGL---NRDHANRYPHEFSGG 155
Cdd:PRK14243 82 PDVDPVEVRRRIGMVFQKPNPF--PKS-IYDNIAYGARINGY---KGDMDELVERSLRQAALwdeVKDKLKQSGLSLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkgLTYLFIAHDLSMVKQISDRI----------GVM 225
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTaffnveltegGGR 233
|
250 260
....*....|....*....|....*
gi 2570312733 226 YlGHLVEQTASRELYKKPLHPYTQA 250
Cdd:PRK14243 234 Y-GYLVEFDRTEKIFNSPQQQATRD 257
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-269 |
2.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLkkHFHLGKGAtlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElkgKD 82
Cdd:PRK13647 1 MDNIIEVEDL--HFRYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---EN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYYRQMQMIFQDPYASLNPrSTVLEIIS-EPMEvhgMYKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIG 161
Cdd:PRK13647 74 EKWVRSKVGLVFQDPDDQVFS-STVWDDVAfGPVN---MGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYK 241
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2570312733 242 KPL---------------HPYTQALLTAIPIpdpDVEDKRERI 269
Cdd:PRK13647 228 EDIveqaglrlplvaqifEDLPELGQSKLPL---TVKEAVQII 267
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-239 |
2.70e-23 |
|
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: 100.28 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQT--EGEVLFNGKNIHELKGKDK 83
Cdd:TIGR02633 1 LLEMKGIVKTF-----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAyyRQMQMIFQDpyASLNPRSTVLEIISEPMEV--HGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIG 161
Cdd:TIGR02633 76 ER--AGIVIIHQE--LTLVPELSVAENIFLGNEItlPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-233 |
2.98e-23 |
|
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: 95.64 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkDKFAYYRQMQMIFQDPY------- 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 ASLNPrstvLEIISEpmevhgmyknkqgrtEKVHQLLEDVGLnRDHANRYP-------HE----FSGGQRQRIGIARALA 167
Cdd:cd03244 96 SNLDP----FGEYSD---------------EELWQALERVGL-KEFVESLPggldtvvEEggenLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 168 LDPEFIIADEPISALDVSVQAQVVNLMKRlqKEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQ 233
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEF 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-222 |
4.18e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLkkHFHLGkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKG 80
Cdd:PRK10247 2 QENSPLLQLQNV--GYLAG---DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KdkfAYYRQMQMIFQDPyaSLNPrSTVLEIISEPMEVhgmyKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRI 160
Cdd:PRK10247 77 E---IYRQQVSYCAQTP--TLFG-DTVYDNLIFPWQI----RNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRI 222
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-239 |
4.63e-23 |
|
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: 95.43 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLkkhfHLGKGATlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdk 83
Cdd:COG0410 1 MPMLEVENL----HAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fAYYR---------QMQMIFqdpyaslnPRSTV---LEIisepmevhGMYKNKQGRteKVHQLLEDVglnrdhANRYP-- 149
Cdd:COG0410 72 -PHRIarlgigyvpEGRRIF--------PSLTVeenLLL--------GAYARRDRA--EVRADLERV------YELFPrl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 150 HEF--------SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDR 221
Cdd:COG0410 127 KERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADR 205
|
250
....*....|....*...
gi 2570312733 222 IGVMYLGHLVEQTASREL 239
Cdd:COG0410 206 AYVLERGRIVLEGTAAEL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
9.70e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlgKGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFnGKNIhelkgkdKFA 85
Cdd:COG0488 315 VLELEGLSKSY---GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQmifqdpyASLNPRSTVLEIISEPMEvhgmyknkQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARA 165
Cdd:COG0488 382 YFDQHQ-------EELDPDKTVLDELRDGAP--------GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 166 LALDPEFIIADEPISALDV-SVQAqvvnLMKRLQKEKGlTYLFIAHDLSMVKQISDRI 222
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHDRYFLDRVATRI 499
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-212 |
1.61e-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: 98.20 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGAtlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaY 86
Cdd:TIGR02868 335 LELRDL--SAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---V 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYASlnpRSTVLEIIsepmevhgMYKNKQGRTEKVHQLLEDVGLNrDHANRYPH-----------EFSGG 155
Cdd:TIGR02868 408 RRRVSVCAQDAHLF---DTTVRENL--------RLARPDATDEELWAALERVGLA-DWLRALPDgldtvlgeggaRLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMkrLQKEKGLTYLFIAHDL 212
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-231 |
1.62e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.93 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD 82
Cdd:PRK09700 2 ATPYISMAGIGKSF-----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 kfAYYRQMQMIFQDpyASLNPRSTVLE---IISEPM-EVHGM----YKNKQGRTEkvhQLLEDVGLNRDhANRYPHEFSG 154
Cdd:PRK09700 77 --AAQLGIGIIYQE--LSVIDELTVLEnlyIGRHLTkKVCGVniidWREMRVRAA---MMLLRVGLKVD-LDEKVANLSI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 155 GQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKE-KGLTYlfIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVY--ISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-239 |
2.69e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRtILGLYDQ-TEGEVLFNGKNIHELKGKdkfAYYRQMQMIFQD-PYASlnpRSTV 107
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPpSEGEILLDAQPLESWSSK---AFARKVAYLPQQlPAAE---GMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 108 LEIIS---EPMevHG-MYKNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:PRK10575 103 RELVAigrYPW--HGaLGRFGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 184 VSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
231-298 |
3.50e-22 |
|
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: 88.23 E-value: 3.50e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 231 VEQTASRELYKKPLHPYTQALLTAIPIPDPDvedKRERIILQGELPSPMNPPSGCVFRTRCAYAMEAC 298
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPP---KRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
27-225 |
4.00e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfAYYRQMQMIFQDPYASLNPR-S 105
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR---AASRRVASVPQDTSLSFEFDvR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 TVLEIISEPMEVHGMYKNKQGRTeKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVS 185
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETDRA-AVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2570312733 186 VQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:PRK09536 174 HQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-212 |
6.79e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.84 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfAY 86
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-----EY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQM--IFQDPYASLNPRSTVLEIISepmevhgMYKNK-----------QGRTEKVHQLLEDVGL---NRDHAnryPH 150
Cdd:COG1101 77 KRAKYIgrVFQDPMMGTAPSMTIEENLA-------LAYRRgkrrglrrgltKKRRELFRELLATLGLgleNRLDT---KV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 151 EF-SGGQRQrigiarALAL------DPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDL 212
Cdd:COG1101 147 GLlSGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-245 |
1.10e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTveNLLEVRNLKKHFHLGKGA--TLK---------------AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQ 63
Cdd:COG1134 1 MS--SMIEVENVSKSYRLYHEPsrSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 64 TEGEVLFNGKnIH---ELkGkdkfayyrqmqmifqdpyASLNPRSTVLEIISEPMEVHGMYKnkqgrtEKVHQLLEDVgl 140
Cdd:COG1134 79 TSGRVEVNGR-VSallEL-G------------------AGFHPELTGRENIYLNGRLLGLSR------KEIDEKFDEI-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 141 nrdhanrypHEFSG--------------GQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYL 206
Cdd:COG1134 131 ---------VEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVI 200
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2570312733 207 FIAHDLSMVKQISDRIGVMYLGHLVEQTASRE---LYKKPLH 245
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEviaAYEALLA 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-231 |
1.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNG---KNIHELKGKDKFayyrqMQMIFQDPYASLN 102
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKL-----VGIVFQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 103 PRsTVLEIIS--------EPMEVHgmyknkqgrtEKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIARALALDPEFII 174
Cdd:PRK13644 92 GR-TVEEDLAfgpenlclPPIEIR----------KRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 175 ADEPISALDVSVQAQVVNLMKRLQkEKGLTYLFIAHDLSMVkQISDRIGVMYLGHLV 231
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIV 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-232 |
2.08e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.67 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKG-----------------ATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVL 69
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 70 FNGKnIHELKGkdkFAyyrqmqmifqdpyASLNPRSTVLEIISEPMEVHGMyKNKQGRtEKVHQLLEDVGLNrDHANRYP 149
Cdd:cd03220 81 VRGR-VSSLLG---LG-------------GGFNPELTGRENIYLNGRLLGL-SRKEID-EKIDEIIEFSELG-DFIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 150 HEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGH 229
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
...
gi 2570312733 230 LVE 232
Cdd:cd03220 220 IRF 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-239 |
2.10e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.89 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLkkHFHLgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTagrtILGL----YDQTEGEVLFNGKNIHELkgk 81
Cdd:PRK11160 338 SLTLNNV--SFTY-PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLltraWDPQQGEILLNGQPIADY--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQMQMIFQDPY---ASLnpRSTVLeiISEPmevhgmyknkQGRTEKVHQLLEDVGL-----NRDHANRYPHE-- 151
Cdd:PRK11160 408 SEAALRQAISVVSQRVHlfsATL--RDNLL--LAAP----------NASDEALIEVLQQVGLeklleDDKGLNAWLGEgg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 --FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQIsDRIGVMYLGH 229
Cdd:PRK11160 474 rqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQ 550
|
250
....*....|
gi 2570312733 230 LVEQTASREL 239
Cdd:PRK11160 551 IIEQGTHQEL 560
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-210 |
2.16e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKkhFHLGKGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNgknihelkgkdk 83
Cdd:COG4178 360 DGALALEDLT--LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP------------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fayyRQMQMIF--QDPYAslnPRSTVLEIISEPMEVHGMyknkqgRTEKVHQLLEDVGL----NR-DHANRYPHEFSGGQ 156
Cdd:COG4178 424 ----AGARVLFlpQRPYL---PLGTLREALLYPATAEAF------SDAELREALEAVGLghlaERlDEEADWDQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQvvnLMKRLQKE-KGLTYLFIAH 210
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREElPGTTVISVGH 542
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-238 |
2.76e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLkkhfHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDk 83
Cdd:COG3845 255 EVVLEVENL----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fayYRQMQM--IFQDPYAS-LNPRSTVLE------IISEPMEVHGMYKNKQGRtEKVHQLLE--DVglnrdhanRYPHE- 151
Cdd:COG3845 330 ---RRRLGVayIPEDRLGRgLVPDMSVAEnlilgrYRRPPFSRGGFLDRKAIR-AFAEELIEefDV--------RTPGPd 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 -----FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:COG3845 398 tparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMY 476
|
250
....*....|....*.
