|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-339 |
7.36e-177 |
|
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: 492.65 E-value: 7.36e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAdITGGSVEMGDVDLVTAKTKVR 99
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEPESRADSYPHQFSGGMRQRLL 179
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 260 SPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPDLHSIPDGCVYQARCPIARGICISSRPPLESVGNGRLSACHFPNEVSR 339
Cdd:COG0444 241 NPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEEAP 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-279 |
7.53e-132 |
|
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: 386.35 E-value: 7.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKTKVR 99
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEPESRADSYPHQFSGGMRQRLL 179
Cdd:COG4172 87 RRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
250 260
....*....|....*....|
gi 1993389136 260 SPRHPYTKGLLDSVPVHAVR 279
Cdd:COG4172 247 APQHPYTRKLLAAEPRGDPR 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-336 |
1.79e-121 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 352.88 E-value: 1.79e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiADITGGSVEMGDVDLVTAKTKVR 99
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEPESRADSYPHQFSGGMRQRLL 179
Cdd:PRK09473 92 NKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFY 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 260 SPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPDLHSIPDGCVYQARCPIARGICiSSRPPLESVGNGRLSACHFPNE 336
Cdd:PRK09473 252 QPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEIC-SSAPPLEEFGPGRLRACFKPVE 327
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-339 |
3.81e-115 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 336.70 E-value: 3.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVD-------LRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLV 92
Cdd:COG4608 8 LEVRDLKKHfpvrgglFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP----TSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 93 TAKTKVRRTIAAtELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPePEsRADSYPHQFSG 172
Cdd:COG4608 84 GLSGRELRPLRR-RMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PE-HADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 173 GMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 253 LVSEVFGSPRHPYTKGLLDSVPVH--AVRGEDLKsIGGTPPDLHSIPDGCVYQARCPIARGICISSRPPLESVGNGRLSA 330
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPdpERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQVA 319
|
....*....
gi 1993389136 331 CHFPNEVSR 339
Cdd:COG4608 320 CHLAEEGSG 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-252 |
2.64e-111 |
|
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: 322.92 E-value: 2.64e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP----TSGSIIFDGKDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RtIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARvEAIALMARVGIPEPESRADSYPHQFSGGMRQRLL 179
Cdd:cd03257 78 K-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEAR-KEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-334 |
6.55e-111 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 325.93 E-value: 6.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKTKVR 99
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEPESRADSYPHQFSGGMRQRLL 179
Cdd:PRK11022 84 RNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 260 SPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPDLHSIPDGCVYQARCPIARGICISSRPPLESVGnGRLSACHFP 334
Cdd:PRK11022 244 APRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA-GRQSKCHYP 317
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-275 |
7.24e-103 |
|
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: 311.84 E-value: 7.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 3 APATSAPSARPDTGSVALDVRGLTVDLRT-PSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTG 81
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----TS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 GSVEMGDVDLVTAKTKVRRTIAaTELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEpeS 161
Cdd:COG1123 320 GSILFDGKDLTKLSRRSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--D 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 162 RADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVA 241
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
250 260 270
....*....|....*....|....*....|....
gi 1993389136 242 IMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVPV 275
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPS 510
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-334 |
5.04e-93 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 280.25 E-value: 5.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKTKVR 99
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGTQLAE--PFRIHRGM---SAKQARVEAIALMARVGIPEPESRADSYPHQFSGGM 174
Cdd:COG4170 84 RKIIGREIAMIFQEPSSCLDPSAKIGDQLIEaiPSWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLV 254
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 255 SEVFGSPRHPYTKGLLDSVP------VHAVRgedLKSIGGTPPDLHSIPDGCVYQARCPIARGICISSrPPLESVgNGRL 328
Cdd:COG4170 244 EQILKSPHHPYTKALLRSMPdfrqplPHKSR---LNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PRLRKI-KGHE 318
|
....*.
gi 1993389136 329 SACHFP 334
Cdd:COG4170 319 FACHFP 324
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-274 |
2.72e-90 |
|
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: 280.03 E-value: 2.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 8 APSARPDTGSVALDVRGLTVD-------LRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadiT 80
Cdd:COG4172 264 DPRPVPPDAPPLLEARDLKVWfpikrglFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----S 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 81 GGSVEMGDVDLVTAKTKVRRTIAAtELAIVFQDALTALNPVYTVGTQLAEPFRIHR-GMSAKQARVEAIALMARVGIPeP 159
Cdd:COG4172 339 EGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLD-P 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 160 ESRaDSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADR 239
Cdd:COG4172 417 AAR-HRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHR 495
|
250 260 270
....*....|....*....|....*....|....*
gi 1993389136 240 VAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVP 274
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-293 |
4.79e-88 |
|
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: 273.70 E-value: 4.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVdlRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADItGGSVEMGDVDLVTAKTKV 98
Cdd:COG1123 4 LLEVRDLSV--RYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RrtiaATELAIVFQDALTALNPVyTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRL 178
Cdd:COG1123 81 R----GRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1993389136 259 GSPRhpytkgLLDSVPVHAVRGEDLKSIGGTPPDL 293
Cdd:COG1123 232 AAPQ------ALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-332 |
2.95e-86 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 262.98 E-value: 2.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 32 PSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLV---TAKTKVRRTiaatELA 108
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP----TGGELYYQGQDLLkadPEAQKLLRQ----KIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 109 IVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIpEPEsRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:PRK11308 96 IVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPE-HYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKG 268
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 269 LLDSVPV--HAVRGEDLKSIGGTPPDLHSiPDGCVYQARCPIARGICISSRPPLESVGnGRLSACH 332
Cdd:PRK11308 254 LLSATPRlnPDDRRERIKLTGELPSPLNP-PPGCAFNARCPRAFGRCRQEQPQLRDYD-GRLVACF 317
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-274 |
1.12e-85 |
|
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: 258.58 E-value: 1.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV 98
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTiaatELAIVFQDALTALNPVYTVGTQLAEPFRIHrGMSAKQARVEAiaLMARVGIPEpeSRADSYPHQFSGGMRQRL 178
Cdd:COG1124 77 FRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIH-GLPDREERIAE--LLEQVGLPP--SFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 1993389136 259 GSPRHPYTKGLLDSVP 274
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-322 |
3.15e-85 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 260.41 E-value: 3.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 18 VALDVRGLTV--DLR-------TPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadITGGSVEMGD 88
Cdd:PRK15079 7 VLLEVADLKVhfDIKdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 89 VDLVTAKTKVRRTIAaTELAIVFQDALTALNPVYTVGTQLAEPFRIHR-GMSAKQARVEAIALMARVGI-PEPESRadsY 166
Cdd:PRK15079 83 KDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLlPNLINR---Y 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 167 PHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 247 NVVETGLVSEVFGSPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPDLHS---IPDGCVYQARCPIARGICISSRPPLES 322
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSpinPPSGCVFRTRCPIAGPECAKTRPVLEG 317
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-283 |
2.37e-82 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 261.71 E-value: 2.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 10 SARPDTGSVaLDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGD- 88
Cdd:PRK10261 4 SDELDARDV-LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQ----AGGLVQCDKm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 89 ---------VDLVTAKTKVRRTIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEP 159
Cdd:PRK10261 79 llrrrsrqvIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 160 ESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADR 239
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1993389136 240 VAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVP-VHAVRGEDL 283
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPqLGAMKGLDY 283
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-312 |
4.00e-80 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 253.47 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLL-EPIADITGGSVEMGDVDLVTAKTKV 98
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEPESRADSYPHQFSGGMRQRL 178
Cdd:PRK15134 86 LRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 259 GSPRHPYTKGLLDSVPvhavRGEDLKSIGGTPPDLHsipdgcVYQARC--PIARGI 312
Cdd:PRK15134 246 SAPTHPYTQKLLNSEP----SGDPVPLPEPASPLLD------VEQLQVafPIRKGI 291
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
38-270 |
9.41e-75 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 229.95 E-value: 9.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKTKVRrtiaatELAIVFQDALTA 117
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLSIRGR------HIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIPEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 198 TALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLL 270
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-334 |
1.65e-72 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 227.76 E-value: 1.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKTKVR 99
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGTQLAE--PFRIHRGMSAKQ---ARVEAIALMARVGIPEPESRADSYPHQFSGGM 174
Cdd:PRK15093 84 RKLVGHNVSMIFQEPQSCLDPSERVGRQLMQniPGWTYKGRWWQRfgwRKRRAIELLHRVGIKDHKDAMRSFPYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLV 254
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 255 SEVFGSPRHPYTKGLLDSVP------VHAVRgedLKSIGGTPPDLHSIPDGCVYQARCPIARGICISSrPPLESVGNgRL 328
Cdd:PRK15093 244 KELVTTPHHPYTQALIRAIPdfgsamPHKSR---LNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRLTGAKN-HL 318
|
....*.
gi 1993389136 329 SACHFP 334
Cdd:PRK15093 319 YACHFP 324
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
20-273 |
9.80e-64 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 203.12 E-value: 9.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSV-----EMGDVDLVTA 94
Cdd:COG4107 9 LSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAP----TSGSVyyrdrDGGPRDLFAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRRTIAATELAIVFQDALTALNPVYTVGTQLAEpfrihRGMSA-----KQARVEAIALMARVGIPEpeSRADSYPHQ 169
Cdd:COG4107 85 SEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAE-----RLMAAgerhyGDIRARALEWLERVEIPL--ERIDDLPRT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:COG4107 158 FSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVV 237
|
250 260
....*....|....*....|....
gi 1993389136 250 ETGLVSEVFGSPRHPYTKGLLDSV 273
Cdd:COG4107 238 ESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
20-272 |
1.47e-61 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 197.37 E-value: 1.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIR-----AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTA 94
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEP----TSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRrtiaATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGI-PEpesRADSYPHQFSGG 173
Cdd:COG4167 81 DYKYR----CKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE---HANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGL 253
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*....
gi 1993389136 254 VSEVFGSPRHPYTKGLLDS 272
Cdd:COG4167 234 TAEVFANPQHEVTKRLIES 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-275 |
1.04e-57 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 197.00 E-value: 1.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 1 MSAPATSAPSARPDT---GSVALDVRGLTVDLRTPSGV-------IRAVDNVTFSARRGETLALLGESGCGKSMTAQAIV 70
Cdd:PRK10261 292 LEHPAKQEPPIEQDTvvdGEPILQVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 71 GLLEPiadiTGGSVEMGD--VDLVTAKT--KVRRTIAatelaIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVE 146
Cdd:PRK10261 372 RLVES----QGGEIIFNGqrIDTLSPGKlqALRRDIQ-----FIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAAR 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 147 AIALMARVGIpEPEsRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLI 226
Cdd:PRK10261 443 VAWLLERVGL-LPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFI 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1993389136 227 THDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVPV 275
Cdd:PRK10261 521 SHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-270 |
5.43e-54 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 185.29 E-value: 5.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 1 MSAPATSAPSARPDTGSVALDVRGLTVDLRTPSGVIR-------AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLL 73
Cdd:PRK15134 257 LNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 74 EpiadiTGGSVEMGDVDLVTAKTK----VRRTIAatelaIVFQDALTALNPVYTVGTQLAEPFRIHR-GMSAKQARVEAI 148
Cdd:PRK15134 337 N-----SQGEIWFDGQPLHNLNRRqllpVRHRIQ-----VVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 149 ALMARVGIpEPESRaDSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITH 228
Cdd:PRK15134 407 AVMEEVGL-DPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1993389136 229 DLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLL 270
Cdd:PRK15134 485 DLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-279 |
7.81e-54 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 177.69 E-value: 7.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTpSGVIRA------VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVT 93
Cdd:TIGR02769 3 LEVRDVTHTYRT-GGLFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP----AQGTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 94 AKTKVRRTIaATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIpePESRADSYPHQFSGG 173
Cdd:TIGR02769 78 LDRKQRRAF-RRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGL--RSEDADKLPRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGL 253
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
250 260
....*....|....*....|....*..
gi 1993389136 254 VSEVFgSPRHPYTKGLLDSV-PVHAVR 279
Cdd:TIGR02769 235 VAQLL-SFKHPAGRNLQSAVlPEHPVR 260
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-250 |
1.34e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 175.62 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 17 SVALDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEPIadiTGGSVEMGDVDLVTAKT 96
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLDRP---TSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 97 KVRRTIAATELAIVFQDAltALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQ 176
Cdd:COG1136 78 RELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALvAEEADRVAIMYAGNVVE 250
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVS 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-272 |
1.68e-53 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 176.43 E-value: 1.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPsgvirAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKTKVR 99
Cdd:PRK10418 5 IELRNIALQAAQP-----LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTiaatelAIVFQDALTALNPVYTVGTQLAEPFRIhRGMSAKQARveAIALMARVGIPEPESRADSYPHQFSGGMRQRLL 179
Cdd:PRK10418 80 KI------ATIMQNPRSAFNPLHTMHTHARETCLA-LGKPADDAT--LTAALEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250
....*....|...
gi 1993389136 260 SPRHPYTKGLLDS 272
Cdd:PRK10418 231 APKHAVTRSLVSA 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-292 |
1.40e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 22 VRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTK---- 97
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERP----TSGSVLVDGVDLTALSERelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 98 VRRTIAatelaIVFQ-----DALTALNPVytvgtqlAEPFRIHrGMSAKQARVEAIALMARVGIpepESRADSYPHQFSG 172
Cdd:COG1135 80 ARRKIG-----MIFQhfnllSSRTVAENV-------ALPLEIA-GVPKAEIRKRVAELLELVGL---SDKADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 173 GMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1993389136 253 LVSEVFGSPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPD 292
Cdd:COG1135 224 PVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGG 263
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-273 |
9.76e-52 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 172.03 E-value: 9.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVE--MGD---VDLVTA 94
Cdd:PRK11701 7 LSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAP----DAGEVHyrMRDgqlRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRRTIAATELAIVFQDALTALNPVYTVGTQLAEPF-----RiHRGmsakQARVEAIALMARVGIPEpeSRADSYPHQ 169
Cdd:PRK11701 79 SEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLmavgaR-HYG----DIRATAGDWLERVEIDA--ARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|....
gi 1993389136 250 ETGLVSEVFGSPRHPYTKGLLDSV 273
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-252 |
2.72e-50 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 166.54 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTKVR 99
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP----DSGEILIDGRD-VTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAatelaIVFQDAltALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEPESRadsYPHQFSGGMRQRLL 179
Cdd:cd03259 72 RNIG-----MVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
26-283 |
1.64e-49 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 166.40 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 26 TVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAAT 105
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP----SQGNVSWRGEPLAKLNRAQRKAFRRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 106 eLAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEpeSRADSYPHQFSGGMRQRLLIAMAVA 185
Cdd:PRK10419 91 -IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 186 LSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVfGSPRHPY 265
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK-LTFSSPA 246
|
250 260
....*....|....*....|..
gi 1993389136 266 TKGLLDSV----PVHAVRGEDL 283
Cdd:PRK10419 247 GRVLQNAVlpafPVRRRTTEKV 268
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-257 |
3.80e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 3.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP----TSGEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAAtelaiVFQDAltALNPVYTVGTQLAEpFRIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLL 179
Cdd:COG1131 73 RRIGY-----VPQEP--ALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
40-273 |
2.33e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 162.47 E-value: 2.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEPIadiTGGSVEMGDVDLVTAKTKVRRTIAatELAIVFQDA----- 114
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLEEP---DSGTITVDGEDLTDSKKDINKLRR--KVGMVFQQFnlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 LTAL-NpvytvgtqLAEPFRIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:COG1126 92 LTVLeN--------VTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSV 273
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
40-267 |
3.51e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 162.07 E-value: 3.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAAtELAIVFQD-AL-TA 117
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP----DSGEILVDGQDITGLSEKELYELRR-RIGMLFQGgALfDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LnpvyTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:COG1127 97 L----TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPG---AADKMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 198 TALD-VTVqAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPrHPYTK 267
Cdd:COG1127 170 AGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVR 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-243 |
3.55e-48 |
|
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: 161.49 E-value: 3.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvdlvtakTKVR 99
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP----TSGEVLVDG-------EPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RtiAATELAIVFQDAltALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLL 179
Cdd:cd03293 70 G--PGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGL---SGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLalvaEEA----DRVAIM 243
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI----DEAvflaDRVVVL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-258 |
1.36e-47 |
|
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: 160.19 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTK-V 98
Cdd:COG1122 1 IELENLSF--SYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP----TSGEVLVDGKDITKKNLReL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAatelaIVFQDALTAL-NPvyTVGTQLA---EpfriHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGM 174
Cdd:COG1122 74 RRKVG-----LVFQNPDDQLfAP--TVEEDVAfgpE----NLGLPREEIRERVEEALELVGL---EHLADRPPHELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDLALVAEEADRVAIMYAGNVVETGLV 254
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
....
gi 1993389136 255 SEVF 258
Cdd:COG1122 219 REVF 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-267 |
4.33e-47 |
|
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: 159.20 E-value: 4.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTpsgviRAV-DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV 98
Cdd:cd03261 1 IELRGLTKSFGG-----RTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP----DSGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAaTELAIVFQDAltALNPVYTVGTQLAEPFRIHRGMSakQARVEAIALM--ARVGIPEpesRADSYPHQFSGGMRQ 176
Cdd:cd03261 72 LYRLR-RRMGMLFQSG--ALFDSLTVFENVAFPLREHTRLS--EEEIREIVLEklEAVGLRG---AEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSE 256
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
250
....*....|.
gi 1993389136 257 VFGSPrHPYTK 267
Cdd:cd03261 224 LRASD-DPLVR 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-248 |
6.85e-47 |
|
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: 158.04 E-value: 6.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEpiaDITGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLD---RPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDalTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLL 179
Cdd:cd03255 77 AAFRRRHIGFVFQS--FNLLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLaLVAEEADRVAIMYAGNV 248
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-262 |
1.97e-46 |
|
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: 157.36 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 22 VRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRT 101
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP----TSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 102 IAAtELAIVFQ--DALTALnpvyTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLL 179
Cdd:cd03258 80 ARR-RIGMIFQhfNLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGL---EDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 1993389136 260 SPR 262
Cdd:cd03258 231 NPQ 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
15-243 |
4.85e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.48 E-value: 4.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 15 TGSVALDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvta 94
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP----TSGEVLVDGKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 ktkvrrTIAATELAIVFQDAltALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGM 174
Cdd:COG1116 76 ------TGPGPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGL---AGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLalvaEEA----DRVAIM 243
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV----DEAvflaDRVVVL 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-272 |
3.55e-44 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 152.64 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIR-----AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTA 94
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP----TSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRrtiaATELAIVFQDALTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGI-PEpesRADSYPHQFSGG 173
Cdd:PRK15112 81 DYSYR----SQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPD---HASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGL 253
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*....
gi 1993389136 254 VSEVFGSPRHPYTKGLLDS 272
Cdd:PRK15112 234 TADVLASPLHELTKRLIAG 252
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-246 |
6.71e-44 |
|
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: 149.92 E-value: 6.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 32 PSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDLVTAKTKVRRTIAAtelaIVF 111
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS----GEVLVDGKDLTKLSLKELRRKVG----LVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QDALTAL-NPvyTVGTQLAEPFRiHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSV 190
Cdd:cd03225 82 QNPDDQFfGP--TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 191 LLADEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
20-273 |
1.18e-43 |
|
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: 150.75 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIA-DITGGSVEMGDVDLVTAKTKV 98
Cdd:TIGR02323 4 LQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHgTATYIMRSGAELELYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAATELAIVFQDALTALNPVYTVGTQLAEpfrihRGMSAKQ-----ARVEAIALMARVGIPEpeSRADSYPHQFSGG 173
Cdd:TIGR02323 80 RRRLMRTEWGFVHQNPRDGLRMRVSAGANIGE-----RLMAIGArhygnIRATAQDWLEEVEIDP--TRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGL 253
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
250 260
....*....|....*....|
gi 1993389136 254 VSEVFGSPRHPYTKGLLDSV 273
Cdd:TIGR02323 233 TDQVLDDPQHPYTQLLVSSI 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
30-273 |
1.80e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.03 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 30 RTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAK----TKVRRTIAat 105
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERP----TSGRVLVDGQDLTALSekelRKARRQIG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 106 elaIVFQ--DALTAlnpvYTVGTQLAEPFRIhRGMSAKQ--ARVEAiaLMARVGIpepESRADSYPHQFSGGMRQRLLIA 181
Cdd:PRK11153 86 ---MIFQhfNLLSS----RTVFDNVALPLEL-AGTPKAEikARVTE--LLELVGL---SDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 182 MAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
250
....*....|..
gi 1993389136 262 RHPYTKGLLDSV 273
Cdd:PRK11153 233 KHPLTREFIQST 244
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-265 |
2.84e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.56 E-value: 2.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 17 SVALDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtakT 96
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP----DSGRILLDGRDV----T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 97 KV---RRTIAatelaIVFQDAltALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGG 173
Cdd:COG3842 71 GLppeKRNVG-----MVFQDY--ALFPHLTVAENVAFGLRM-RGVPKAEIRARVAELLELVGL---EGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLalvaEEA----DRVAIMYAGNVV 249
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ----EEAlalaDRIAVMNDGRIE 215
|
250
....*....|....*.
gi 1993389136 250 ETGLVSEVFGSPRHPY 265
Cdd:COG3842 216 QVGTPEEIYERPATRF 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-258 |
3.30e-43 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.42 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLRTpsgvIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV 98
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP----SSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RrtiaATELAIVFQDALTALNpvYTVgtqlAE-------PFRIHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFS 171
Cdd:COG1120 73 L----ARRIAYVPQEPPAPFG--LTV----RElvalgryPHLGLFGRPSAEDREAVEEALERTGL---EHLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 172 GGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVET 251
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
....*..
gi 1993389136 252 GLVSEVF 258
Cdd:COG1120 220 GPPEEVL 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
37-302 |
6.18e-43 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 151.45 E-value: 6.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAatelaIVFQDAlt 116
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETP----DSGRIVLNGRDLFTNLPPRERRVG-----FVFQHY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEPESRadsYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:COG1118 85 ALFPHMTVAENIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSV--- 273
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVnvl 240
|
250 260
....*....|....*....|....*....
gi 1993389136 274 PVHaVRGEDLKSIGGTPPDLHSIPDGCVY 302
Cdd:COG1118 241 RGR-VIGGQLEADGLTLPVAEPLPDGPAV 268
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-278 |
8.10e-43 |
|
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: 148.95 E-value: 8.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 28 DLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATEL 107
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP----TSGKVLIDGQDIAAMSRKELRELRRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 108 AIVFQDalTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALS 187
Cdd:cd03294 105 SMVFQS--FALLPHRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 188 PSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTK 267
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258
|
250
....*....|.
gi 1993389136 268 GLLDSVPVHAV 278
Cdd:cd03294 259 EFFRGVDRAKV 269
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-248 |
3.11e-40 |
|
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: 139.46 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP----DSGEIKVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAatelaIVFQDAltALNPVYTVGTQLaepfrihrgmsakqarveaialmarvgipepesradsyphQFSGGMRQRLL 179
Cdd:cd03230 73 RRIG-----YLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNV 248
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
34-256 |
2.02e-39 |
|
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: 138.66 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAatelaIVFQD 113
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP----TSGRATVAGHDVVREPREVRRRIG-----IVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 -----ALTALNPVYTVGtqlaepfRIHrGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:cd03265 82 lsvddELTGWENLYIHA-------RLY-GVPGAERRERIDELLDFVGLLE---AADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSE 256
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-249 |
9.29e-39 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 137.70 E-value: 9.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03256 1 IEVENLSK--TYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP----TSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAAtELAIVFQD-----ALTALNPVYTvgTQLAE--PFRIHRGMSAKQARVEAIALMARVGIPEPES-RADsyphQFS 171
Cdd:cd03256 74 RQLRR-QIGMIFQQfnlieRLSVLENVLS--GRLGRrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYqRAD----QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 172 GGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-251 |
1.16e-38 |
|
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: 137.18 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVT----A 94
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRP----TSGTVRLAGQDLFAldedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRrtiaATELAIVFQD-----ALTALNPVyTVGTQLAepfrihrgmSAKQARVEAIALMARVGIpepESRADSYPHQ 169
Cdd:COG4181 84 RARLR----ARHVGFVFQSfqllpTLTALENV-MLPLELA---------GRRDARARARALLERVGL---GHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALvAEEADRVAIMYAGNVV 249
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRAGRLV 225
|
..
gi 1993389136 250 ET 251
Cdd:COG4181 226 ED 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-246 |
1.82e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 135.01 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtAKTKVR 99
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP----DSGSILIDGEDL--TDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDAltALNPVYTVGTQLAEPFrihrgmsakqarveaialmarvgipepesradsyphqfSGGMRQRLL 179
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
34-270 |
8.44e-38 |
|
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: 135.16 E-value: 8.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTKVRRTIAatelaIVFQD 113
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP----DSGTILFGGED-ATDVPVQERNVG-----FVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 alTALNPVYTVGTQLAEPFRIHRGMS-----AKQARVEAIALMARVgipepESRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:cd03296 83 --YALFRHMTVFDNVAFGLRVKPRSErppeaEIRAKVHELLKLVQL-----DWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKG 268
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
..
gi 1993389136 269 LL 270
Cdd:cd03296 236 FL 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
38-246 |
1.03e-37 |
|
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: 134.19 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAatELAIVFQDalTA 117
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEP----DSGTIIIDGLKLTDDKKNINELRQ--KVGMVFQQ--FN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:cd03262 87 LFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1993389136 198 TALDVTVQAQIMALLKELRTEHdMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
39-198 |
1.80e-37 |
|
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: 131.23 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtakTKVRRTIAATELAIVFQDalTAL 118
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDL----TDDERKSLRKEIGYVFQD--PQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPE-PESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:pfam00005 71 FPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1993389136 198 T 198
Cdd:pfam00005 150 A 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-263 |
2.63e-37 |
|
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: 133.01 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTvdLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03263 1 LQIRNLT--KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRP----TSGTAYINGYSIRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RtiaatELAIVFQ-----DALTALNPVYTVGtqlaepfRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGM 174
Cdd:cd03263 75 Q-----SLGYCPQfdalfDELTVREHLRFYA-------RL-KGLPKSEIKEEVELLLRVLGL---TDKANKRARTLSGGM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVAEEADRVAIMYAGNVVetglv 254
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR----- 211
|
....*....