gi 2570312733 227 LGHLVE----QTASRE 238
Cdd:COG3845 477 EGRIVGevpaAEATRE 492
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-239 |
3.14e-21 |
|
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: 90.30 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 32 FTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNihELKGKDKFAYYRQMQMIFQD-----PYASLNPRST 106
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS--PGKGWRHIGYVPQRHEFAWDfpisvAHTVMSGRTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VLEIISEPmevhgmyknKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSV 186
Cdd:TIGR03771 79 HIGWLRRP---------CVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 187 QAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIgVMYLGHLVEQTASREL 239
Cdd:TIGR03771 149 QELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-230 |
4.67e-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: 89.84 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfAYYRQMQMIFQDPyaSLNPRStVL 108
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHSKVSLVGQEP--VLFARS-LQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIISEPMEVHGMYKNKQGrTEKVH-----QLLEDvGLNRDhANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:cd03248 106 DNIAYGLQSCSFECVKEA-AQKAHahsfiSELAS-GYDTE-VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2570312733 184 VSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHL 230
Cdd:cd03248 183 AESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
30-230 |
7.16e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA----YY---RQMQMIFQDpyASLN 102
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvYLpedRQSSGLYLD--APLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 103 PRSTVLEIISEPMEVHGMYKNKqgRTEKVHQLLedvGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISAL 182
Cdd:PRK15439 360 WNVCALTHNRRGFWIKPARENA--VLERYRRAL---NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2570312733 183 DVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-243 |
7.69e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 93.24 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 14 KHFHLgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKD---KFAYYRQM 90
Cdd:PRK10789 319 RQFTY-PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 91 QMIFQDPYASL----NPRSTVLEIisepmevhgmykNKQGRTEKVHqllEDVglnrdhaNRYPHEF-----------SGG 155
Cdd:PRK10789 398 PFLFSDTVANNialgRPDATQQEI------------EHVARLASVH---DDI-------LRLPQGYdtevgergvmlSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTA 235
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
....*...
gi 2570312733 236 SRELYKKP 243
Cdd:PRK10789 533 HDQLAQQS 540
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-242 |
1.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHEL-KGKDKFAYYRQMQMIFQDPYASLNp 103
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIKPVRKKVGVVFQFPESQLF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 RSTVLEIISEPMEVHGMYKNKqgrTEKVH-QLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISAL 182
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEK---AEKIAaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 183 DVSVQAQVVNLMKRLQkEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKK 242
Cdd:PRK13643 176 DPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-225 |
1.55e-20 |
|
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: 92.12 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 21 GATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkGKDKFAyyrqmQMIF---QDP 97
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DREELG-----RHIGylpQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 yaSLNPrSTVLEIISEPMEVhgmyknkqgRTEKVHQLLEDVGLnrdhanrypHEF-------------------SGGQRQ 158
Cdd:COG4618 416 --ELFD-GTIAENIARFGDA---------DPEKVVAAAKLAGV---------HEMilrlpdgydtrigeggarlSGGQRQ 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVkQISDRIGVM 225
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVL 539
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-225 |
1.60e-20 |
|
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: 87.91 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihelkgkdkFAY 86
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS----------IAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDpyaslnprsTVLEII--SEPMEvHGMYKnkqgRTEKVHQLLEDV--------------GLNrdhanryph 150
Cdd:cd03250 71 VSQEPWIQNG---------TIRENIlfGKPFD-EERYE----KVIKACALEPDLeilpdgdlteigekGIN--------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 151 eFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVN--LMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVM 225
Cdd:cd03250 128 -LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVL 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-231 |
1.69e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 25 KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNI-HELKGKDKFAYYRQMQMIFQDPYASLNp 103
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 RSTVLEIISEPMEVHGMYKNKQGRT--EKVHQlledVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISA 181
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAEALarEKLAL----VGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570312733 182 LDVSVQAQVVNLMKRLQkEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK13649 176 LDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-231 |
1.75e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELK- 79
Cdd:PRK15439 6 TTAPPLLCARSISKQY-----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 80 -GKDKFAYYrqmqMIFQDPYasLNPRSTVLEIIsepmeVHGMYKNkQGRTEKVHQLLEDVGLNRDhanryPHEFSG---- 154
Cdd:PRK15439 81 aKAHQLGIY----LVPQEPL--LFPNLSVKENI-----LFGLPKR-QASMQKMKQLLAALGCQLD-----LDSSAGslev 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 155 GQRQRIGIARALALDPEFIIADEPISALdvsVQAQVVNLMKRLQK--EKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK15439 144 ADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-216 |
2.23e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.40 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKkhFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNgkNIHELKGKDKFAY 86
Cdd:PTZ00265 383 IQFKNVR--FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYASLNP-RSTV---------LEIISEPMEVHGM--YKNKQGRT-------------------------E 129
Cdd:PTZ00265 459 RSKIGVVSQDPLLFSNSiKNNIkyslyslkdLEALSNYYNEDGNdsQENKNKRNscrakcagdlndmsnttdsneliemR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 130 KVHQLLED---VGLNR-----DHANRYPHEF-----------SGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQV 190
Cdd:PTZ00265 539 KNYQTIKDsevVDVSKkvlihDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|....*.
gi 2570312733 191 VNLMKRLQKEKGLTYLFIAHDLSMVK 216
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-260 |
3.66e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 18 LGKGATLKAvDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYYRQMQMIFQDp 97
Cdd:PRK10253 15 LGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 yASLNPRSTVLEIISEPMEVHG--MYKNKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIA 175
Cdd:PRK10253 90 -ATTPGDITVQELVARGRYPHQplFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 176 DEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYKKPLHPYTQALLTAI 255
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
....*
gi 2570312733 256 pIPDP 260
Cdd:PRK10253 248 -IDDP 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-194 |
4.90e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 86.26 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKdkfaYYRQMQMIFQDPyaSLNPRSTVL 108
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE----PHENILYLGHLP--GLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIISEPMEVHGmyknkqGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQA 188
Cdd:TIGR01189 92 ENLHFWAAIHG------GAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
....*.
gi 2570312733 189 QVVNLM 194
Cdd:TIGR01189 165 LLAGLL 170
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-239 |
7.09e-20 |
|
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: 90.26 E-value: 7.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 28 DGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfayyrQmqmifqdpyASLN----- 102
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---------Q---------ASLRaaigi 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 103 -PRSTVL--EIIsepmevhgmYKNKQ-GRTEKVHQLLEDVGlnrDHANRypHEF-------------------SGGQRQR 159
Cdd:COG5265 437 vPQDTVLfnDTI---------AYNIAyGRPDASEEEVEAAA---RAAQI--HDFieslpdgydtrvgerglklSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDV----SVQAQvvnlMKRLQKEKglTYLFIAHDLSMVkQISDRIGVMYLGHLVEQTA 235
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSrterAIQAA----LREVARGR--TTLVIAHRLSTI-VDADEILVLEAGRIVERGT 575
|
....
gi 2570312733 236 SREL 239
Cdd:COG5265 576 HAEL 579
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-239 |
7.88e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkdkfAY 86
Cdd:PRK13537 8 IDFRNVEKRY----GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR------AR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPYASLNPRSTVleiiSEPMEVHGMY---KNKQGRtEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIA 163
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTV----RENLLVFGRYfglSAAAAR-ALVPPLLEFAKL-ENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 164 RALALDPEFIIADEPISALDvsvqAQVVNLM-KRLQK--EKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLD----PQARHLMwERLRSllARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-232 |
8.00e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 85.93 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATL-KAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfa 85
Cdd:cd03369 7 IEVENLSVRY----APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 YYRQMQMIFQDPyaslnprsTVLE-IISEPMEVHGMYKNKQgrtekVHQLLE--DVGLNrdhanrypheFSGGQRQRIGI 162
Cdd:cd03369 80 LRSSLTIIPQDP--------TLFSgTIRSNLDPFDEYSDEE-----IYGALRvsEGGLN----------LSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQvvnLMKRLQKE-KGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVE 232
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDAL---IQKTIREEfTNSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-222 |
9.30e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.22 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLKKHFHL-----GKGATLK-----------AVDGISFTVKKGETYGIVGESGCGKSTagrTI---LGLYDQTEGEV 68
Cdd:COG4586 3 EVENLSKTYRVyekepGLKGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKST---TIkmlTGILVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 69 LFNGKNIHelkgKDKFAYYRQMQMIF-Q------DpyasLNPRSTvLEIISEpmevhgMYK-NKQGRTEKVHQLLE--DV 138
Cdd:COG4586 80 RVLGYVPF----KRRKEFARRIGVVFgQrsqlwwD----LPAIDS-FRLLKA------IYRiPDAEYKKRLDELVEllDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 139 G--LNRdhanryP-HEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMV 215
Cdd:COG4586 145 GelLDT------PvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI 218
|
....*..
gi 2570312733 216 KQISDRI 222
Cdd:COG4586 219 EALCDRV 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-233 |
9.52e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.90 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGL--YdqtEGEVLFNGKNIHELkgkDKF 84
Cdd:PRK11174 350 IEAEDLEILSPDGK----TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELREL---DPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 AYYRQMQMIFQDPyaSLnPRSTVLEIISepmevhgmYKNKQGRTEKVHQLLEDVGLN---RDHANRYPHE-------FSG 154
Cdd:PRK11174 420 SWRKHLSWVGQNP--QL-PHGTLRDNVL--------LGNPDASDEQLQQALENAWVSeflPLLPQGLDTPigdqaagLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 155 GQRQRIGIARALALDPEFIIADEPISALDVSVQAQVvnlMKRLQKE-KGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVEQ 233
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV---MQALNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQ 564
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
1.78e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 86.23 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 1 MTVENLLEVRNLkkHFHLGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILG--LYDQTEGEVLFNGKNIHEL 78
Cdd:CHL00131 2 NKNKPILEIKNL--HASVNENEILK---GLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 KGKDK--------FAY----------------YRQMQMIFQDPyaSLNPRStVLEIISEPMEVhgmyknkqgrtekvhql 134
Cdd:CHL00131 77 EPEERahlgiflaFQYpieipgvsnadflrlaYNSKRKFQGLP--ELDPLE-FLEIINEKLKL----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 135 ledVGLNRDHANRYPHE-FSGGQRQRIGIARALALDPEFIIADEPISALDVS---VQAQVVNLMKRLQKekglTYLFIAH 210
Cdd:CHL00131 137 ---VGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDalkIIAEGINKLMTSEN----SIILITH 209
|
250 260 270
....*....|....*....|....*....|...
gi 2570312733 211 DLSMVKQIS-DRIGVMYLGHLVEqTASRELYKK 242
Cdd:CHL00131 210 YQRLLDYIKpDYVHVMQNGKIIK-TGDAELAKE 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-231 |
1.96e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHfhlgkgatlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHeLKG--- 80
Cdd:COG1129 254 EVVLEVEGLSVG---------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRSprd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 --KDKFAYY---RQMQMIFQDpyaslnpRS-------TVLEIISepmevHGMYKNKQGRTEKVHQLLEDVGLNRDHANRY 148
Cdd:COG1129 324 aiRAGIAYVpedRKGEGLVLD-------LSirenitlASLDRLS-----RGGLLDRRRERALAEEYIKRLRIKTPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 149 PHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLG 228
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREG 470
|
...
gi 2570312733 229 HLV 231
Cdd:COG1129 471 RIV 473
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-240 |
6.48e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgKDKFAYYRQMQMIFQDPyaslNPRSTVL 108
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQDP----EQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIISEpmeVHGMYKNKQGRTEKVHQLLEDvGLNRDHANRYPHE----FSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:PRK13638 94 DIDSD---IAFSLRNLGVPEAEITRRVDE-ALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 185 SVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-213 |
7.11e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 82.98 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNL---KKHFHLGKGATLkaVDGISFTVKKGETYGIVGESGCGKST-----AGRTILGlydQTEGEVLFNGKNIHel 78
Cdd:cd03213 4 LSFRNLtvtVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTllnalAGRRTGL---GVSGEVLINGRPLD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 79 kgkdKFAYYRQMQMIFQDPYasLNPRSTVLEIIsepmevhgMYknkqgrTEKVHQLledvglnrdhanryphefSGGQRQ 158
Cdd:cd03213 77 ----KRSFRKIIGYVPQDDI--LHPTLTVRETL--------MF------AAKLRGL------------------SGGERK 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLS 213
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPS 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-232 |
1.21e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFA- 85
Cdd:PRK11288 5 LSFDGIGKTF-----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 86 ----YYRQMQMIfqdpyaslnPRSTVLEII---SEPmEVHGMYKNKQGRTEkVHQLLEDVGLNRDHANRYPHeFSGGQRQ 158
Cdd:PRK11288 80 gvaiIYQELHLV---------PEMTVAENLylgQLP-HKGGIVNRRLLNYE-AREQLEHLGVDIDPDTPLKY-LSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-239 |
3.95e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlgKGAtlKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHEL----KGK 81
Cdd:PRK10895 3 TLTAKNLAKAY---KGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhaRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQMQMIFQdpyaslnpRSTVLEIISEPMEVHGMYKNKQgRTEKVHQLLEDVGLN--RDHANRyphEFSGGQRQR 159
Cdd:PRK10895 78 RGIGYLPQEASIFR--------RLSVYDNLMAVLQIRDDLSAEQ-REDRANELMEEFHIEhlRDSMGQ---SLSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEPISALDvsvQAQVVNLMKRLQ--KEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASR 237
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
..
gi 2570312733 238 EL 239
Cdd:PRK10895 223 EI 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-239 |
4.05e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 3 VENLLEVRNLKKHFHLGKGatLKAVDgisFTVKKGETYGIVGESGCGKSTAGRTILGLY--DQTEG---EVLFNGKNIHE 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiELLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 78 LKGKDKFAYYRQMQMIFQDpyASLNPRSTVLEII------SEPMEVHGMYKNKQGRTEKVHQLLEDVGLNRdHANRYPHE 151
Cdd:PRK09984 76 RLARDIRKSRANTGYIFQQ--FNLVNRLSVLENVligalgSTPFWRTCFSWFTREQKQRALQALTRVGMVH-FAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
....*...
gi 2570312733 232 EQTASREL 239
Cdd:PRK09984 233 YDGSSQQF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-242 |
4.25e-18 |
|
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: 84.85 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgKGatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGL--YDQTEGEVLFN------------- 71
Cdd:TIGR03269 1 IEVKNLTKKF---DG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 72 ---GKNIHELKG--------------KDKFAYYRQMQMIFQDPYAsLNPRSTVLEIISEPMEVHGmYKNKQGrTEKVHQL 134
Cdd:TIGR03269 76 skvGEPCPVCGGtlepeevdfwnlsdKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIG-YEGKEA-VGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 135 LEDVGLnrdhANRYPH---EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHD 211
Cdd:TIGR03269 153 IEMVQL----SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|.
gi 2570312733 212 LSMVKQISDRIGVMYLGHLVEQTASRELYKK 242
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-232 |
7.56e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFHlgkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLY--DQTEGEVLFNG-----KNIH-- 76
Cdd:NF040905 1 ILEMRGITKTFP-----GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphGSYEGEILFDGevcrfKDIRds 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 77 ELKGkdkfayyrqMQMIFQD----PYASL-------NPRSTvLEIISEPmEVHGmyknkqgRTEkvhQLLEDVGLNRDHA 145
Cdd:NF040905 76 EALG---------IVIIHQElaliPYLSIaeniflgNERAK-RGVIDWN-ETNR-------RAR---ELLAKVGLDESPD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 146 NRYPHeFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:NF040905 135 TLVTD-IGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVL 212
|
....*..
gi 2570312733 226 YLGHLVE 232
Cdd:NF040905 213 RDGRTIE 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-229 |
1.04e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhelKGKDKFAYYRqMQMIFQdpYASLNPRST 106
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARLARAR-IGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VleiiSEPMEVHGMYKNKQGRT--EKVHQLLEDVGLNRdHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:PRK13536 131 V----RENLLVFGRYFGMSTREieAVIPSLLEFARLES-KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2570312733 185 SVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQISDRIGVMYLGH 229
Cdd:PRK13536 206 HARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-222 |
2.74e-17 |
|
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: 77.49 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHlgkGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngknihELKGKDKFAY 86
Cdd:cd03221 1 IELENLSKTYG---GKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMqmifqdpyaslnprstvleiisepmevhgmyknkqgrtekvhqlledvglnrdhanryphefSGGQRQRIGIARAL 166
Cdd:cd03221 68 FEQL--------------------------------------------------------------SGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLmkrLQKEKGlTYLFIAHDLSMVKQISDRI 222
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEA---LKEYPG-TVILVSHDRYFLDQVATKI 137
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-196 |
3.08e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 2 TVENLLEVRNLKKHFHlgkgatlkavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGK 81
Cdd:PRK13539 4 EGEDLACVRGGRVLFS-----------GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQmqmifQDPyasLNPRSTVLEIISEPMEVHGmyknkqGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIG 161
Cdd:PRK13539 73 EACHYLGH-----RNA---MKPALTVAENLEFWAAFLG------GEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVA 137
|
170 180 190
....*....|....*....|....*....|....*
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKR 196
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-222 |
5.91e-17 |
|
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: 77.92 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGkdkfAYYRQMQMIFQDPyaSLNPRSTVL 108
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD----SIARGLLYLGHAP--GIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIISEPMEVHGmyknkqgrTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQA 188
Cdd:cd03231 92 ENLRFWHADHS--------DEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....