gi 1993389136 255 seVFGSPRH 263
Cdd:cd03263 212 --CIGSPQE 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-252 |
5.13e-37 |
|
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: 131.02 E-value: 5.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 21 DVRGLTVdlRTPSGVIraVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRr 100
Cdd:cd03214 1 EVENLSV--GYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP----SSGEILLDGKDLASLSPKEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 101 tiaATELAIVFQdaltalnpvytvgtqlaepfrihrgmsakqarveaiaLMARVGIpepESRADSYPHQFSGGMRQRLLI 180
Cdd:cd03214 72 ---ARKIAYVPQ-------------------------------------ALELLGL---AHLADRPFNELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 181 AMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-261 |
3.33e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 130.92 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSgviraVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIaditGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD----SGKILLNGKDITNLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RtiaateLAIVFQDalTALNPVYTVGTQLAEPFRIHRGMSAK-QARVEAIALMarVGIPEPESRadsYPHQFSGGMRQRL 178
Cdd:cd03299 72 D------ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEiERKVLEIAEM--LGIDHLLNR---KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
...
gi 1993389136 259 GSP 261
Cdd:cd03299 219 KKP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-258 |
3.73e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 15 TGSVALDVRGLTVDLRTPsgviRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvta 94
Cdd:COG1121 2 MMMPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP----TSGTVRLFGKPP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 kTKVRRTIA----ATELAIVFQdaLTALNpvyTVGTQLAEPFRIHRGMSAKQaRVEAIALMARVGIpepESRADSYPHQF 170
Cdd:COG1121 71 -RRARRRIGyvpqRAEVDWDFP--ITVRD---VVLMGRYGRRGLFRRPSRAD-REAVDEALERVGL---EDLADRPIGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMyAGNVVE 250
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-NRGLVA 218
|
....*...
gi 1993389136 251 TGLVSEVF 258
Cdd:COG1121 219 HGPPEEVL 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
38-272 |
8.02e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 130.11 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLV-TAKTKVRRTIAatelaIVFQDalT 116
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP----TSGEIFIDGEDIReQDPVELRRKIG-----YVIQQ--I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTVGTQLAE-PFRIHRGMSAKQARVEAiaLMARVGIPePESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADE 195
Cdd:cd03295 85 GLFPHMTVEENIALvPKLLKWPKEKIRERADE--LLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 196 PTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDS 272
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-262 |
2.13e-35 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 128.71 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtAKTKVR 99
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP----TSGSVLFDGEDI--TGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RtIAATELAIVFQ-----DALTALNPVYtVGTQLAEPFRIHRGMSAK---QARVEAIALMARVGIPEpesRADSYPHQFS 171
Cdd:cd03219 71 E-IARLGIGRTFQiprlfPELTVLENVM-VAAQARTGSGLLLARARReerEARERAEELLERVGLAD---LADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 172 GGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVET 251
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|.
gi 1993389136 252 GLVSEVFGSPR 262
Cdd:cd03219 225 GTPDEVRNNPR 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
34-257 |
4.03e-35 |
|
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: 128.05 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRtiaatELAIVFQD 113
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKP----DSGSILIDGEDVRKEPREARR-----QIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 alTALNPVYTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIPEPesrADSYPHQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:COG4555 83 --RGLYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEF---LDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
34-275 |
4.81e-35 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 127.99 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRrtiaatELAIVFQD 113
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQP----DSGRIRLNGQDATRVHARDR------KIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 alTALNPVYTVGTQLAEPFRIHRGMSAK-QARVEAiaLMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:TIGR00968 81 --YALFKHLTVRDNIAFGLEIRKHPKAKiKARVEE--LLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDS 272
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGE 233
|
...
gi 1993389136 273 VPV 275
Cdd:TIGR00968 234 VNV 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
27-250 |
5.00e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.09 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTK----VRRTI 102
Cdd:COG2884 7 VSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERP----TSGQVLVNGQDLSRLKRReipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 103 AatelaIVFQDA--LTALnpvyTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLI 180
Cdd:COG2884 82 G-----VVFQDFrlLPDR----TVYENVALPLRVT-GKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 181 AMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVE 250
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-248 |
1.12e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 28 DLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAK-TKVRRTIAAte 106
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP----TSGEIYLDGKPLSAMPpPEWRRQVAY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 107 laiVFQDALTALNpvyTVGTQLAEPFRIHrgmSAKQARVEAIALMARVGIPEpeSRADSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:COG4619 79 ---VPQEPALWGG---TVRDNLPFPFQLR---ERKFDRERALELLERLGLPP--DILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNV 248
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-257 |
1.32e-34 |
|
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: 126.14 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDlrtpSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADI-TGGSVEMGDVDLVTAKTKV 98
Cdd:cd03260 1 IELRDLNVY----YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 ---RRTIAatelaIVFQDAltalNPV-YTVGTQLAEPFRIH--RGMSAKQARVEAiaLMARVGIPEPESRaDSYPHQFSG 172
Cdd:cd03260 77 lelRRRVG-----MVFQKP----NPFpGSIYDNVAYGLRLHgiKLKEELDERVEE--ALRKAALWDEVKD-RLHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 173 GMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 1993389136 253 LVSEV 257
Cdd:cd03260 223 PTEQI 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
34-256 |
1.61e-34 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 128.28 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAatelaIVFQD 113
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRP----TSGTARVAGYDVVREPRKVRRSIG-----IVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 A-----LTALNPVYTVGTQLaepfrihrGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:TIGR01188 75 AsvdedLTGRENLEMMGRLY--------GLPKDEAEERAEELLELFELGE---AADRPVGTYSGGMRRRLDIAASLIHQP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSE 256
Cdd:TIGR01188 144 DVLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
37-261 |
1.82e-34 |
|
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: 126.20 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRtiaateLAIVFQDalT 116
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETP----TSGEILLDGKDITNLPPHKRP------VNTVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEPESRadsYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:cd03300 82 ALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDlalvAEEA----DRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHD----QEEAltmsDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
37-263 |
5.36e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.88 E-value: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTKVRRTIAatelaIVFQDAlt 116
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP----TSGEILIGGRD-VTDLPPKDRNIA-----MVFQSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTVGTQLAEPFRIhRGMSAK--QARVEAIAlmARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLAD 194
Cdd:COG3839 85 ALYPHMTVYENIAFPLKL-RKVPKAeiDRRVREAA--ELLGL---EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 195 EPTTALDVTVQAQIMALLKELRTEHDMAVVLITHD----LALvaeeADRVAIMYAGNVVETGLVSEVFGSPRH 263
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
37-258 |
1.09e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtAKTKVRRTIAATELAIVFQdalt 116
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP----TSGKIIIDGVDI--TDKKVKLSDIRKKVGLVFQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 alNPVYtvgtQLAE----------PfrIHRGMSAKQARVEAIALMARVGIPEpESRADSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:PRK13637 91 --YPEY----QLFEetiekdiafgP--INLGLSEEEIENRVKRAMNIVGLDY-EDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
28-265 |
1.64e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 126.69 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 28 DLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRrtiaatEL 107
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQ----TAGTIYQGGRDITRLPPQKR------DY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 108 AIVFQDalTALNPVYTVGTQLAepFRIH-RGMSAKQARVEAIALMARVGIPEPEsraDSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:TIGR03265 79 GIVFQS--YALFPNLTVADNIA--YGLKnRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDlalvAEEA----DRVAIMYAGNVVETGLVSEVFGSPR 262
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHD----QEEAlsmaDRIVVMNHGVIEQVGTPQEIYRHPA 227
|
...
gi 1993389136 263 HPY 265
Cdd:TIGR03265 228 TPF 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
28-246 |
1.94e-33 |
|
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: 121.20 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 28 DLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTK-VRRTIaate 106
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEILIDGKDIAKLPLEeLRRRI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 107 laivfqdaltalnpvytvgtqlaepfrihrgmsakqarveaialmarvgipepesradSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:cd00267 76 ----------------------------------------------------------GYVPQLSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
49-252 |
3.63e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 122.02 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 49 GETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV-----RRTIAatelaIVFQDAltALNPVYT 123
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKP----DGGTIVLNGTVLFDSRKKInlppqQRKIG-----LVFQQY--ALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 124 VGTQLAEPFRIHRGMSAKQaRVEAIalMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVT 203
Cdd:cd03297 92 VRENLAFGLKRKRNREDRI-SVDEL--LDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1993389136 204 VQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
38-252 |
4.73e-33 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 121.98 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRrtiaatELAIVFQDalTA 117
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEP----TSGRIYIGGRDVTDLPPKDR------DIAMVFQN--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVGTQLAEPFRIHRGMSAK-QARVEAIALMARVgipepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPKDEiDERVREVAELLQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-258 |
1.39e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDLvTAKT--KVRRTIAa 104
Cdd:PRK13635 11 ISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA----GTITVGGMVL-SEETvwDVRRQVG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 105 telaIVFQdaltalNPVYT-VGTQLAE--PFRI-HRGMSAKQ--ARVEAiALmARVGIpepESRADSYPHQFSGGMRQRL 178
Cdd:PRK13635 85 ----MVFQ------NPDNQfVGATVQDdvAFGLeNIGVPREEmvERVDQ-AL-RQVGM---EDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAeEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIF 228
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-250 |
2.00e-32 |
|
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: 120.53 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:TIGR02211 2 LKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNP----TSGEVLFNGQSLSKLSSNER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQdaLTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLL 179
Cdd:TIGR02211 78 AKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALvAEEADRVAIMYAGNVVE 250
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-271 |
1.16e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 119.08 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLRTPSgVIRAVDnvtFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAK--T 96
Cdd:PRK11264 3 AIEVKNLVKKFHGQT-VLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQP----EAGTIRVGDITIDTARslS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 97 KVRRTIAA--TELAIVFQDalTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEPEsraDSYPHQFSGGM 174
Cdd:PRK11264 75 QQKGLIRQlrQHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDV----TVQAQIMALLKELRTehdmaVVLITHDLALVAEEADRVAIMYAGNVVE 250
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPelvgEVLNTIRQLAQEKRT-----MVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250 260
....*....|....*....|.
gi 1993389136 251 TGLVSEVFGSPRHPYTKGLLD 271
Cdd:PRK11264 225 QGPAKALFADPQQPRTRQFLE 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
34-252 |
1.36e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEpIAD-----ITGGSVEMGDVDLVTAKTKVRRtiaatELA 108
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLE-MPRsgtlnIAGNHFDFSKTPSDKAIRELRR-----NVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 109 IVFQDalTALNPVYTVGTQLAE-PFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALS 187
Cdd:PRK11124 86 MVFQQ--YNLWPHLTVQQNLIEaPCRV-LGLSKDQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 188 PSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-267 |
2.68e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.22 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 10 SARPDTGSVALDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKS--------MTAqaivglLEPIADITG 81
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKStllrclnrMND------LIPGARVEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 gSVEMGDVDLVTAK---TKVRRTIAatelaIVFQDAltalNP---------VYtvgtqlaePFRIHrGMSAKQ---ARVE 146
Cdd:COG1117 72 -EILLDGEDIYDPDvdvVELRRRVG-----MVFQKP----NPfpksiydnvAY--------GLRLH-GIKSKSeldEIVE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 147 AiALMaRVGI-PEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVL 225
Cdd:COG1117 133 E-SLR-KAALwDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVI 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1993389136 226 ITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTK 267
Cdd:COG1117 209 VTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-273 |
5.98e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.12 E-value: 5.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadITGGSVEMGDVDLVTAKTKVRRTiaATELAIVFQD 113
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE----ITSGDLIVDGLKVNDPKVDERLI--RQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 -----ALTALNPVytvgtqLAEPFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:PRK09493 86 fylfpHLTALENV------MFGPLRV-RGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKG 268
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
....*
gi 1993389136 269 LLDSV 273
Cdd:PRK09493 235 FLQHV 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-260 |
6.47e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 6.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTK------VRRTIAatelaIVF 111
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP----TTGTVTVDDIT-ITHKTKdkyirpVRKRIG-----MVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QdaltalnpvyTVGTQLAEPfRIHR---------GMSAKQARVEAIALMARVGIPEpeSRADSYPHQFSGGMRQRLLIAM 182
Cdd:PRK13646 92 Q----------FPESQLFED-TVEReiifgpknfKMNLDEVKNYAHRLLMDLGFSR--DVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 183 AVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGS 260
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
33-252 |
8.42e-31 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 119.82 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 33 SGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATELAIVFQ 112
Cdd:COG4175 37 TGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEP----TAGEVLIDGEDITKLSKKELRELRRKKMSMVFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 DalTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:COG4175 113 H--FALLPHRTVLENVAFGLEI-QGVPKAERRERAREALELVGL---AGWEDSYPDELSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 193 ADEPTTALD----VTVQAQIMALLKEL-RTehdmaVVLITHDLalvaEEA----DRVAIMYAGNVVETG 252
Cdd:COG4175 187 MDEAFSALDplirREMQDELLELQAKLkKT-----IVFITHDL----DEAlrlgDRIAIMKDGRIVQIG 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
34-261 |
1.84e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 115.88 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEpIAD-----ITGGSVEMGDVDLVTAKTKVRRtiaatELA 108
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLE-TPDsgqlnIAGHQFDFSQKPSEKAIRLLRQ-----KVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 109 IVFQDalTALNPVYTVGTQLAE-PFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALS 187
Cdd:COG4161 86 MVFQQ--YNLWPHLTVMENLIEaPCKV-LGLSKEQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 188 PSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGlVSEVFGSP 261
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
38-252 |
4.75e-30 |
|
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: 120.71 E-value: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaktkvrRTIAATEL----AIVFQD 113
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP----TSGRILIDGIDL--------RQIDPASLrrqiGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 A-LTAlnpvytvGTqLAEPFRIHRGmSAKQARVEAIALMArvGI-PEPESRADSYPHQ-------FSGGMRQRLLIAMAV 184
Cdd:COG2274 558 VfLFS-------GT-IRENITLGDP-DATDEEIIEAARLA--GLhDFIEALPMGYDTVvgeggsnLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 185 ALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLALVAeEADRVAIMYAGNVVETG 252
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
33-278 |
6.69e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.83 E-value: 6.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 33 SGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATELAIVFQ 112
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 DalTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:PRK10070 114 S--FALMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDS 272
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
....*.