gi 2570312733 189 QVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRI 222
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-211 |
7.29e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 28 DGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNgKNIhelkgkdKFAYYRQmqmifqDPYasLNPRSTV 107
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGL-------RIGYLPQ------EPP--LDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 108 LEI-----------------ISEPMEVHGMYKNKQGRTE-------------KVHQLLEDVGLNRDHANRYPHEFSGGQR 157
Cdd:COG0488 79 LDTvldgdaelraleaeleeLEAKLAEPDEDLERLAELQeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDV-SVQAqvvnLMKRLQKEKGlTYLFIAHD 211
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLeSIEW----LEEFLKNYPG-TVLVVSHD 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-194 |
1.58e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.77 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 28 DGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGkdkfAYYRqmQMIFQDPYASLNPRSTV 107
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----EYHQ--DLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 108 LEIISEPMEVHGMYknkqgRTEKVHQLLEDVGL-NRDHAnryP-HEFSGGQRQRIGIARaLAL-DPEFIIADEPISALDV 184
Cdd:PRK13538 92 LENLRFYQRLHGPG-----DDEALWEALAQVGLaGFEDV---PvRQLSAGQQRRVALAR-LWLtRAPLWILDEPFTAIDK 162
|
170
....*....|
gi 2570312733 185 SVQAQVVNLM 194
Cdd:PRK13538 163 QGVARLEALL 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-210 |
1.86e-16 |
|
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: 75.65 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKkhFHLGKGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngkNIHElkgkdkfay 86
Cdd:cd03223 1 IELENLS--LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPE--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yrQMQMIF--QDPYAslnPRSTVLEIISepmevhgmyknkqgrtekvhqlledvglnrdhanrYP--HEFSGGQRQRIGI 162
Cdd:cd03223 63 --GEDLLFlpQRPYL---PLGTLREQLI-----------------------------------YPwdDVLSGGEQQRLAF 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2570312733 163 ARALALDPEFIIADEPISALDVSVQAQVVNLMkrlqKEKGLTYLFIAH 210
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-220 |
2.33e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAYYRQMQMIfqdpyaslnprS 105
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEV-----------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 TVLEIISEPMEVHGMY-------KNKQGRTEKVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEP 178
Cdd:PRK15056 91 WSFPVLVEDVVMMGRYghmgwlrRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2570312733 179 ISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISD 220
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-238 |
2.80e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQtEGEVLFNGKNIHELKGKD---KFAYYRQMQM------IFQdp 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAElarHRAYLSQQQSppfampVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 YASLN-PRSTVLEIIsepmevhgmyknkqgrTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL-----ALDPE 171
Cdd:COG4138 89 YLALHqPAGASSEAV----------------EQLLAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 172 --FIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRE 238
Cdd:COG4138 152 gqLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-224 |
3.10e-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: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 23 TLKAVDGisfTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGknihelkgkDKFAYYRQmqmifqdpYASLN 102
Cdd:cd03237 14 TLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL---------DTVSYKPQ--------YIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 103 PRSTVLEIISEpmEVHGMYKNKQGRTE-----KVHQLLEdvglnrdhanRYPHEFSGGQRQRIGIARALALDPEFIIADE 177
Cdd:cd03237 74 YEGTVRDLLSS--ITKDFYTHPYFKTEiakplQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2570312733 178 PISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGV 224
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-230 |
1.78e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKkhfhlGKGatlkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAY 86
Cdd:PRK10762 258 LKVDNLS-----GPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 ---YrqmqmIFQDPYASlnprSTVLEI-ISEPMEVHGM----YKNKQGRTEKVHQLLED-VGL------NRDHANRyphE 151
Cdd:PRK10762 328 givY-----ISEDRKRD----GLVLGMsVKENMSLTALryfsRAGGSLKHADEQQAVSDfIRLfniktpSMEQAIG---L 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-238 |
2.11e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHfhlgkgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNI---HELKG 80
Cdd:PRK09700 263 ETVFEVRNVTSR-------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDK--------------FAYYRQMQMIFQDPYASLNPRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGlnrdhan 146
Cdd:PRK09700 336 VKKgmayitesrrdngfFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNIT------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 147 ryphEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:PRK09700 409 ----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFC 483
|
250
....*....|..
gi 2570312733 227 LGHLVEQTASRE 238
Cdd:PRK09700 484 EGRLTQILTNRD 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-224 |
3.04e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 2 TVENLLEVRNLKKHFhlgKGATLKAVDGisfTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFngknihelkgK 81
Cdd:PRK13409 336 ERETLVEYPDLTKKL---GDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP----------E 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQmqmifqdpYASLNPRSTVLEIISEpmeVHGMYKNKQGRTEKVHQLledvGLNRDHaNRYPHEFSGGQRQRIG 161
Cdd:PRK13409 400 LKISYKPQ--------YIKPDYDGTVEDLLRS---ITDDLGSSYYKSEIIKPL----QLERLL-DKNVKDLSGGELQRVA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGV 224
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-239 |
4.26e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.36 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNI-----HELKgkdkfayyRQMQMIFQDPY----- 98
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgayglRELR--------RQFSMIPQDPVlfdgt 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 --ASLNPrstVLEIISE----PMEVHGMYKNKQGRTEKVHQLLEDVGLNrdhanrypheFSGGQRQRIGIARA-LALDPE 171
Cdd:PTZ00243 1400 vrQNVDP---FLEASSAevwaALELVGLRERVASESEGIDSRVLEGGSN----------YSVGQRQLMCMARAlLKKGSG 1466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570312733 172 FIIADEPIS----ALDVSVQAQVVNLMkrlqkeKGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVEQTASREL 239
Cdd:PTZ00243 1467 FILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-230 |
5.19e-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: 75.63 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKgaTLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-QTEGEVLFNGKNIHELKGKD 82
Cdd:TIGR02633 255 DVILEARNLTCWDVINP--HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYY-------RQMQMIFQDPYASLNPRSTVLEIISEPMEVhgmykNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGG 155
Cdd:TIGR02633 333 AIRAGiamvpedRKRHGIVPILGVGKNITLSVLKSFCFKMRI-----DAAAELQIIGSAIQRLKVKTASPFLPIGRLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 156 QRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-239 |
5.23e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgkdk 83
Cdd:PRK10762 2 QALLQLKGIDKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQ-----MIFQDpyasLN--PRSTVLEIISEPMEvhgmYKNKQGRTE--KVHQ----LLEDVGLNRdHANRYPH 150
Cdd:PRK10762 70 FNGPKSSQeagigIIHQE----LNliPQLTIAENIFLGRE----FVNRFGRIDwkKMYAeadkLLARLNLRF-SSDKLVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 151 EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
....*....
gi 2570312733 231 VEQTASREL 239
Cdd:PRK10762 220 IAEREVADL 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-224 |
5.37e-15 |
|
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: 75.59 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 2 TVENLLEVRNLKKHFhlgKGATLKAVDGisfTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngknihelKGK 81
Cdd:COG1245 337 EEETLVEYPDLTKSY---GGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQmqmifqdpYASLNPRSTVLEI----ISEPMEVHgMYKNKQGRTEKVHQLLEdvglnrdhanRYPHEFSGGQR 157
Cdd:COG1245 401 LKISYKPQ--------YISPDYDGTVEEFlrsaNTDDFGSS-YYKTEIIKPLGLEKLLD----------KNVKDLSGGEL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 158 QRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGV 224
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-222 |
6.22e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngknihELKGKDKFAYYRQMqmifqdpyaSLNPRS 105
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGARVAYVPQR---------SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 ---TVLEIISEPMEVHGMYKNKQGRTEK--VHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPIS 180
Cdd:NF040873 70 lplTVRDLVAMGRWARRGLWRRLTRDDRaaVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2570312733 181 ALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRI 222
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-210 |
7.59e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 24 LKAVDGISftvKKGETYGIVGESGCGKST-----AGRTILGLydQTEGEVLFNGKNIHELKGKDKFAYYRQMQMIFqdpy 98
Cdd:TIGR00955 41 LKNVSGVA---KPGELLAVMGSSGAGKTTlmnalAFRSPKGV--KGSGSVLLNGMPIDAKEMRAISAYVQQDDLFI---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 aslnPRSTVLE--IISEPMEVHGMYKNKQgRTEKVHQLLEDVGLnRDHAN------RYPHEFSGGQRQRIGIARALALDP 170
Cdd:TIGR00955 112 ----PTLTVREhlMFQAHLRMPRRVTKKE-KRERVDEVLQALGL-RKCANtrigvpGRVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2570312733 171 EFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAH 210
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-210 |
1.00e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 8 EVRNLKKHFHLGKGATLKAV-DGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGevlfngknihelKGKDKFay 86
Cdd:COG2401 26 RVAIVLEAFGVELRVVERYVlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------------AGCVDV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 yrqmqmifqdPYASLNPRSTVLEIISepmevhgmyknKQGRTEKVHQLLEDVGLNrDHAN--RYPHEFSGGQRQRIGIAR 164
Cdd:COG2401 92 ----------PDNQFGREASLIDAIG-----------RKGDFKDAVELLNAVGLS-DAVLwlRRFKELSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2570312733 165 ALALDPEFIIADEPISALDVSVqAQVVNL-MKRLQKEKGLTYLFIAH 210
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-225 |
1.23e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 24 LKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfAYYRQMQMIFQDpyASLNP 103
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQE--LNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 104 RSTVLEII---SEPMEvhGMYKNKQGRTEKVHQLLEDVGLNRDHANRYPhEFSGGQRQRIGIARALALDPEFIIADEPIS 180
Cdd:PRK10982 87 QRSVMDNMwlgRYPTK--GMFVDQDKMYRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2570312733 181 ALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-212 |
1.68e-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: 71.59 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 21 GATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDKFAYYRqmqmiFQDPYAS 100
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNR-----YSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 101 LNP---RSTVLEIISepmevHGMYKNKQgrteKVHQLLEDVGLNRDhANRYPH-----------EFSGGQRQRIGIARAL 166
Cdd:cd03290 86 QKPwllNATVEENIT-----FGSPFNKQ----RYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVN--LMKRLQKEKgLTYLFIAHDL 212
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
42-225 |
2.35e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 42 IVGESGCGKSTAGRTILGLYDQTEGEVLFNG-------KNIHELKGKDKFAYyrqmqmIFQDpyASLNPRSTV---LEii 111
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKRRIGY------VFQD--ARLFPHYKVrgnLR-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 112 sepmevHGMYKNKQGRTEKVHQLLedvGLnRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVV 191
Cdd:PRK11144 99 ------YGMAKSMVAQFDKIVALL---GI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....
gi 2570312733 192 NLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-231 |
3.02e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLKKHFhlGKgatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKG----K 81
Cdd:PRK11614 5 MLSFDKVSAHY--GK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 DKFAYYRQMQMIFQdpyaslnpRSTVleiiSEPMEVHGMYKNK---QGRTEKVHQLLEdvglnRDHANRYPHE--FSGGQ 156
Cdd:PRK11614 80 EAVAIVPEGRRVFS--------RMTV----EENLAMGGFFAERdqfQERIKWVYELFP-----RLHERRIQRAgtMSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLV 231
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-249 |
9.24e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.85 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 16 FHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngknihELKGKDKFAYYRqmqmifq 95
Cdd:PRK13545 29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--------DIKGSAALIAIS------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 96 dpyASLNPRSTVLEIIsepmEVHG--MYKNKQGRTEKVHQLLE--DVGlnrDHANRYPHEFSGGQRQRIGIARALALDPE 171
Cdd:PRK13545 94 ---SGLNGQLTGIENI----ELKGlmMGLTKEKIKEIIPEIIEfaDIG---KFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 172 FIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL---YKKPLHPYT 248
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVvdhYDEFLKKYN 242
|
.
gi 2570312733 249 Q 249
Cdd:PRK13545 243 Q 243
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-242 |
2.24e-13 |
|
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: 71.13 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihelkgkdkFAYYRQMQMIFQDpyaSLnpRST 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------VAYVPQQAWIQND---SL--REN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VLeiISEPMEvhgmyKNKQGRTEKVHQLLEDV----GLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISAL 182
Cdd:TIGR00957 719 IL--FGKALN-----EKYYQQVLEACALLPDLeilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570312733 183 DVSVQAQVV-NLMKRLQKEKGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVEQTASRELYKK 242
Cdd:TIGR00957 792 DAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-226 |
8.09e-13 |
|
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: 67.39 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 33 TVKKGETYGIVGESGCGKSTAGRTI-------LGLYDQTEG--EVL--FNGKNIHE----LKGKDkfayyrqMQMIFQDP 97
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILagklkpnLGKFDDPPDwdEILdeFRGSELQNyftkLLEGD-------VKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 YASLNPRS---TVLEIISEpmevhgmyKNKQGRTEKVHQLLEDVGLnrdhANRYPHEFSGGQRQRIGIARALALDPEFII 174
Cdd:cd03236 95 YVDLIPKAvkgKVGELLKK--------KDERGKLDELVDQLELRHV----LDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2570312733 175 ADEPISALDVSVQAQVVNLMKRLQKEKGlTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-239 |
1.23e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.59 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELkgkdKFAYYRQ-MQMIFQDPY---ASLNPRS 105
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL----SHSVLRQgVAMVQQDPVvlaDTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 106 TVLEIISEpmevhgmyknkqgrtEKVHQLLEDVGLNrDHANRYP-----------HEFSGGQRQRIGIARALALDPEFII 174
Cdd:PRK10790 436 TLGRDISE---------------EQVWQALETVQLA-ELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 175 ADEPISALDvSVQAQVVNLMKRLQKEKgLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASREL 239
Cdd:PRK10790 500 LDEATANID-SGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-232 |
2.33e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 6 LLEVRNLkkHFHLGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGL--YDQTEGEVLFNGKNIHELKGKDK 83
Cdd:PRK09580 1 MLSIKDL--HVSVEDKAILR---GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAyyRQMQMIFQDP---------------------YASLNP--RSTVLEIISEPMEVHGMYKNKQGRTEKVHqlledvgl 140
Cdd:PRK09580 76 AG--EGIFMAFQYPveipgvsnqfflqtalnavrsYRGQEPldRFDFQDLMEEKIALLKMPEDLLTRSVNVG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 141 nrdhanrypheFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKgLTYLFIAHDLSMVKQIS- 219
Cdd:PRK09580 146 -----------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYQRILDYIKp 213
|
250
....*....|...
gi 2570312733 220 DRIGVMYLGHLVE 232
Cdd:PRK09580 214 DYVHVLYQGRIVK 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-230 |
2.70e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFHLGKGatLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-QTEGEVLFNGKNIHELKGKD 82
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPH--IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 83 KFAYyrQMQMIFQD----------------PYASLNpRSTVLEIISEPMEVHGMYKNKQGRTEKVHQLLEDVGlnrdhan 146
Cdd:PRK13549 335 AIAQ--GIAMVPEDrkrdgivpvmgvgkniTLAALD-RFTGGSRIDDAAELKTILESIQRLKVKTASPELAIA------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 147 ryphEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:PRK13549 405 ----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMH 479
|
....
gi 2570312733 227 LGHL 230
Cdd:PRK13549 480 EGKL 483
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-216 |
3.06e-12 |
|
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: 67.47 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDqtegevLFNGKNIHELKGKdkfayyrqMQMIFQDPYASLnprST 106
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP------VYGGRLTKPAKGK--------LFYVPQRPYMTL---GT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 107 VLEIISEPMEVHGMyKNKQGRTEKVHQLLEDVGLNR--------DHANRYPHEFSGGQRQRIGIARALALDPEFIIADEP 178
Cdd:TIGR00954 531 LRDQIIYPDSSEDM-KRRGLSDKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|....*...
gi 2570312733 179 ISALDVSVQAQvvnlMKRLQKEKGLTYLFIAHDLSMVK 216
Cdd:TIGR00954 610 TSAVSVDVEGY----MYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-238 |
3.09e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQtEGEVLFNGKNIHELKGKD---KFAYYRQMQM------IFQdpYAS 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElarHRAYLSQQQTppfampVFQ--YLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 101 LnprstvleiiSEPMEVHgmyknKQGRTEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARAL-----ALDPE--FI 173
Cdd:PRK03695 92 L----------HQPDKTR-----TEAVASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 174 IADEPISALDVSVQAQVVNLMKRLQkEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRE 238
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-230 |
3.19e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 9 VRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIH-ELKG-KDKFAY 86
Cdd:TIGR01257 931 VKNLVKIF---EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtNLDAvRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQdpyaslnpRSTVLEIISepmevhgMYKNKQGRTEKVHQL-----LEDVGLNRDHaNRYPHEFSGGQRQRIG 161
Cdd:TIGR01257 1008 CPQHNILFH--------HLTVAEHIL-------FYAQLKGRSWEEAQLemeamLEDTGLHHKR-NEEAQDLSGGMQRKLS 1071
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMkrLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHL 230
Cdd:TIGR01257 1072 VAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
7-234 |
5.25e-12 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 66.52 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfay 86
Cdd:TIGR01194 338 IELKDVHMNPKAPEGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDD---- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQM-QMIFQDPYaslnprstVLEIISEPMEvhgmykNKQGRTEKVHQLLEDVGLN-----RDHANRYPHEFSGGQRQRI 160
Cdd:TIGR01194 414 YRDLfSAIFADFH--------LFDDLIGPDE------GEHASLDNAQQYLQRLEIAdkvkiEDGGFSTTTALSTGQQKRL 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDlSMVKQISDRIGVMYLGHLVEQT 234
Cdd:TIGR01194 480 ALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHD-DQYFELADQIIKLAAGCIVKDT 552
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-239 |
5.33e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYYRQMQMIFQDPYASlnprSTVL 108
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQSPVLF----SGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIISEPMEVHgmykNKQGRTEKVHQL-LEDV------GLNRDhANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISA 181
Cdd:PLN03232 1327 RFNIDPFSEH----NDADLWEALERAhIKDVidrnpfGLDAE-VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 182 LDVSVQAqvvnLMKRLQKE--KGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASREL 239
Cdd:PLN03232 1402 VDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
30-222 |
1.77e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVlfngknihELKGKDKFAYYRQMqmIFQDPyaslnprstvle 109
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRIGYVPQK--LYLDT------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 110 iiSEPMEVHGMYKNKQG-RTEKVHQLLEDVglNRDHANRYP-HEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQ 187
Cdd:PRK09544 81 --TLPLTVNRFLRLRPGtKKEDILPALKRV--QAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2570312733 188 AQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRI 222
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-231 |
2.72e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 15 HFHLGKGA-TLKAVDGISFTVKKGETYGIVGESGCGKST---AGRTILGLYDQTEGEVLFNGKNIHElkgkdkFAYYRQM 90
Cdd:cd03233 10 SFTTGKGRsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKE------FAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 91 QMIFQDPYASLNPRSTVleiisepmevhgmyknkqgrtekvHQLLEDVGLNRdhANRYPHEFSGGQRQRIGIARALALDP 170
Cdd:cd03233 84 EIIYVSEEDVHFPTLTV------------------------RETLDFALRCK--GNEFVRGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 171 EFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIahdlsmVKQIS-------DRIGVMYLGHLV 231
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS------LYQASdeiydlfDKVLVLYEGRQI 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-239 |
3.07e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGlyDQTE----------GEVLFNGKNIHELKGKdKFAYYRQMQMIFQD 96
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAP-RLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 97 PYASLNPRSTVLeiisepmevHGMYKN--KQGRTEKVHQLLEDVGLNRDHAN----RYPHEFSGGQRQRIGIARALA--- 167
Cdd:PRK13547 94 PAFAFSAREIVL---------LGRYPHarRAGALTHRDGEIAWQALALAGATalvgRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 168 ------LDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASREL 239
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-224 |
4.02e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYD-QTEGEVLFNG----------------------KNIHELKGK----- 81
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNehtndmtneqdyqgdeeqnvgmKNVNEFSLTkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 82 -DKFAYYRQMQMIFQDPYA----SLNPRSTVLEIIS-EPMEVH-GMYKN-KQGRTEKVhqlLEDVGL------------- 140
Cdd:PTZ00265 1267 gEDSTVFKNSGKILLDGVDicdyNLKDLRNLFSIVSqEPMLFNmSIYENiKFGKEDAT---REDVKRackfaaidefies 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 141 --NRDHANRYPH--EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEKGLTYLFIAHDLSMVK 216
Cdd:PTZ00265 1344 lpNKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
....*...