gi 1993389136 273 VPVHAV 278
Cdd:PRK10070 268 VDISQV 273
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-261 |
1.12e-29 |
|
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: 116.35 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV------RRtiaateLAIVFQDA 114
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERP----DSGRIRLGGEVLQDSARGIflpphrRR------IGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 ltALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMarvGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLAD 194
Cdd:COG4148 87 --RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 195 EPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
37-243 |
1.19e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 112.63 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV-----RRTIAATELAIVF 111
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP----TSGSIRVFGKPLEKERKRIgyvpqRRSIDRDFPISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QdaltalnpvyTVGTQLAEPFRIHRGMSAKQARvEAIALMARVGIPEPESRADSyphQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:cd03235 89 D----------VVLMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIG---ELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 192 LADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIM 243
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
38-261 |
1.70e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKT---KVRRTIAatelaIVFQ-- 112
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKP----TSGEVLIKGEPIKYDKKsllEVRKTVG-----IVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 -DALTAlnPvyTVGTQLA-EPFRIHRGMSAKQARV-EAialMARVGIPEPESRAdsyPHQFSGGMRQRLLIAMAVALSPS 189
Cdd:PRK13639 88 dDQLFA--P--TVEEDVAfGPLNLGLSKEEVEKRVkEA---LKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-252 |
2.03e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 118.33 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 3 APATSAPSA-RPDTGSVALDVRGLTVdlRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTG 81
Cdd:COG4987 316 PPAVTEPAEpAPAPGGPSLELEDVSF--RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP----QS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 GSVEMGDVDLVT-AKTKVRRTIAatelaIVFQDAltalnpvYTVGTQLAEPFRIHRGmSAKQArvEAIALMARVGIPE-- 158
Cdd:COG4987 390 GSITLGGVDLRDlDEDDLRRRIA-----VVPQRP-------HLFDTTLRENLRLARP-DATDE--ELWAALERVGLGDwl 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 159 ---PE---SRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLAL 232
Cdd:COG4987 455 aalPDgldTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAG 532
|
250 260
....*....|....*....|
gi 1993389136 233 VaEEADRVAIMYAGNVVETG 252
Cdd:COG4987 533 L-ERMDRILVLEDGRIVEQG 551
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-249 |
2.17e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.97 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 36 IRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlvtAKTKVRRTIAAtelaIVFQDal 115
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGKP---IKAKERRKSIG----YVMQD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 talnpvytVGTQL------AEPFRIHRGMSAKQARVEAIalMARVGIPEPesrADSYPHQFSGGMRQRLLIAMAVALSPS 189
Cdd:cd03226 80 --------VDYQLftdsvrEELLLGLKELDAGNEQAETV--LKDLDLYAL---KERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-267 |
2.73e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.08 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 28 DLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLE--PIADITGGSVEMGD----VDLVTAKTKVRrt 101
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEARVSGEVYLDGQdifkMDVIELRRRVQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 102 iaatelaIVFQDAltalNPVYTVGT--QLAEPFRIHRGMSAK---QARVEAIALMARVGiPEPESRADSYPHQFSGGMRQ 176
Cdd:PRK14247 86 -------MVFQIP----NPIPNLSIfeNVALGLKLNRLVKSKkelQERVRWALEKAQLW-DEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTehDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSE 256
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|.
gi 1993389136 257 VFGSPRHPYTK 267
Cdd:PRK14247 232 VFTNPRHELTE 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-267 |
3.98e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 112.63 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 26 TVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLE--PIA------DITGGSVEMGDVDLVtaktK 97
Cdd:PRK14267 7 TVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArvegevRLFGRNIYSPDVDPI----E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 98 VRRtiaatELAIVFQDAltalNPV--YTVGTQLAEPFRIHRGMSAKQARVEAI--ALMARVGIPEPESRADSYPHQFSGG 173
Cdd:PRK14267 83 VRR-----EVGMVFQYP----NPFphLTIYDNVAIGVKLNGLVKSKKELDERVewALKKAALWDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVAEEADRVAIMYAGNVVETGL 253
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
250
....*....|....
gi 1993389136 254 VSEVFGSPRHPYTK 267
Cdd:PRK14267 232 TRKVFENPEHELTE 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-274 |
6.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvDLVTAKTK------VRRTIAatelaIV 110
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQP----TSGTVTIGE-RVITAGKKnkklkpLRKKVG-----IV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 111 FQDALTALNPvYTVGTQLA-EPfrIHRGMSAKQARVEAIALMARVGIPEpESRADSyPHQFSGGMRQRLLIAMAVALSPS 189
Cdd:PRK13634 91 FQFPEHQLFE-ETVEKDICfGP--MNFGVSEEDAKQKAREMIELVGLPE-ELLARS-PFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGL 269
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
....*
gi 1993389136 270 ldSVP 274
Cdd:PRK13634 246 --DLP 248
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-243 |
7.98e-29 |
|
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: 109.39 E-value: 7.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTK-VRRTIAat 105
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP----TSGEILIDGVDLRDLDLEsLRKNIA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 106 elaIVFQDaltalnpvytvgtqlaepfrihrgmsakqarveaialmarvgipepesradsyPHQF---------SGGMRQ 176
Cdd:cd03228 80 ---YVPQD-----------------------------------------------------PFLFsgtirenilSGGQRQ 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLALVaEEADRVAIM 243
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTI-RDADRIIVL 167
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-243 |
8.82e-29 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 110.99 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 17 SVALDVRGL--TVDLRTPSGV-IRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSV----EMGDV 89
Cdd:COG4778 2 TTLLEVENLskTFTLHLQGGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLP----DSGSIlvrhDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 90 DLVTAKTkvrRTIAA---TELAIV--FQDAL---TALNPVytvgtqlAEPFRiHRGMSAKQARVEAIALMARVGIPEpeS 161
Cdd:COG4778 78 DLAQASP---REILAlrrRTIGYVsqFLRVIprvSALDVV-------AEPLL-ERGVDREEARARARELLARLNLPE--R 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 162 RADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVA 241
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVV 223
|
..
gi 1993389136 242 IM 243
Cdd:COG4778 224 DV 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
34-259 |
1.77e-28 |
|
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: 115.28 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVE--MGD--VDLvTAKTKVRRTIAATELAI 109
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP----TSGEVNvrVGDewVDM-TKPGPDGRGRAKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 110 VFQDalTALNPVYTVGTQLAEPFRIHrgMSAKQARVEAIALMARVGIPEPESRA--DSYPHQFSGGMRQRLLIAMAVALS 187
Cdd:TIGR03269 370 LHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEEKAEEilDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 188 PSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-252 |
2.27e-28 |
|
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: 109.38 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEP----DAGFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAatelaivFQDALTALNPVYTVGTQLAEPFRIHrGMSAKQ--ARVEAIAlmARVGIPE-PESRADSyphqFSGGMRQ 176
Cdd:cd03266 78 RRLG-------FVSDSTGLYDRLTARENLEYFAGLY-GLKGDEltARLEELA--DRLGMEElLDRRVGG----FSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
54-275 |
5.65e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 111.05 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 54 LLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDlVTAKTKVRRTIAatelaIVFQDalTALNPVYTVGTQLAEPFR 133
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS----GSIMLDGED-VTNVPPHLRHIN-----MVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 134 IHR-GMSAKQARVeaialMARVGIPEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALL 212
Cdd:TIGR01187 69 MRKvPRAEIKPRV-----LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 213 KELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVPV 275
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-252 |
1.47e-27 |
|
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: 112.93 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 13 PDTGSVALDVRGLTVdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLV 92
Cdd:COG4988 330 PAAGPPSIELEDVSF--SYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP----YSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 93 TAKTKVRRTiaatELAIVFQdaltalNPVYTVGTqLAEPFRIHRgMSAKQARVEAIAlmARVGIPEpesRADSYPHQF-- 170
Cdd:COG4988 403 DLDPASWRR----QIAWVPQ------NPYLFAGT-IRENLRLGR-PDASDEELEAAL--EAAGLDE---FVAALPDGLdt 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 ---------SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVAeEADRVA 241
Cdd:COG4988 466 plgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRIL 542
|
250
....*....|.
gi 1993389136 242 IMYAGNVVETG 252
Cdd:COG4988 543 VLDDGRIVEQG 553
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-264 |
1.56e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.28 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:COG4559 2 LEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTP----SSGEVRLNGRPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 rtiaATELAIVFQDaltalnpvytvgTQLAEPF---------RIHRGMSAKQARVEAIALMARVGIPEPESRadSYPhQF 170
Cdd:COG4559 74 ----ARRRAVLPQH------------SSLAFPFtveevvalgRAPHGSSAAQDRQIVREALALVGLAHLAGR--SYQ-TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMA-------VALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIM 243
Cdd:COG4559 135 SGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLL 213
|
250 260 270
....*....|....*....|....*....|....
gi 1993389136 244 YAGNVVETG---------LVSEVFGSP----RHP 264
Cdd:COG4559 214 HQGRLVAQGtpeevltdeLLERVYGADlrvlAHP 247
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
24-261 |
2.25e-27 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 110.08 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 24 GLTVD-LRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiaDITGGSVEMGDVDLVTAKTKVRrti 102
Cdd:TIGR03258 5 GIRIDhLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKA--AGLTGRIAIADRDLTHAPPHKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 103 aatELAIVFQDalTALNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMArVGIPEPESRadsYPHQFSGGMRQRLLIAM 182
Cdd:TIGR03258 80 ---GLALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKL-VGLGDAAAH---LPAQLSGGMQQRIAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 183 AVALSPSVLLADEPTTALDVTVQAQIMALLKELRTE-HDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:TIGR03258 151 AIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
27-264 |
2.86e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.75 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDL-----------VTAK 95
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKP----SEGSIVVNGQTInlvrdkdgqlkVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 96 TKVRrtIAATELAIVFQ-----DALTALNPVYTVGTQLAepfrihrGMSAKQARVEAIALMARVGIPEpeSRADSYPHQF 170
Cdd:PRK10619 85 NQLR--LLRTRLTMVFQhfnlwSHMTVLENVMEAPIQVL-------GLSKQEARERAVKYLAKVGIDE--RAQGKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVE 250
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250
....*....|....
gi 1993389136 251 TGLVSEVFGSPRHP 264
Cdd:PRK10619 233 EGAPEQLFGNPQSP 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-237 |
3.32e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaktkv 98
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAP----SSGEITLDGVPV------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 rrTIAATELAIVFQDalTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEPESRAdsyPHQFSGGMRQRL 178
Cdd:COG4525 72 --TGPGADRGVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLalvaEEA 237
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV----EEA 198
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
39-287 |
4.55e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.51 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiaditggsvEMGDV----DLVTAKT--KVRRTIAatelaIVFQ 112
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA---------ESGQIiidgDLLTEENvwDIRHKIG-----MVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 daltalNPV-----YTVGTQLAepFRI-HRGMSAKQ--ARV-EAIALmarVGIPEPESRAdsyPHQFSGGMRQRLLIAMA 183
Cdd:PRK13650 89 ------NPDnqfvgATVEDDVA--FGLeNKGIPHEEmkERVnEALEL---VGMQDFKERE---PARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 184 VALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAeEADRVAIMYAGNVVETGLVSEVFGsprh 263
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS---- 229
|
250 260
....*....|....*....|....
gi 1993389136 264 pytkglldsvpvhavRGEDLKSIG 287
Cdd:PRK13650 230 ---------------RGNDLLQLG 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-258 |
5.26e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 18 VALDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaktk 97
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSP----DSGEVRLNGRPL------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 98 vrRTIAATELAivfqdALTALNPVYTvgtQLAEPF---------RIHRGMSAKQARVEAIALMARVGIPEPESRadSYPh 168
Cdd:PRK13548 67 --ADWSPAELA-----RRRAVLPQHS---SLSFPFtveevvamgRAPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 169 QFSGGMRQRLLIAMAVA-LS-----PSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAI 242
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqLWepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
250
....*....|....*.