gi 2570312733 217 QiSDRIGV 224
Cdd:PTZ00265 1424 R-SDKIVV 1430
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-226 |
4.47e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 33 TVKKGETYGIVGESGCGKSTAGRtILGlydqteGEVLFN-GKNIHELKGKDKFAYYR--QMQMIFQDPY-----ASLNPR 104
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVK-ILS------GELIPNlGDYEEEPSWDEVLKRFRgtELQNYFKKLYngeikVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 stVLEIIsePMEVHGmyknkqgrteKVHQLLEDVG-----------LNRDHA-NRYPHEFSGGQRQRIGIARALALDPEF 172
Cdd:PRK13409 168 --YVDLI--PKVFKG----------KVRELLKKVDergkldevverLGLENIlDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 173 IIADEPISALDVSVQAQVVNLMKRLQKEKglTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-183 |
4.73e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 26 AVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEV-LFNgkniHELKGKD------------KFAYY----- 87
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFG----QPVDAGDiatrrrvgymsqAFSLYgeltv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQM----IFQDPYASLNPRstvleiisepmevhgmyknkqgrtekVHQLLEDVGLnRDHANRYPHEFSGGQRQRIGIA 163
Cdd:NF033858 357 RQNLElharLFHLPAAEIAAR--------------------------VAEMLERFDL-ADVADALPDSLPLGIRQRLSLA 409
|
170 180
....*....|....*....|
gi 2570312733 164 RALALDPEFIIADEPISALD 183
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVD 429
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-177 |
6.24e-11 |
|
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: 63.28 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElkgkDKFAY 86
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA----DNREA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQM-QMIFQDPY---ASLNPRSTVLEiisepmevhgmyknkqgrtEKVHQLLEDVGLN-----RDHA--NRyphEFSGG 155
Cdd:COG4615 404 YRQLfSAVFSDFHlfdRLLGLDGEADP-------------------ARARELLERLELDhkvsvEDGRfsTT---DLSQG 461
|
170 180
....*....|....*....|..
gi 2570312733 156 QRQRIGIARALALDPEFIIADE 177
Cdd:COG4615 462 QRKRLALLVALLEDRPILVFDE 483
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-197 |
7.69e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.33 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 19 GKGATLKAVDGISFTVKKGETYGIVGESGCGKST-----AGRTILGLydqTEGEVLFNGKnihelKGKDKFA----YYRQ 89
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGV---ITGEILINGR-----PLDKNFQrstgYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 90 MQMifqdpyasLNPRSTVLEIIsepmevhgmyknkqgrteKVHQLLEDVGLnrdhanryphefsgGQRQRIGIARALALD 169
Cdd:cd03232 87 QDV--------HSPNLTVREAL------------------RFSALLRGLSV--------------EQRKRLTIGVELAAK 126
|
170 180
....*....|....*....|....*...
gi 2570312733 170 PEFIIADEPISALDVSVQAQVVNLMKRL 197
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-216 |
1.04e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHelkgKDKFAYyrQMQMIFQDPYASLNPRSTVLE 109
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTY--QKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 110 iiSEPMEVHGMYKNKQgrtekVHQLLEDVGLnrDHANRYP-HEFSGGQRQRIGIARALALDPEFIIADEPISALDvsvQA 188
Cdd:PRK13540 94 --NCLYDIHFSPGAVG-----ITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---EL 161
|
170 180 190
....*....|....*....|....*....|.
gi 2570312733 189 QVVNLMKRLQ--KEKGLTYLFIAH-DLSMVK 216
Cdd:PRK13540 162 SLLTIITKIQehRAKGGAVLLTSHqDLPLNK 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-226 |
1.87e-10 |
|
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: 61.72 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 33 TVKKGETYGIVGESGCGKSTAGRtILGlydqteGEVLFN-GKNIHELKGKDKFAYYR--QMQMIFQDPY-----ASLNPR 104
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALK-ILS------GELKPNlGDYDEEPSWDEVLKRFRgtELQDYFKKLAngeikVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 105 StVLEIisePMEVHGmyknkqgrteKVHQLLEDVG-----------LNRDHA-NRYPHEFSGGQRQRIGIARALALDPEF 172
Cdd:COG1245 168 Y-VDLI---PKVFKG----------TVRELLEKVDergkldelaekLGLENIlDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 173 IIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-232 |
1.92e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.60 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 20 KGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGknihelkgkdkfayyrQMQMIFQDpyA 99
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 100 SLNPRSTVLEIISEPMEVHGmYKNKQGRtEKVHQLLEDVGLNrDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPI 179
Cdd:PRK13546 95 GLSGQLTGIENIEFKMLCMG-FKRKEIK-AMTPKIIEFSELG-EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 180 SALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVE 232
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-225 |
2.57e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKkhfhlgkGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDK 83
Cdd:PRK10982 248 EVILEVRNLT-------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 ----FAYY---RQMQMIFQdpYASLNPRSTVLEIISepmevhgmYKNKQG-----RTEKVHQLLEDvGLNRDHANRYPH- 150
Cdd:PRK10982 321 inhgFALVteeRRSTGIYA--YLDIGFNSLISNIRN--------YKNKVGlldnsRMKSDTQWVID-SMRVKTPGHRTQi 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 151 -EFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRL-QKEKGLtyLFIAHDLSMVKQISDRIGVM 225
Cdd:PRK10982 390 gSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVM 464
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-225 |
3.11e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKkhfhlgkGATLKAvdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDk 83
Cdd:PRK11288 255 EVRLRLDGLK-------GPGLRE--PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 fAYYRQMQMIFQDPYA-SLNPRSTVLEIISEPMEVH----GMYKNKQGRTEKVHQLLEDVGLNRDHANRYPHEFSGGQRQ 158
Cdd:PRK11288 325 -AIRAGIMLCPEDRKAeGIIPVHSVADNINISARRHhlraGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQ 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570312733 159 RIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQISDRIGVM 225
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-242 |
6.35e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLkkHFHLGKGATlkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHElkgKDKFAY 86
Cdd:PRK10522 323 LELRNV--TFAYQDNGF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQMIFQDPY---ASLNPrstvleiisepmevhgmyKNKQGRTEKVHQLLEDVGLN---RDHANRYPH-EFSGGQRQR 159
Cdd:PRK10522 396 RKLFSAVFTDFHlfdQLLGP------------------EGKPANPALVEKWLERLKMAhklELEDGRISNlKLSKGQKKR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 160 IGIARALALDPEFIIADEpiSALDVSVQAQVV---NLMKRLQkEKGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVE---- 232
Cdd:PRK10522 458 LALLLALAEERDILLLDE--WAADQDPHFRREfyqVLLPLLQ-EMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSEltge 533
|
250
....*....|..
gi 2570312733 233 --QTASRELYKK 242
Cdd:PRK10522 534 erDAASRDAVAR 545
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-239 |
9.40e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 29 GISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKGKDkfaYYRQMQMIFQDPYASlnprSTVL 108
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKVLGIIPQAPVLF----SGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EIISEPMEVHG---MYKNkqgrTEKVHqlLEDV------GLNRDHANRyPHEFSGGQRQRIGIARALALDPEFIIADEPI 179
Cdd:PLN03130 1330 RFNLDPFNEHNdadLWES----LERAH--LKDVirrnslGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570312733 180 SALDVSVQAQVvnlMKRLQKE-KGLTYLFIAHDLSMVKQiSDRIGVMYLGHLVEQTASREL 239
Cdd:PLN03130 1403 AAVDVRTDALI---QKTIREEfKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-226 |
1.80e-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: 56.43 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 34 VKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhelkgkdkfAYYRQmqmifqdpYASLnprstvleiise 113
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP---------VYKPQ--------YIDL------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 114 pmevhgmyknkqgrtekvhqlledvglnrdhanryphefSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNL 193
Cdd:cd03222 73 ---------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|...
gi 2570312733 194 MKRLQKEKGLTYLFIAHDLSMVKQISDRIGVMY 226
Cdd:cd03222 114 IRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-271 |
1.87e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 16 FHLGKGATLKaVDgiSFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIHELKgkdkfayYRQMQMIFQ 95
Cdd:PRK10938 11 FRLSDTKTLQ-LP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-------FEQLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 96 DPYASLNPR----------STVLEIISEpmEVHgmyknkqgRTEKVHQLLEDVG----LNRdhanRYPHeFSGGQRQRIG 161
Cdd:PRK10938 81 DEWQRNNTDmlspgeddtgRTTAEIIQD--EVK--------DPARCEQLAQQFGitalLDR----RFKY-LSTGETRKTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 162 IARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELYK 241
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2570312733 242 KPLhpYTQAL----LTAIPIPDPDVEDKRE-------RIIL 271
Cdd:PRK10938 225 QAL--VAQLAhseqLEGVQLPEPDEPSARHalpanepRIVL 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-239 |
3.36e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNI-----HELKGKdkfayyrqMQMIFQDPY------ 98
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIakiglHDLRFK--------ITIIPQDPVlfsgsl 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 -ASLNPRSTVL-EIISEPMEVHGMYKNKQGRTEKVHQLLEDVGLNrdhanrypheFSGGQRQRIGIARALALDPEFIIAD 176
Cdd:TIGR00957 1377 rMNLDPFSQYSdEEVWWALELAHLKTFVSALPDKLDHECAEGGEN----------LSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 177 EPISALDVSVQaqvvNLMK---RLQKEKgLTYLFIAHDLSMVKQISdRIGVMYLGHLVEQTASREL 239
Cdd:TIGR00957 1447 EATAAVDLETD----NLIQstiRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-228 |
1.05e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKST-----AGRtILGlyDQTEGEVLFNGKNIHElkgkdkfAYYRQMQMIFQDP--YA 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTllnalAGR-IQG--NNFTGTILANNRKPTK-------QILKRTGFVTQDDilYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 100 SLNPRSTVL--EIISEPMEVhgmykNKQGRTEKVHQLLEDVGL----NRDHANRYPHEFSGGQRQRIGIARALALDPEFI 173
Cdd:PLN03211 154 HLTVRETLVfcSLLRLPKSL-----TKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2570312733 174 IADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHD-LSMVKQISDRIGVMYLG 228
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-228 |
3.49e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFhlgKGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNIhelkgkdkf 84
Cdd:TIGR01257 1936 DILRLNELTKVY---SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------- 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 ayYRQMQMIFQDpyASLNPRSTVLEIISEPMEVHGMYKNKQG----RTEKVHQL-LEDVGLNRdHANRYPHEFSGGQRQR 159
Cdd:TIGR01257 2004 --LTNISDVHQN--MGYCPQFDAIDDLLTGREHLYLYARLRGvpaeEIEKVANWsIQSLGLSL-YADRLAGTYSGGNKRK 2078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 160 IGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLG 228
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-229 |
4.05e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihelkgkdkFAYYRQMQMIFQdpyaslnprSTVLE 109
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------ISFSPQTSWIMP---------GTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 110 IIsepmeVHGMYKNKQGRTE--KVHQLLEDVGLNRDHANRYPHE----FSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:TIGR01271 506 NI-----IFGLSYDEYRYTSviKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2570312733 184 VSVQAQVV-NLMKRLQKEKglTYLFIAHDLSMVKQiSDRIGVMYLGH 229
Cdd:TIGR01271 581 VVTEKEIFeSCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGV 624
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-241 |
5.00e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILG-LYDQTEGEVLFNGKnihelkgkdkFAYYRQMQMIFQdpyASLnpRSTVL 108
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT----------VAYVPQVSWIFN---ATV--RDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 eiISEPMEvhgmyKNKQGRTEKVHQLLEDVGL--NRDHAN--RYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:PLN03130 701 --FGSPFD-----PERYERAIDVTALQHDLDLlpGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2570312733 185 SVQAQVVNlmKRLQKE-KGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVEQTASRELYK 241
Cdd:PLN03130 774 HVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSN 828
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-222 |
5.99e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.94 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 20 KGATLKAVDGISFTVKKGETYGIVGESGCGKSTAGRTILglydQTEGEVLFNgknihelkgKDKFAYYRQmQMIFQDpya 99
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI---------SFLPKFSRN-KLIFID--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 100 SLnprstvleiisepmevhgmyknkqgrtekvhQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPE---FIIaD 176
Cdd:cd03238 67 QL-------------------------------QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtlFIL-D 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2570312733 177 EPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKQiSDRI 222
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-211 |
9.98e-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: 50.83 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 36 KGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLF-NGKNIHElkgkdkfayyrqmqmifqdpyaslnprstvleiisep 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILE------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 115 mevhgmyknkqgrtekvhqlLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQV---- 190
Cdd:smart00382 44 --------------------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllle 103
|
170 180
....*....|....*....|..
gi 2570312733 191 -VNLMKRLQKEKGLTYLFIAHD 211
Cdd:smart00382 104 eLRLLLLLKSEKNLTVILTTND 125
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-242 |
1.12e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFhlgkgATLKAVDGISFTVKKGETYGIVGESGcgkSTAGRTILGLY----DQTEGEVLFNGKNIHELKG 80
Cdd:NF000106 12 NAVEVRGLVKHF-----GEVKAVDGVDLDVREGTVLGVLGP*G---AA**RGALPAHv*gpDAGRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 81 KDKFAYYRQMQMIFQDPYASLNPrstvLEIISEPMEVHgmYKNKQGRTEkvhQLLEDVGLNrDHANRYPHEFSGGQRQRI 160
Cdd:NF000106 84 RRTIG*HRPVR*GRRESFSGREN----LYMIGR*LDLS--RKDARARAD---ELLERFSLT-EAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 161 GIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKEkGLTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
..
gi 2570312733 241 KK 242
Cdd:NF000106 233 TK 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-241 |
1.37e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTE-GEVLFNGKnihelkgkdkFAYYRQMQMIFQdpyaslnprSTVL 108
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGS----------VAYVPQVSWIFN---------ATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 109 EII-----SEPmevhgmykNKQGRTEKVHQLLEDV----GLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIADEPI 179
Cdd:PLN03232 697 ENIlfgsdFES--------ERYWRAIDVTALQHDLdllpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 180 SALDVSVQAQVVN-LMKrlQKEKGLTYLFIAHDLSMVKQIsDRIGVMYLGHLVEQTASRELYK 241
Cdd:PLN03232 769 SALDAHVAHQVFDsCMK--DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-222 |
1.39e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 27 VDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGK------NiHELKGKDKFAY---------YRQMQ 91
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvN-QETPALPQPALeyvidgdreYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 92 MIFQDPyaslNPRSTVLEIISepmeVHGMYKNKQGRT--EKVHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALD 169
Cdd:PRK10636 96 AQLHDA----NERNDGHAIAT----IHGKLDAIDAWTirSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 170 PEFIIADEPISALDVSVqaqVVNLMKRLQKEKGlTYLFIAHDLSMVKQISDRI 222
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-184 |
1.98e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKHFhlgkGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFnGKNIhelkgkdK 83
Cdd:TIGR03719 320 DKVIEAENLTKAF----GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQmifqdpyASLNPRSTVLEIISEPMEVH--GMYK----------NKQG--RTEKVHQLledvglnrdhanryp 149
Cdd:TIGR03719 387 LAYVDQSR-------DALDPNKTVWEEISGGLDIIklGKREipsrayvgrfNFKGsdQQKKVGQL--------------- 444
|
170 180 190
....*....|....*....|....*....|....*
gi 2570312733 150 hefSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:TIGR03719 445 ---SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-240 |
2.14e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 32 FTVKKGETYGIVGESGCGKST-----AGRTILG----LYDQ--------------TEGEVL-FNGKNIHELKGKDKfAYY 87
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTlmkilNGEVLLDdgriIYEQdlivarlqqdpprnVEGTVYdFVAEGIEEQAEYLK-RYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 88 RQMQMIFQDPYAS-LNPRSTVLEIIsepmEVHGMYKNKqgrtEKVHQLLEDVGLNrdhANRYPHEFSGGQRQRIGIARAL 166
Cdd:PRK11147 103 DISHLVETDPSEKnLNELAKLQEQL----DHHNLWQLE----NRINEVLAQLGLD---PDAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 167 ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKekglTYLFIAHDLSMVKQISDRIGVMYLGHLVEQTASRELY 240
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQY 241
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-191 |
3.50e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLfngknihelkGKDKFAYYRQMQMIFQdpyASLnpRSTVLE 109
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------AERSIAYVPQQAWIMN---ATV--RGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 110 IISEPMEvhgmyknKQGRTEKVHQLLEDV--------------GLNrdhanrypheFSGGQRQRIGIARALALDPEFIIA 175
Cdd:PTZ00243 744 FDEEDAA-------RLADAVRVSQLEADLaqlgggleteigekGVN----------LSGGQKARVSLARAVYANRDVYLL 806
|
170
....*....|....*.
gi 2570312733 176 DEPISALDVSVQAQVV 191
Cdd:PTZ00243 807 DDPLSALDAHVGERVV 822
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-183 |
3.86e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 28 DGISFTVKKGETYGIVGESGCGKSTAGRTILGlyDQTEGE----VLF-----NGKNIHELKgkDKFAYY-RQMQMifqDP 97
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGYsndlTLFgrrrgSGETIWDIK--KHIGYVsSSLHL---DY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 98 YASLNPRSTvleIISEPMEVHGMYKNKQGRTEK-VHQLLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFIIAD 176
Cdd:PRK10938 350 RVSTSVRNV---ILSGFFDSIGIYQAVSDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILD 426
|
....*..