gi 1993389136 243 MYAGNVVETGLVSEVF 258
Cdd:PRK13548 214 LHQGRLVADGTPAEVL 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-270 |
7.49e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 7.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 43 TFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVtaktkvRRTIAATELAIVFQDalTALNPVY 122
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP----DSGRILWNGQDLT------ALPPAERPVSMLFQE--NNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 123 TVGTQLAepFRIHRGM---SAKQARVEAIAlmARVGIPEPESRadsYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTA 199
Cdd:COG3840 87 TVAQNIG--LGLRPGLkltAEQRAQVEQAL--ERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 200 LDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTKGLL 270
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
20-243 |
9.40e-27 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 105.55 E-value: 9.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGL--TVDLRTPSGVIR-AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGGSVEMGDVDLVTAKT 96
Cdd:TIGR02324 2 LEVEDLskTFTLHQQGGVRLpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQASP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 97 K----VRRTiaatELAIVFQdALTALNPVYTVGTqLAEPFrIHRGMSAKQARVEAIALMARVGIPEpesRA-DSYPHQFS 171
Cdd:TIGR02324 82 RevleVRRK----TIGYVSQ-FLRVIPRVSALEV-VAEPL-LERGVPREAARARARELLARLNIPE---RLwHLPPATFS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 172 GGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIM 243
Cdd:TIGR02324 152 GGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-248 |
1.08e-26 |
|
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: 104.80 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIrAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLV----TAKTKVRRTI 102
Cdd:cd03292 6 VTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP----TSGTIRVNGQDVSdlrgRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 103 AatelaIVFQDALtaLNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAM 182
Cdd:cd03292 81 G-----VVFQDFR--LLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 183 AVALSPSVLLADEPTTALDVTVQAQIMALLKELrteHDMA--VVLITHDLALVAEEADRVAIMYAGNV 248
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI---NKAGttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
38-258 |
2.34e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKT--KVRRTIAatelaIVFQdal 115
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIP----SEGKVYVDGLDTSDEENlwDIRNKAG-----MVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 talNP-VYTVGTQLAEPFRI---HRGMSAKQARVEAIALMARVGIPEPESRAdsyPHQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:PRK13633 93 ---NPdNQIVATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHA---PHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 192 LADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAeEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEIF 232
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
248-333 |
3.42e-26 |
|
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: 99.74 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 248 VVETGLVSEVFGSPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPDLHSIPDGCVYQARCPIARGICISSRPPLESVGNGR 327
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEGH 81
|
....*.
gi 1993389136 328 LSACHF 333
Cdd:TIGR01727 82 RVACHL 87
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
41-232 |
3.75e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.13 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATELAIVFQdaLTALNP 120
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP----TSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 121 VYTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTAL 200
Cdd:PRK11629 101 DFTALENVAMPLLIG-KKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|..
gi 1993389136 201 DVTVQAQIMALLKELRTEHDMAVVLITHDLAL 232
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
42-234 |
4.26e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 103.71 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 42 VTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDLVTAKTKVRRTIAATELAIVFQD-----ALT 116
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSfmlipTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVytvgtQLAEpfrIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:PRK10584 105 ALENV-----ELPA---LLRGESSRQSRNGAKALLEQLGLGK---RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVA 234
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
38-258 |
4.60e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.83 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvDLVTA--KTKVRRTIaatelAIVFQdal 115
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKV----KSGEIFYNN-QAITDdnFEKLRKHI-----GIVFQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 talNP---------VYTVGTQLAEPFRIHRGMSAKQARVeaialMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:PRK13648 91 ---NPdnqfvgsivKYDVAFGLENHAVPYDEMHRRVSEA-----LKQVDMLE---RADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLAlVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
39-263 |
5.06e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 103.70 E-value: 5.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaktkvrrTIAATELAIVFQDalTAL 118
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP----TSGGVILEGKQI---------TEPGPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQLA---EPFRIHRGMSAKQARVEA-IALmarVGIPEPesrADSYPHQFSGGMRQRLLIAMAVALSPSVLLAD 194
Cdd:TIGR01184 66 LPWLTVRENIAlavDRVLPDLSKSERRAIVEEhIAL---VGLTEA---ADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 195 EPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV-FGSPRH 263
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
41-246 |
5.12e-26 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 103.17 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSmTAQAIVGLLEPIADitgGSVEMGDVDLVTAK----TKVRRTIAatelaIVFQ---- 112
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKT-TLLTLIGGLRSVQE---GSLKVLGQELHGASkkqlVQLRRRIG-----YIFQahnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 -DALTALNPVytvgtQLAepFRIHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:TIGR02982 94 lGFLTARQNV-----QMA--LELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 192 LADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDlALVAEEADRVAIMYAG 246
Cdd:TIGR02982 164 LADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDG 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-252 |
5.82e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 103.04 E-value: 5.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVdlRTPSGviRAVDNVTFSARRGeTLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03264 1 LQLENLTK--RYGKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP----SSGTIRIDGQDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDALTALNPVYTVGtqlaepfrIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLL 179
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIA--------WLKGIPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
53-265 |
6.33e-26 |
|
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: 105.96 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 53 ALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATELAIVFQDAltALNPVYTVGTQLAEPF 132
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRP----DEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEA--RLFPHLSVRGNLRYGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 133 RIHRGmsaKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALL 212
Cdd:TIGR02142 101 KRARP---SERRISFERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 213 KELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPY 265
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-267 |
6.45e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 6.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpIAD----ITGGSVEMGDVDLVTAKTKVRRtiaatELAIVFQDAlt 116
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIE-IYDskikVDGKVLYFGKDIFQIDAIKLRK-----EVGMVFQQP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 alNPV--YTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGI-PEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:PRK14246 100 --NPFphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRTEhdMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTK 267
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-251 |
1.06e-25 |
|
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: 100.58 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvdlvtaktkvr 99
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP----DSGEILVDG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 rtiaatelaivfqdaltalnpvytvgtqlaEPFRIHRGMSAKQARVEAIalmarvgipepesradsypHQFSGGMRQRLL 179
Cdd:cd03216 62 ------------------------------KEVSFASPRDARRAGIAMV-------------------YQLSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDLALVAEEADRVAIMYAGNVVET 251
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
40-242 |
1.64e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.40 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRtiaatELAIVFQDAltALN 119
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP----SAGEVLWNGEPIRDAREDYRR-----RLAYLGHAD--GLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 120 PVYTVGTQLaepfRIHRGMSAKQARVEAI-ALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTT 198
Cdd:COG4133 88 PELTVRENL----RFWAALYGLRADREAIdEALEAVGL---AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1993389136 199 ALDVTVQAQIMALLKELRtEHDMAVVLITHDlALVAEEADRVAI 242
Cdd:COG4133 161 ALDAAGVALLAELIAAHL-ARGGAVLLTTHQ-PLELAAARVLDL 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-249 |
1.72e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 11 ARPDTGSVALDVRGLTVdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVD 90
Cdd:COG3845 249 APAEPGEVVLEVENLSV--RDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP----ASGSIRLDGED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 91 lVTAKTkvRRTIAATELAIVFQDAL-TALNPVYTV------GTQLAEPFRIHRGMSAKQARVEAIALMARVGI--PEPES 161
Cdd:COG3845 322 -ITGLS--PRERRRLGVAYIPEDRLgRGLVPDMSVaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVrtPGPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 162 RADSyphqFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLalvaEE----A 237
Cdd:COG3845 399 PARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAGAAVLLISEDL----DEilalS 469
|
250
....*....|..
gi 1993389136 238 DRVAIMYAGNVV 249
Cdd:COG3845 470 DRIAVMYEGRIV 481
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-257 |
3.69e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 30 RTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEmgdvdlvtaktkVRRTIAA-TELA 108
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP----TSGRVE------------VNGRVSAlLELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 109 IVFQDALTALNPVYTVGtqlaepfRIHrGMSAKQ--ARVEAIALMARVG--IPEPESRadsyphqFSGGMRQRLLIAMAV 184
Cdd:COG1134 97 AGFHPELTGRENIYLNG-------RLL-GLSRKEidEKFDEIVEFAELGdfIDQPVKT-------YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 185 ALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-257 |
4.69e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 100.59 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTkvr 99
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP----RSGSIRFDGRDITGLPP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELAIVFQDAltALNPVYTVgtqlAEPFRI---HRGMSAKQARVEAIALMarvgIPEPESRADSYPHQFSGGMRQ 176
Cdd:cd03224 70 HERARAGIGYVPEGR--RIFPELTV----EENLLLgayARRRAKRKARLERVYEL----FPRLKERRKQLAGTLSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSE 256
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
.
gi 1993389136 257 V 257
Cdd:cd03224 219 L 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
34-252 |
1.35e-24 |
|
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: 99.53 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEmgdvdlvtaktkVRRTIAA-TELAIVFQ 112
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPP----DSGTVT------------VRGRVSSlLGLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 DALTALNPVYTVGtqlaepfRIHrGMSAKQ--ARVEAIALMARVG--IPEPESRadsyphqFSGGMRQRLLIAMAVALSP 188
Cdd:cd03220 97 PELTGRENIYLNG-------RLL-GLSRKEidEKIDEIIEFSELGdfIDLPVKT-------YSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-261 |
1.48e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 33 SGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTK-VRRTIAatelaIVF 111
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP----TSGSVLIRGEPITKENIReVRKFVG-----LVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QDALTAL-NPvyTVGTQLA-EPFRIHRGMSAKQARVEAIALMarVGIPEPESRAdsyPHQFSGGMRQRLLIAMAVALSPS 189
Cdd:PRK13652 85 QNPDDQIfSP--TVEQDIAfGPINLGLDEETVAHRVSSALHM--LGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-257 |
1.84e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.95 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaKTKVRRTIAatelaivfqdalt 116
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP----DSGEVLWDGEPL---DPEDRRRIG------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 alnpvY-----------TVGTQLAepF--RIHrGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMA 183
Cdd:COG4152 75 -----YlpeerglypkmKVGEQLV--YlaRLK-GLSKAEAKRRADEWLERLGLGD---RANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 184 VALSPSVLLADEPTTALD-VTVQAqIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:COG4152 144 LLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-258 |
2.30e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTK------VRRTIAatelaIV 110
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP----TQGSVRVDDTL-ITSTSKnkdikqIRKKVG-----LV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 111 FQDAL------TALNPVyTVGTQlaepfriHRGMSAKQARVEAIALMARVGIPEpeSRADSYPHQFSGGMRQRLLIAMAV 184
Cdd:PRK13649 91 FQFPEsqlfeeTVLKDV-AFGPQ-------NFGVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 185 ALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-257 |
2.81e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 18 VALDVRGLTvdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvdlvtAKTK 97
Cdd:COG1129 3 PLLEMRGIS---KSFGGV-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQP----DSGEILLDG-----EPVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 98 VRRTIAATEL--AIVFQDaltaLNPV--YTV------GTQLAEPFRIHRgmsaKQARVEAIALMARVGIPE-PESRADSY 166
Cdd:COG1129 70 FRSPRDAQAAgiAIIHQE----LNLVpnLSVaeniflGREPRRGGLIDW----RAMRRRARELLARLGLDIdPDTPVGDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 167 phqfSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:COG1129 142 ----SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDG 216
|
250
....*....|.
gi 1993389136 247 NVVETGLVSEV 257
Cdd:COG1129 217 RLVGTGPVAEL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
37-273 |
4.39e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDL--VTAKTKVRRtiaateLAIVFQDA 114
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS----GTVFLGDKPIsmLSSRQLARR------LALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 LTalnPVYTVGTQLAE----PFRIHRG-MSAK-QARVEAIalMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:PRK11231 86 LT---PEGITVRELVAygrsPWLSLWGrLSAEdNARVNQA--MEQTRINH---LADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFgsprhpyTKG 268
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-------TPG 229
|
....*
gi 1993389136 269 LLDSV 273
Cdd:PRK11231 230 LLRTV 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-246 |
5.88e-24 |
|
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: 96.73 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 16 GSVALDVRGLTVDlrtpsgviRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtak 95
Cdd:cd03215 1 GEPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP----ASGEITLDGKPV---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 96 tKVRRTIAATELAIVFqdaltalnpvytvgtqLAEPfRIHRGMSAKQARVEAIALmarvgipepesradsyPHQFSGGMR 175
Cdd:cd03215 65 -TRRSPRDAIRAGIAY----------------VPED-RKREGLVLDLSVAENIAL----------------SSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 176 QRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
39-240 |
8.60e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.17 E-value: 8.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGgSVEMGDVDLVTAKTKVRRtiaateLAIVFQDALtaL 118
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASG-EVLLNGRRLTALPAEQRR------IGILFQDDL--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQL--AEPFRIHRgmSAKQARVEAiALmARVGIPepeSRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:COG4136 88 FPHLSVGENLafALPPTIGR--AQRRARVEQ-AL-EEAGLA---GFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDLAlVAEEADRV 240
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE-DAPAAGRV 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
37-237 |
9.15e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 9.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVdlvtaktkvRRTIAATELAIVFQDalT 116
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPY----QHGSITLDGK---------PVEGPGAERGVVFQN--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTV------GTQLAepfrihrGMSAKQARVEAIALMARVGIPEPESRadsYPHQFSGGMRQRLLIAMAVALSPSV 190
Cdd:PRK11248 80 GLLPWRNVqdnvafGLQLA-------GVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1993389136 191 LLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLalvaEEA 237
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI----EEA 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-275 |
9.77e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.29 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVA---LDVRGLTvdlRTPSGvIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVE 85
Cdd:PRK11607 6 PRPQAKTRKALtplLEIRNLT---KSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 86 MGDVDLVTAKTKVRrtiaatELAIVFQDalTALNPVYTVGTQLAepfrihrgMSAKQARVEAIALMARV----GIPEPES 161
Cdd:PRK11607 78 LDGVDLSHVPPYQR------PINMMFQS--YALFPHMTVEQNIA--------FGLKQDKLPKAEIASRVnemlGLVHMQE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 162 RADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVA 241
Cdd:PRK11607 142 FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIA 221
|
250 260 270
....*....|....*....|....*....|....