gi 2570312733 177 EPISALD 183
Cdd:PRK10938 427 EPLQGLD 433
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-190 |
4.13e-07 |
|
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: 50.63 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKnihelkgkdkFAYYRQMQMIFQdpyaslnprSTVLE 109
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------ISFSSQFSWIMP---------GTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 110 IIsepmeVHGM----YKNKQgrTEKVHQLLEDVGLNRDHANRYPHE----FSGGQRQRIGIARALALDPEFIIADEPISA 181
Cdd:cd03291 117 NI-----IFGVsydeYRYKS--VVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
....*....
gi 2570312733 182 LDVSVQAQV 190
Cdd:cd03291 190 LDVFTEKEI 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-231 |
9.90e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 4 ENLLEVRNLKKH--FHLGKgatlKAVDGISFTVKKGETYGIVGESGcgkstAGRTILGL------YDQ-TEGEVLFNGKN 74
Cdd:NF040905 255 EVVFEVKNWTVYhpLHPER----KVVDDVSLNVRRGEIVGIAGLMG-----AGRTELAMsvfgrsYGRnISGTVFKDGKE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 75 IhELKG-----KDKFAYY----RQMQMIFQDP------YASLN--PRSTVLEIISEpMEVHGMYKNKQgRTeKVHQLLED 137
Cdd:NF040905 326 V-DVSTvsdaiDAGLAYVtedrKGYGLNLIDDikrnitLANLGkvSRRGVIDENEE-IKVAEEYRKKM-NI-KTPSVFQK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 138 VGlnrdhanryphEFSGGQRQRIGIARALALDPEFIIADEPISALDVSVQAQVVNLMKRLQKE-KGLtyLFIAHDLSMVK 216
Cdd:NF040905 402 VG-----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGV--IVISSELPELL 468
|
250
....*....|....*
gi 2570312733 217 QISDRIGVMYLGHLV 231
Cdd:NF040905 469 GMCDRIYVMNEGRIT 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-222 |
1.32e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 5 NLLEVRNLKKHFhlgKGATLkaVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKNihelkgkdKF 84
Cdd:PRK15064 318 NALEVENLTKGF---DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA--------NI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 85 AYYRqmqmifQDPYASLNPRSTVLEIISepmevhgmyknkQGRTEK-----VHQLLEDVGLNRDHANRYPHEFSGGQRQR 159
Cdd:PRK15064 385 GYYA------QDHAYDFENDLTLFDWMS------------QWRQEGddeqaVRGTLGRLLFSQDDIKKSVKVLSGGEKGR 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570312733 160 IGIARALALDPEFIIADEPISALDV-SVQAqvvnLMKRLQKEKGlTYLFIAHDLSMVKQISDRI 222
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMeSIES----LNMALEKYEG-TLIFVSHDREFVSSLATRI 505
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-183 |
4.34e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDqTEGEVLFNGKNIHEL---KGKDK 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLE---NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVplqKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQDPY-ASLNPrstvleiisepmevhgmykNKQGRTEKVHQLLEDVGLnRDHANRYPHE----------- 151
Cdd:cd03289 79 FGVIPQKVFIFSGTFrKNLDP-------------------YGKWSDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcv 138
|
170 180 190
....*....|....*....|....*....|..
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALD 183
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-184 |
1.61e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFhlgkGATLkAVDGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFnGKNIhelkgkdKFAY 86
Cdd:PRK11819 325 IEAENLSKSF----GDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 87 YRQMQmifqdpyASLNPRSTVLEIISEPMEVHgmyknKQGRTE-------------------KVHQLledvglnrdhanr 147
Cdd:PRK11819 392 VDQSR-------DALDPNKTVWEEISGGLDII-----KVGNREipsrayvgrfnfkggdqqkKVGVL------------- 446
|
170 180 190
....*....|....*....|....*....|....*..
gi 2570312733 148 yphefSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:PRK11819 447 -----SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-183 |
3.34e-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: 45.67 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 7 LEVRNLKKHFHLGKGATLKavdGISFTVKKGETYGIVGESGCGKSTAGRTILGLYDqTEGEVLFNG---KNIHELKGKDK 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQ---DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 84 FAYYRQMQMIFQ-------DPYASLNPRstvlEIISEPMEVhGMYKNKQGRTEKVHQLLEDVGlnrdhanrypHEFSGGQ 156
Cdd:TIGR01271 1294 FGVIPQKVFIFSgtfrknlDPYEQWSDE----EIWKVAEEV-GLKSVIEQFPDKLDFVLVDGG----------YVLSNGH 1358
|
170 180
....*....|....*....|....*..
gi 2570312733 157 RQRIGIARALALDPEFIIADEPISALD 183
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-226 |
1.16e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 1.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570312733 153 SGGQRQRIGIARALAL-----DPeFIIADEPISALDVSVQAQVVNLMKRLQKeKGLTYLFIAHDLsMVKQISDRIGVMY 226
Cdd:cd03227 79 SGGEKELSALALILALaslkpRP-LYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLP-ELAELADKLIHIK 154
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
67-216 |
1.36e-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: 42.99 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 67 EVLFNGKNIHElkgkdkfayyrqmqmifqdpyaslnprstVLEIISEpmEVHGMYKNKQGRTEKVhQLLEDVGLNRDHAN 146
Cdd:cd03271 117 EVRYKGKSIAD-----------------------------VLDMTVE--EALEFFENIPKIARKL-QTLCDVGLGYIKLG 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 147 RYPHEFSGGQRQRIGIARAL---ALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVK 216
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIK 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
152-184 |
2.18e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.18e-04
10 20 30
....*....|....*....|....*....|...
gi 2570312733 152 FSGGQRQRIGIARALALDPEFIIADEPISALDV 184
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-183 |
2.86e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.37 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 30 ISFTVKKGETYGIVGESGCGKSTAGRTILGLYDQTEGEVLFNGKniHELKGKdkfayyRQMQMIFQDPYASLNPRSTVLE 109
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGD------RSRFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570312733 110 IISEPMEVHGmYKNKQGRTEKvhqlLEDVGLNrDHANRYPHEFSGGQRQRIGIARaLALDPEFI-IADEPISALD 183
Cdd:PRK13543 102 NLHFLCGLHG-RRAKQMPGSA----LAIVGLA-GYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-222 |
6.73e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 20 KGATLKAVDGISFTVKKGETYGIVGESGCGKST-AGRTILglydqTEGEVLFngknIHELKgkdkfAYYRQMQMIFQDPY 98
Cdd:cd03270 4 RGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSlAFDTIY-----AEGQRRY----VESLS-----AYARQFLGQMDKPD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 99 -----------------ASLNPRSTVlEIISEPMEVHGMYKNKQGRTEKVHQLLeDVGLNRDHANRYPHEFSGGQRQRIG 161
Cdd:cd03270 70 vdsieglspaiaidqktTSRNPRSTV-GTVTEIYDYLRLLFARVGIRERLGFLV-DVGLGYLTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570312733 162 IARAL--ALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHDLSMVKqISDRI 222
Cdd:cd03270 148 LATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR-AADHV 208
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-217 |
7.60e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 133 QLLEDVGLNRDHANRYPHEFSGGQRQRIGIARAL---ALDPEFIIADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIA 209
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIE 889
|
....*...
gi 2570312733 210 HDLSMVKQ 217
Cdd:TIGR00630 890 HNLDVIKT 897
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-191 |
1.54e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 24 LKAVDGISFTVKKGETYGIVGESGCGKST-----AGRTILGLydqTEGEVLFNGKNihelKGKDKFA----YYRQMQMif 94
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTlmdvlAGRKTGGY---IEGDIRISGFP----KKQETFArisgYCEQNDI-- 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 95 qdpyasLNPRSTVLE--IISE----PMEVhgmykNKQGRTEKVHQLLEDVGLN--RDHANRYP--HEFSGGQRQRIGIAR 164
Cdd:PLN03140 964 ------HSPQVTVREslIYSAflrlPKEV-----SKEEKMMFVDEVMELVELDnlKDAIVGLPgvTGLSTEQRKRLTIAV 1032
|
170 180
....*....|....*....|....*..
gi 2570312733 165 ALALDPEFIIADEPISALDVSVQAQVV 191
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
68-258 |
3.29e-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: 39.23 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 68 VLFNGKNIHELKGK---DKFAYYRQMQmifqdpyasLNPRStvlEIISEPMevhgmyknKQGRTEKVhQLLEDVGLNRDH 144
Cdd:TIGR00630 423 VTVGGKSIADVSELsirEAHEFFNQLT---------LTPEE---KKIAEEV--------LKEIRERL-GFLIDVGLDYLS 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 145 ANRYPHEFSGGQRQRIGIARAL--ALDPEFIIADEPISALDVSVQAQVVNLMKRLQKeKGLTYLFIAHDLSMVKQiSDRI 222
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDEDTIRA-ADYV 559
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2570312733 223 -------GVmYLGHLVEQTASRELYKKPlHPYTQALLTA---IPIP 258
Cdd:TIGR00630 560 idigpgaGE-HGGEVVASGTPEEILANP-DSLTGQYLSGrkkIEVP 603
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-222 |
4.09e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570312733 134 LLEDVGLNRDHANRYPHEFSGGQRQRIGIARALALDPEFI--IADEPISALDVSVQAQVVNLMKRLqKEKGLTYLFIAHD 211
Cdd:PRK00635 459 ILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD 537
|
90
....*....|.
gi 2570312733 212 LSMVkQISDRI 222
Cdd:PRK00635 538 EQMI-SLADRI 547
|
|
| |