gi 1993389136 242 IMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVPV 275
Cdd:PRK11607 222 IMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
38-265 |
1.54e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.64 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTKVRRTIAAtelaiVFQDalTA 117
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETP----DSGRIMLDGQD-ITHVPAENRHVNT-----VFQS--YA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVGTQLAEPFRIHRGMSAK-QARV-EAIAlMARVgipepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADE 195
Cdd:PRK09452 97 LFPHMTVFENVAFGLRMQKTPAAEiTPRVmEALR-MVQL-----EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 196 PTTALDVTVQAQIMALLKELRTEHDMAVVLITHDlalvAEEA----DRVAIMYAGNVvetglvsEVFGSPRHPY 265
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHD----QEEAltmsDRIVVMRDGRI-------EQDGTPREIY 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-252 |
1.80e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.01 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSmTaqaIVGLLEPIADITGGSVEMGDVDLVTAKTK-VRRTIAatelaIVFQDALt 116
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKS-T---LVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQIG-----VVPQDTF- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 alnpVYTvGTqLAEPFRIHRgMSAKQARVEAIALMARVgipepESRADSYPHQF-----------SGGMRQRLLIAMAVA 185
Cdd:COG1132 425 ----LFS-GT-IRENIRYGR-PDATDEEVEEAAKAAQA-----HEFIEALPDGYdtvvgergvnlSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 186 LSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLALVAeEADRVAIMYAGNVVETG 252
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIR-NADRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
37-261 |
3.58e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKT------KVRRtiaatELAIV 110
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP----SSGTITIAGYH-ITPETgnknlkKLRK-----KVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 111 FQDALTALNPVYTVGTQLAEPFRIhrGMSAKQARVEAIALMARVGIPEpeSRADSYPHQFSGGMRQRLLIAMAVALSPSV 190
Cdd:PRK13641 91 FQFPEAQLFENTVLKDVEFGPKNF--GFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 191 LLADEPTTALDVTVQAQIMALLKELRTE-HdmAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAgH--TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-292 |
3.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMgDVDLVTAKT--K 97
Cdd:PRK13642 5 LEVENLVFKYEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFE----GKVKI-DGELLTAENvwN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 98 VRRTIAatelaIVFQDALTALnpvytVGTQLAE--PFRIHRGMSAKQARVEAI--ALMArVGIPEPESRAdsyPHQFSGG 173
Cdd:PRK13642 79 LRRKIG-----MVFQNPDNQF-----VGATVEDdvAFGMENQGIPREEMIKRVdeALLA-VNMLDFKTRE---PARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAeEADRVAIMYAGNVVETGL 253
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAA 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 1993389136 254 VSEVFGSPRHPYTKGLldSVPVHAVRGEDLKSIGGTPPD 292
Cdd:PRK13642 224 PSELFATSEDMVEIGL--DVPFSSNLMKDLRKNGFDLPE 260
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-256 |
8.94e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 2 SAPATSAPSARPDTGSVALDVRGLTVDLRTPsGVIRAVDNVTFSARRGETLALLGESGCGKSMTaqaiVGLLEPIADITG 81
Cdd:PRK13657 315 AVPDVRDPPGAIDLGRVKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRVFDPQS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 GSVEMGDVDL--VTAKTkVRRTIAatelaIVFQDALTaLNPVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARvgipep 159
Cdd:PRK13657 390 GRILIDGTDIrtVTRAS-LRRNIA-----VVFQDAGL-FNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIER------ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 160 esRADSYP-------HQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLAL 232
Cdd:PRK13657 457 --KPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLST 532
|
250 260
....*....|....*....|....
gi 1993389136 233 VAeEADRVAIMYAGNVVETGLVSE 256
Cdd:PRK13657 533 VR-NADRILVFDNGRVVESGSFDE 555
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
39-302 |
1.19e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRrtiaATELAIVFQDalTAL 118
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPP----DSGEVLVDGLDVATTPSREL----AKRLAILRQE--NHI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVgTQLAE----PFriHRG-MSAKQARV--EAIALMarvgipEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:COG4604 87 NSRLTV-RELVAfgrfPY--SKGrLTAEDREIidEAIAYL------DLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 192 LADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVfgsprhpytkglld 271
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI-------------- 223
|
250 260 270
....*....|....*....|....*....|...
gi 1993389136 272 svpvhaVRGEDLKSIGGTPPDLHSIPDG--CVY 302
Cdd:COG4604 224 ------ITPEVLSDIYDTDIEVEEIDGKriCVY 250
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
38-261 |
1.37e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiaDITGGSVEMGDVDLVTAKT--KVRRTIAatelaIVFQdal 115
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP--DDNPNSKITVDGITLTAKTvwDIREKVG-----IVFQ--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 talNPV-----YTVGTQLAepFRI-HRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPS 189
Cdd:PRK13640 92 ---NPDnqfvgATVGDDVA--FGLeNRAVPRPEMIKIVRDVLADVGMLD---YIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLAlVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-258 |
1.50e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVdLVTAKTKVRRTIAA-TELAIVFQDAL 115
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP----TEGKVTVGDI-VVSSTSKQKEIKPVrKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 TALNPVYTVGTQLAEPFRIhrGMSAKQARVEAIALMARVGIPEpeSRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADE 195
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNF--GIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 196 PTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
38-258 |
1.54e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDL-VTAK--TKVRRTIAatelaIVFQDA 114
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS----GRILFDGKPIdYSRKglMKLRESVG-----MVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 LTAL--NPVY------TVGTQLAEPfRIHRgmsakqaRVEAIalMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:PRK13636 92 DNQLfsASVYqdvsfgAVNLKLPED-EVRK-------RVDNA--LKRTGI---EHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-252 |
2.78e-22 |
|
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: 97.48 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 13 PDTGSVALD-VRGL----TVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMG 87
Cdd:TIGR02203 317 KDTGTRAIErARGDvefrNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 88 DVDLVTAKTKVRRTiaatELAIVFQDaltalnpVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVgipepESRADSYP 167
Cdd:TIGR02203 393 GHDLADYTLASLRR----QVALVSQD-------VVLFNDTIANNIAYGRTEQADRAEIERALAAAYA-----QDFVDKLP 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 168 HQF-----------SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVvlITHDLALVaEE 236
Cdd:TIGR02203 457 LGLdtpigengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLV--IAHRLSTI-EK 533
|
250
....*....|....*.
gi 1993389136 237 ADRVAIMYAGNVVETG 252
Cdd:TIGR02203 534 ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-258 |
5.39e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.52 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 14 DTGSVALDVRGLTvdLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVT 93
Cdd:PRK13632 2 KNKSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP----QSGEIKIDGITISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 94 A-KTKVRRTIAatelaIVFQdaltalNPV-----YTVGTQLA---EPFRIHRG-MSAKqarVEAIAlmARVGIpepESRA 163
Cdd:PRK13632 76 EnLKEIRKKIG-----IIFQ------NPDnqfigATVEDDIAfglENKKVPPKkMKDI---IDDLA--KKVGM---EDYL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 164 DSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLalvaEE---ADRV 240
Cdd:PRK13632 137 DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM----DEailADKV 212
|
250
....*....|....*...
gi 1993389136 241 AIMYAGNVVETGLVSEVF 258
Cdd:PRK13632 213 IVFSEGKLIAQGKPKEIL 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
35-252 |
6.60e-22 |
|
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: 92.40 E-value: 6.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 35 VIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAAtelaivfqda 114
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP----TSGEVRVAGLVPWKRRKKFLRRIGV---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 ltalnpVYTVGTQL------AEPFRIHRGM-----SAKQARVEAIALMARVgipepESRADSYPHQFSGGMRQRLLIAMA 183
Cdd:cd03267 99 ------VFGQKTQLwwdlpvIDSFYLLAAIydlppARFKKRLDELSELLDL-----EELLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 184 VALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
41-305 |
7.17e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRtiaateLAIVFQDalTALNP 120
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ----TSGHIRFHGTDVSRLHARDRK------VGFVFQH--YALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 121 VYTVGTQLAEPFRI---HRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:PRK10851 88 HMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAH---LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 198 TALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFgspRHPYTKGLLDSV-PVH 276
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW---REPATRFVLEFMgEVN 241
|
250 260 270
....*....|....*....|....*....|..
gi 1993389136 277 AVRGEDLKS---IGGTPPDLHSIPdgcVYQAR 305
Cdd:PRK10851 242 RLQGTIRGGqfhVGAHRWPLGYTP---AYQGP 270
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-249 |
8.36e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 32 PSG--VIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEpiaDITGGSVEMGDVDLVT----AKTKVRRTiaat 105
Cdd:PRK10535 15 PSGeeQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLD---KPTSGTYRVAGQDVATldadALAQLRRE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 106 ELAIVFQ-----DALTALNPVytvgtqlaEPFRIHRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLI 180
Cdd:PRK10535 87 HFGFIFQryhllSHLTAAQNV--------EVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 181 AMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDlALVAEEADRVAIMYAGNVV 249
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-249 |
8.59e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVALDVRGLTVDlrtpsgviRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGD 88
Cdd:COG1129 246 PKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA----DSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 89 vdlvtAKTKVRRTIAATELAIVF------QDALTALNPVYTvGTQLAEPFRIHRG--MSAKQARVEAIALMARVGI--PE 158
Cdd:COG1129 314 -----KPVRIRSPRDAIRAGIAYvpedrkGEGLVLDLSIRE-NITLASLDRLSRGglLDRRRERALAEEYIKRLRIktPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 159 PESRADSyphqFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEAD 238
Cdd:COG1129 388 PEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSD 462
|
250
....*....|.
gi 1993389136 239 RVAIMYAGNVV 249
Cdd:COG1129 463 RILVMREGRIV 473
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-243 |
9.85e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.82 E-value: 9.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 2 SAPATSAPSArpdtgsvALDVRGLTVdlrTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTG 81
Cdd:TIGR02857 311 KAPVTAAPAS-------SLEFSGVSV---AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP----TE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 GSVEMGDVDLVTAKTKVRRTiaatelaivfQDALTALNPVYTVGTqLAEPFRIHRGMSAKQARVEAIAlmaRVGIPE--- 158
Cdd:TIGR02857 377 GSIAVNGVPLADADADSWRD----------QIAWVPQHPFLFAGT-IAENIRLARPDASDAEIREALE---RAGLDEfva 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 159 -----PESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALv 233
Cdd:TIGR02857 443 alpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLAL- 519
|
250
....*....|
gi 1993389136 234 AEEADRVAIM 243
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-249 |
1.10e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.47 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDLVTAKTK----VRRTIAatelaIVFQ 112
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA----GKIWFSGHDITRLKNRevpfLRRQIG-----MIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 DALTALNpvYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:PRK10908 87 DHHLLMD--RTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
249-313 |
1.17e-21 |
|
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: 86.69 E-value: 1.17e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 249 VETGLVSEVFGSPRHPYTKGLLDSVPVHAVRGEDLKSIGGTPPDLHSIPDGCVYQARCPIARGIC 313
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
40-252 |
1.19e-21 |
|
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: 91.83 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDLVTAKTKVRRTIaateLAIVFQDaltaln 119
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQE------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 120 PVYTVGTqLAEPFRIHRGmSAKQARVEAIALMAR-----VGIPEP-ESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:cd03249 86 PVLFDGT-IAENIRYGKP-DATDEEVEEAAKKANihdfiMSLPDGyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRTehDMAVVLITHDLALVaEEADRVAIMYAGNVVETG 252
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-257 |
1.64e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 15 TGSVALDVRGLTVdlRTPSgvIRAVDNVTFSARRGETLALLGESGCGKS--MtaQAIVGLLEPiadiTGGSVEMGDvdlv 92
Cdd:COG3845 1 MMPPALELRGITK--RFGG--VVANDDVSLTVRPGEIHALLGENGAGKStlM--KILYGLYQP----DSGEILIDG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 93 tAKTKVRRTIAATELAI--VFQ-----DALTAL-NPVytVGTQLAEPFRIHRgmsaKQARVEAIALMARVGIP-EPesra 163
Cdd:COG3845 67 -KPVRIRSPRDAIALGIgmVHQhfmlvPNLTVAeNIV--LGLEPTKGGRLDR----KAARARIRELSERYGLDvDP---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 164 DSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALdvTVQ--AQIMALLKELRTEhDMAVVLITHDLALVAEEADRVA 241
Cdd:COG3845 136 DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVT 212
|
250
....*....|....*.
gi 1993389136 242 IMYAGNVVETGLVSEV 257
Cdd:COG3845 213 VLRRGKVVGTVDTAET 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
34-252 |
1.69e-21 |
|
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: 90.80 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAktkVRRTIAatelaivFQD 113
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP----DSGEVLFDGKPLDIA---ARNRIG-------YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 ALTALNPVYTVGTQLAEPFRIhRGMSAKQARVEAIALMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSE---YANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-266 |
2.05e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 25 LTV-DLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAI--VGLLEPIADITGgSVEMGDVDLVTAKT---KV 98
Cdd:PRK14239 6 LQVsDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITG-SIVYNGHNIYSPRTdtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRtiaatELAIVFQDAltalNPV-YTVGTQLAEPFRIhRGMSAKQARVEAI--ALMARVGIPEPESRADSYPHQFSGGMR 175
Cdd:PRK14239 85 RK-----EIGMVFQQP----NPFpMSIYENVVYGLRL-KGIKDKQVLDEAVekSLKGASIWDEVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 176 QRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVS 255
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
250
....*....|.
gi 1993389136 256 EVFGSPRHPYT 266
Cdd:PRK14239 233 QMFMNPKHKET 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
39-264 |
2.55e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.25 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMgDVDLVTaktkvRRTIAATELAIVFQDalTAL 118
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP----TEGQIFI-DGEDVT-----HRSIQQRDICMVFQS--YAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQLAEPFRIH-RGMSAKQARV-EAIALMARVGIpepesrADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLgVPKEERKQRVkEALELVDLAGF------EDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFgspRHP 264
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQP 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-252 |
4.03e-21 |
|
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: 90.37 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDLVTAKTK-VRRTIAat 105
Cdd:cd03251 6 VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLAsLRRQIG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 106 elaIVFQDaltalnpVYTVGTQLAEPFRIHRgMSAKQARVEAIALMArvgipepesradsYPHQF--------------- 170
Cdd:cd03251 80 ---LVSQD-------VFLFNDTVAENIAYGR-PGATREEVEEAARAA-------------NAHEFimelpegydtviger 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 ----SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKEL---RTehdmaVVLITHDLALVaEEADRVAIM 243
Cdd:cd03251 136 gvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmknRT-----TFVIAHRLSTI-ENADRIVVL 209
|
....*....
gi 1993389136 244 YAGNVVETG 252
Cdd:cd03251 210 EDGKIVERG 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
45-248 |
7.18e-21 |
|
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: 89.15 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 45 SARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDlVTAKTKVRRTIAatelaIVFQDalTALNPVYTV 124
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPAS----GSIKVNDQS-HTGLAPYQRPVS-----MLFQE--NNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 125 GTQLAepFRIHRGM---SAKQARVEAIAlmARVGIPEPESRadsYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALD 201
Cdd:TIGR01277 88 RQNIG--LGLHPGLklnAEQQEKVVDAA--QQVGIADYLDR---LPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1993389136 202 VTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNV 248
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-248 |
1.02e-20 |
|
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: 87.66 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVdlRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVT-AKTKV 98
Cdd:cd03246 1 LEVENVSF--RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP----TSGRVRLDGADISQwDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAAtelaiVFQDALtaLNPvytvGTqLAEpfrihrgmsakqarveAIalmarvgipepesradsyphqFSGGMRQRL 178
Cdd:cd03246 75 GDHVGY-----LPQDDE--LFS----GS-IAE----------------NI---------------------LSGGQRQRL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAeEADRVAIMYAGNV 248
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
40-252 |
1.05e-20 |
|
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: 89.21 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDL--VTAKTkVRRTIAatelaIVFQDalTA 117
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDIreVTLDS-LRRAIG-----VVPQD--TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 L-NPvyTVGtqlaepFRIHRG-MSAKQARVEAIALMARVGiPEPESRADSYPHQ-------FSGGMRQRLLIAMAVALSP 188
Cdd:cd03253 86 LfND--TIG------YNIRYGrPDATDEEVIEAAKAAQIH-DKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKEL---RTehdmaVVLITHDLALVAeEADRVAIMYAGNVVETG 252
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVskgRT-----TIVIAHRLSTIV-NADKIIVLKDGRIVERG 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-262 |
1.05e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 35 VIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAatelaIVFqda 114
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVP----TSGEVRVLGYVPFKRRKEFARRIG-----VVF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 ltalnpvytvG--TQL------AEPFRIHR---GMSAKQARvEAIALMarVGIPEPESRADSYPHQFSGGMRQRLLIAMA 183
Cdd:COG4586 102 ----------GqrSQLwwdlpaIDSFRLLKaiyRIPDAEYK-KRLDEL--VELLDLGELLDTPVRQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 184 VALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV---FGS 260
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELkerFGP 248
|
..
gi 1993389136 261 PR 262
Cdd:COG4586 249 YK 250
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
39-260 |
1.27e-20 |
|
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: 89.37 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditGGSVE-----MGDVDLvtakTKVRRTI--AATELAIVF 111
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY---GNDVRlfgerRGGEDV----WELRKRIglVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QDALTALNPVYT-----VGtqlaepfrIHRGMSAKQARvEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:COG1119 92 PRDETVLDVVLSgffdsIG--------LYREPTDEQRE-RARELLELLGL---AHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGS 260
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
34-252 |
1.38e-20 |
|
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: 88.43 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATELAIVFqD 113
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKP----DSGEITFDGKSYQKNIEALRRIGALIEAPGFY-P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 ALTALnpvytvgtqlaEPFRIH-RGMSAKQARVEAIalMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:cd03268 86 NLTAR-----------ENLRLLaRLLGIRKKRIDEV--LDVVGL---KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-243 |
1.45e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGD---VDLVTAKTKVRRTIAATELAIVfqda 114
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP----TSGTVRRAGgarVAYVPQRSEVPDSLPLTVRDLV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 ltalnpvyTVGT-QLAEPFRIHRgmsaKQARVEAIALMARVGIPEPESRADSyphQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:NF040873 79 --------AMGRwARRGLWRRLT----RDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAeEADRVAIM 243
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-266 |
1.64e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.77 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDLVTAKTKVRRTIAA--TELAIVFQDAlt 116
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKT----TFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEfrRRVGMLFQRP-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 alNPV-YTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIPEP-ESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLAD 194
Cdd:PRK14271 111 --NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 195 EPTTALDVTVQAQIMALLKELRTEhdMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYT 266
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-260 |
1.83e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.68 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 15 TGSVALDVRGLTVDLRTPSGvIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLepIADiTGGSVeMGDVDLVTA 94
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFE-FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI--ISE-TGQTI-VGDYAIPAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRRTI-AATELAIVFQdaltalNPVYTVGTQLAE------PfrIHRGMSAKQARVEAIALMARVGIPEpeSRADSYP 167
Cdd:PRK13645 79 LKKIKEVKrLRKEIGLVFQ------FPEYQLFQETIEkdiafgP--VNLGENKQEAYKKVPELLKLVQLPE--DYVKRSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 168 HQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGN 247
Cdd:PRK13645 149 FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
250
....*....|...
gi 1993389136 248 VVETGLVSEVFGS 260
Cdd:PRK13645 229 VISIGSPFEIFSN 241
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
44-280 |
2.67e-20 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 87.98 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 44 FSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAATELAIVFqdALTALNPVYT 123
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPP----AKGTVKVAGASPGKGWRHIGYVPQRHEFAWDF--PISVAHTVMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 124 VGTQLAEPFRihRGMSAKQARVEAIalMARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVT 203
Cdd:TIGR03771 75 GRTGHIGWLR--RPCVADFAAVRDA--LRRVGLTE---LADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 204 VQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVaIMYAGNVVETGLVSEVFGSPRHPYTKGLLDSVPVHAVRG 280
Cdd:TIGR03771 148 TQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGVSDSSPLLRIVG 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-262 |
3.27e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVr 99
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSARA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 rtiAATELAIVFQDALTALNpvYTVGTQLAEPFRIHRGM-----SAKQARVEAIalMARVGIpepESRADSYPHQFSGGM 174
Cdd:PRK09536 75 ---ASRRVASVPQDTSLSFE--FDVRQVVEMGRTPHRSRfdtwtETDRAAVERA--MERTGV---AQFADRPVTSLSGGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLV 254
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
....*...
gi 1993389136 255 SEVFGSPR 262
Cdd:PRK09536 224 ADVLTADT 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-261 |
3.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 10 SARPDTGSVALDVRGLTV--DLRTPSGvIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEP------IADITG 81
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCvfDEKQENE-LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkygtiqVGDIYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 G---SVEMGDVDLVTAKTK----VRRTIAatelaIVFQdaltalNPVYTVGTQLAE------PfrIHRGMSAKQARVEAI 148
Cdd:PRK13631 91 GdkkNNHELITNPYSKKIKnfkeLRRRVS-----MVFQ------FPEYQLFKDTIEkdimfgP--VALGVKKSEAKKLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 149 ALMARVGIPEPesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITH 228
Cdd:PRK13631 158 FYLNKMGLDDS--YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITH 234
|
250 260 270
....*....|....*....|....*....|...
gi 1993389136 229 DLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK13631 235 TMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-252 |
4.75e-20 |
|
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: 86.78 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 48 RGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKtkvrrtIAATELAIVFQD--ALTALNPVYTVG 125
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETP----QSGRVLINGVDVTAAP------PADRPVSMLFQEnnLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 126 TQLAEPFRIHrgmSAKQARVEAIAlmARVGIPEPESRAdsyPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQ 205
Cdd:cd03298 93 LGLSPGLKLT---AEDRQAIEVAL--ARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1993389136 206 AQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-257 |
9.41e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVrrtiaATEL--AIVF 111
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINNINYNKLDHKL-----AAQLgiGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 Q-----DALTALNPVYtVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVAL 186
Cdd:PRK09700 87 QelsviDELTVLENLY-IGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-252 |
1.11e-19 |
|
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: 86.10 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 16 GSVALDvrglTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAK 95
Cdd:cd03245 1 GRIEFR----NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKP----TSGSVLLDGTDIRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 96 TKVRRTiaatELAIVFQDaltalnPVYTVGT-----QLAEPFrihrgmsAKQARVEAIALMARVgipepESRADSYPHQF 170
Cdd:cd03245 73 PADLRR----NIGYVPQD------VTLFYGTlrdniTLGAPL-------ADDERILRAAELAGV-----TDFVNKHPNGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 -----------SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTehDMAVVLITHDLALVaEEADR 239
Cdd:cd03245 131 dlqigergrglSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDR 207
|
250
....*....|...
gi 1993389136 240 VAIMYAGNVVETG 252
Cdd:cd03245 208 IIVMDSGRIVADG 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
38-252 |
1.42e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.67 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIAatelaivfqdalta 117
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP----QQGEITLDGVPVSDLEKALSSLIS-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 lnpvytVGTQlaepfRIHrgmsakqarVEAIALMARVGIpepesradsyphQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:cd03247 79 ------VLNQ-----RPY---------LFDTTLRNNLGR------------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 198 TALDVTVQAQIMALL-KELRtehDMAVVLITHDLALVaEEADRVAIMYAGNVVETG 252
Cdd:cd03247 127 VGLDPITERQLLSLIfEVLK---DKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
37-261 |
2.06e-19 |
|
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: 85.67 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTA--KTKVRRTIA--ATElAIVFQ 112
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKP----DSGKILLDGQDITKLpmHKRARLGIGylPQE-ASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 113 DaltalnpvYTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:cd03218 89 K--------LTVEENILAVLEIR-GLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELRtEHDMAvVLIT-HDLALVAEEADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILK-DRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-262 |
2.59e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 85.42 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKT--K 97
Cdd:COG0410 4 LEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP----RSGSIRFDGEDITGLPPhrI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 98 VRRTIA-ATELAIVFQDaLTalnpVY---TVGTqlaepfRIHRGMSAKQARVEAI-ALMarvgiPEPESRADSYPHQFSG 172
Cdd:COG0410 76 ARLGIGyVPEGRRIFPS-LT----VEenlLLGA------YARRDRAEVRADLERVyELF-----PRLKERRRQRAGTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 173 GMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
250
....*....|
gi 1993389136 253 LVSEVFGSPR 262
Cdd:COG0410 219 TAAELLADPE 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-261 |
8.05e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 25 LTVDLRTPSgviravdnvtfsarRGETlALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV-----R 99
Cdd:PRK11144 15 LTVNLTLPA--------------QGIT-AIFGRSGAGKTSLINAISGLTRP----QKGRIVLNGRVLFDAEKGIclppeK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAatelaIVFQDAltALNPVYTVGTQLaepfriHRGMsAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLL 179
Cdd:PRK11144 76 RRIG-----YVFQDA--RLFPHYKVRGNL------RYGM-AKSMVAQFDKIVALLGI---EPLLDRYPGSLSGGEKQRVA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFG 259
Cdd:PRK11144 139 IGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWA 218
|
..
gi 1993389136 260 SP 261
Cdd:PRK11144 219 SS 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
41-252 |
1.07e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTiaatELAIVFQDaltalnP 120
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP----TGGQVLLDGVPLVQYDHHYLHR----QVALVGQE------P 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 121 VYTVGTqlaepFR--IHRGM-SAKQARVEAIALMARVG--IPEPESRADSY--PH--QFSGGMRQRLLIAMAVALSPSVL 191
Cdd:TIGR00958 565 VLFSGS-----VRenIAYGLtDTPDEEIMAAAKAANAHdfIMEFPNGYDTEvgEKgsQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 192 LADEPTTALDvtvqAQIMALLKELRTEHDMAVVLITHDLALVaEEADRVAIMYAGNVVETG 252
Cdd:TIGR00958 640 ILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
37-262 |
1.28e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAK---TKVRRTIA--ATElAIVF 111
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKP----DSGRIFLDGED-ITHLpmhKRARLGIGylPQE-ASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QDaLTALNPVYTVgtqlAEpfriHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:COG1137 91 RK-LTVEDNILAV----LE----LRKLSKKEREERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 192 LADEPTTALD-VTVqAQIMALLKELRtEHDMAvVLIT-HD----LALVaeeaDRVAIMYAGNVVETGLVSEVFGSPR 262
Cdd:COG1137 159 LLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIG-VLITdHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-252 |
1.37e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 43 TFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvTAKTKVRRTIAatelaIVFQDalTALNPVY 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP----ASGSLTLNGQDH-TTTPPSRRPVS-----MLFQE--NNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 123 TVGTQLAepFRIHRGM---SAKQARVEAIAlmARVGIPEPESRadsYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTA 199
Cdd:PRK10771 87 TVAQNIG--LGLNPGLklnAAQREKLHAIA--RQMGIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 200 LDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
38-252 |
1.54e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 83.30 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTA-KTKVRRtiaatELAIVFQDALT 116
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP----ENGRVLVDGHDLALAdPAWLRR-----QVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 aLNPVYTVGTQLAEPfrihrGMSAKqaRVEAIALMARVG--IPE-PESRADSYPHQ---FSGGMRQRLLIAMAVALSPSV 190
Cdd:cd03252 88 -FNRSIRDNIALADP-----GMSME--RVIEAAKLAGAHdfISElPEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 191 LLADEPTTALDVTVQAQIMALLKEL---RTehdmaVVLITHDLALVaEEADRVAIMYAGNVVETG 252
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDIcagRT-----VIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-252 |
1.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 26 TVDLRTPSgVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSV----------------EMGDV 89
Cdd:PRK13651 11 IFNKKLPT-ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLP----DTGTIewifkdeknkkktkekEKVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 90 DLVTAKTKVRRTIAATEL----AIVFQDAltalnpVYTVGTQLAE------PfrIHRGMSAKQARVEAIALMARVGIpeP 159
Cdd:PRK13651 86 KLVIQKTRFKKIKKIKEIrrrvGVVFQFA------EYQLFEQTIEkdiifgP--VSMGVSKEEAKKRAAKYIELVGL--D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 160 ESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrteHDMA--VVLITHDLALVAEEA 237
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL---NKQGktIILVTHDLDNVLEWT 232
|
250
....*....|....*
gi 1993389136 238 DRVAIMYAGNVVETG 252
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
39-240 |
4.63e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditggsvemGDVDLVTAKTKVRRTIAATELAIVFQdaLTAL 118
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA---------GSISLCGEPVPSRARHARQRVGVVPQ--FDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQLaEPFRIHRGMSAKQARVEAIALM--ARVgipepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:PRK13537 92 DPDFTVRENL-LVFGRYFGLSAAAARALVPPLLefAKL-----ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEhDMAVVLITHDLalvaEEADRV 240
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFM----EEAERL 204
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-249 |
6.10e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.06 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlVTAKTKVRRtiaATELAIVFQDAL- 115
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP----DSGSILIDGKD-VTKLPEYKR---AKYIGRVFQDPMm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 -TAlnPVYTVGTQLA------EPFRIHRGMSAKQaRVEAIALMARVGIpEPESRADSYPHQFSGGMRQRLLIAMAVALSP 188
Cdd:COG1101 92 gTA--PSMTIEENLAlayrrgKRRGLRRGLTKKR-RELFRELLATLGL-GLENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDL--ALvaEEADRVAIMYAGNVV 249
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
27-248 |
1.44e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGviravdnvtfsarrgETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRrtiaate 106
Cdd:PRK11247 31 LDLHIPAG---------------QFVAVVGRSGCGKSTLLRLLAGLETP----SAGELLAGTAPLAEAREDTR------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 107 laIVFQDAltALNP----VYTVGTQLaepfrihRGmsakQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAM 182
Cdd:PRK11247 85 --LMFQDA--RLLPwkkvIDNVGLGL-------KG----QWRDAALQALAAVGL---ADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 183 AVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNV 248
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-261 |
1.84e-17 |
|
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: 79.76 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 13 PDTGSValDVRGLTVdlRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLV 92
Cdd:cd03369 2 PEHGEI--EVENLSV--RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA----EEGKIEIDGIDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 93 TAK-TKVRRTiaateLAIVFQDaltalnPVYTVGTqlaepFRIHRGMSAKQARVEaiaLMARVGIPEPESradsyphQFS 171
Cdd:cd03369 74 TIPlEDLRSS-----LTIIPQD------PTLFSGT-----IRSNLDPFDEYSDEE---IYGALRVSEGGL-------NLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 172 GGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTehDMAVVLITHDLALVAeEADRVAIMYAGNVVEt 251
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTII-DYDKILVMDAGEVKE- 203
|
250
....*....|
gi 1993389136 252 glvsevFGSP 261
Cdd:cd03369 204 ------YDHP 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-252 |
1.97e-17 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 79.96 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTiaatELAIVFQDalta 117
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP----QKGQILIDGIDIRDISRKSLRS----MIGVVLQD---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 lnPVYTVGTqLAEPFRIHRgMSAKQARVEAIAlmARVGI-PEPESRADSYPHQ-------FSGGMRQRLLIAMAVALSPS 189
Cdd:cd03254 86 --TFLFSGT-IMENIRLGR-PNATDEEVIEAA--KEAGAhDFIMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITHDLALVaEEADRVAIMYAGNVVETG 252
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-262 |
2.90e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.03 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDL------VT 93
Cdd:PRK11300 6 LSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP----TGGTILLRGQHIeglpghQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 94 AKTKVRRTIAATELaivFQDaLTAL-NPVYTVGTQLAEPFriHRGM----SAKQARVEAIALMA----RVGIPEPESRAD 164
Cdd:PRK11300 78 ARMGVVRTFQHVRL---FRE-MTVIeNLLVAQHQQLKTGL--FSGLlktpAFRRAESEALDRAAtwleRVGLLEHANRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 165 ---SYPHQfsggmrQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVA 241
Cdd:PRK11300 152 gnlAYGQQ------RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
250 260
....*....|....*....|.
gi 1993389136 242 IMYAGNVVETGLVSEVFGSPR 262
Cdd:PRK11300 226 VVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-261 |
3.65e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 17 SVALDVRGLTvdlRTPSGVIrAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditggsvemGDVDLVTAKT 96
Cdd:PRK13536 39 TVAIDLAGVS---KSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA---------GKITVLGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 97 KVRRTIAATELAIVFQdaLTALNPVYTVGTQLAePFRIHRGMSAKQ--ARVEAIALMARVgipepESRADSYPHQFSGGM 174
Cdd:PRK13536 106 PARARLARARIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTREieAVIPSLLEFARL-----ESKADARVSDLSGGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHdlalVAEEA----DRVAIMYAGNVVE 250
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTH----FMEEAerlcDRLCVLEAGRKIA 252
|
250
....*....|....*
gi 1993389136 251 TG----LVSEVFGSP 261
Cdd:PRK13536 253 EGrphaLIDEHIGCQ 267
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-230 |
6.60e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 81.64 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 3 APATSAPSARP-DTGSVALDVRGLTVdlRTPsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIaditG 81
Cdd:TIGR02868 317 VAEGSAPAAGAvGLGKPTLELRDLSA--GYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL----Q 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 82 GSVEMGDVDLVTAK-TKVRRTIAATElaivfQDAltalnpvYTVGTQLAEPFRIHRGMSAKQarvEAIALMARVGIPEPe 160
Cdd:TIGR02868 390 GEVTLDGVPVSSLDqDEVRRRVSVCA-----QDA-------HLFDTTVRENLRLARPDATDE---ELWAALERVGLADW- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 161 srADSYPH-----------QFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLkeLRTEHDMAVVLITHD 229
Cdd:TIGR02868 454 --LRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
.
gi 1993389136 230 L 230
Cdd:TIGR02868 530 L 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-257 |
7.24e-17 |
|
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: 81.39 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGL--LEPIA-------------------- 77
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSgriiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 78 ------DITGGSVEMGDVDLVTAKTKVRRTIAaTELAIVFQDALtALNPVYTVGTQLAEPFRiHRGMSAKQARVEAIALM 151
Cdd:TIGR03269 77 kvgepcPVCGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 152 ARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLA 231
Cdd:TIGR03269 154 EMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 1993389136 232 LVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
34-261 |
1.25e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.89 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadITGGSVEMGDVDLVTAKTKVRrtiaatELAIVFQD 113
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLER----ITSGEIWIGGRVVNELEPADR------DIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 alTALNPVYTVGTQLAEPFRIhRGMSAKQ--ARVEAIAlmarvGIPEPESRADSYPHQFSGGMRQRllIAMAVAL--SPS 189
Cdd:PRK11650 85 --YALYPHMSVRENMAYGLKI-RGMPKAEieERVAEAA-----RILELEPLLDRKPRELSGGQRQR--VAMGRAIvrEPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 190 VLLADEPTTALD----VTVQAQIMALLKELRTehdmAVVLITHD----LALvaeeADRVAIMYAGNVVETGLVSEVFGSP 261
Cdd:PRK11650 155 VFLFDEPLSNLDaklrVQMRLEIQRLHRRLKT----TSLYVTHDqveaMTL----ADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-261 |
1.94e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLRtpsgviraVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiaditGGSVEMGDVDLvtaktkvr 99
Cdd:COG4138 1 LQLNDVAVAGR--------LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-----QGEILLNGRPL-------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELA-----IVFQDALTALNPVYtvgtQLaepfrIHRGMSAKQARVEAIALMA----RVGIpepesrADSYP--- 167
Cdd:COG4138 60 SDWSAAELArhrayLSQQQSPPFAMPVF----QY-----LALHQPAGASSEAVEQLLAqlaeALGL------EDKLSrpl 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 168 HQFSGGMRQRLLIAmAVAL--SPSV------LLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADR 239
Cdd:COG4138 125 TQLSGGEWQRVRLA-AVLLqvWPTInpegqlLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADR 202
|
250 260 270
....*....|....*....|....*....|.
gi 1993389136 240 VAIMYAGNVVETG---------LVSEVFGSP 261
Cdd:COG4138 203 VWLLKQGKLVASGetaevmtpeNLSEVFGVK 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-252 |
2.41e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.93 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiADITGGSVEMGDVDLvtAKTKVRRTIAATELAIVFQDALT 116
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG-GGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYtvgtqLAEPFRIHRGMSAKQAR-VEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADE 195
Cdd:cd03234 98 VRETLT-----YTAILRLPRKSSDAIRKkRVEDVLLRDLAL---TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 196 PTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
37-255 |
2.74e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVE-MGDVdlVTAKTK--VRrtiaaTELAIVFQD 113
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLP----QRGRVKvMGRE--VNAENEkwVR-----SKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 ------ALTALNPVyTVGTQlaepfriHRGMSAKQ--ARVEAiALMArVGIPEPESRAdsyPHQFSGGMRQRLLIAMAVA 185
Cdd:PRK13647 88 pddqvfSSTVWDDV-AFGPV-------NMGLDKDEveRRVEE-ALKA-VRMWDFRDKP---PYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 186 LSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVS 255
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-252 |
8.27e-16 |
|
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: 74.87 E-value: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLlePIADITGGSVEMGDVDLVTAKTKVR 99
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 rtiAATELAIVFQdaltalnpvytvgtqlaEPFRIHrGMSakqarveaIALMAR---VGipepesradsyphqFSGGMRQ 176
Cdd:cd03217 75 ---ARLGIFLAFQ-----------------YPPEIP-GVK--------NADFLRyvnEG--------------FSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITH-DLALVAEEADRVAIMYAGNVVETG 252
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-246 |
9.95e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVALDVRGLTV-DLRTPSgvIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiaditgGSVEmG 87
Cdd:PRK13549 249 PREPHTIGEVILEVRNLTAwDPVNPH--IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP-------GRWE-G 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 88 DVDLVTAKTKVRRTIAATELAIVF------QDALTalnPVYTVG--------TQLAEPFRIHRGMSAKQARvEAIALMaR 153
Cdd:PRK13549 319 EIFIDGKPVKIRNPQQAIAQGIAMvpedrkRDGIV---PVMGVGknitlaalDRFTGGSRIDDAAELKTIL-ESIQRL-K 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 154 VGIPEPESRADSyphqFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDLALV 233
Cdd:PRK13549 394 VKTASPELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEV 468
|
250
....*....|...
gi 1993389136 234 AEEADRVAIMYAG 246
Cdd:PRK13549 469 LGLSDRVLVMHEG 481
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-252 |
1.15e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVdlrtpsgvirAVD------NVTFSARRGETLALLGESGCGKSMTAQAIVGLlePIADITGGSVEMGDVDLVT 93
Cdd:COG0396 1 LEIKNLHV----------SVEgkeilkGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSILLDGEDILE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 94 AKTKVRrtiAATELAIVFQdaltalNPVYTVGTQLAEPFRI----HRG--MSAKQARVEAIALMARVGIPEpeSRADSYP 167
Cdd:COG0396 69 LSPDER---ARAGIFLAFQ------YPVEIPGVSVSNFLRTalnaRRGeeLSAREFLKLLKEKMKELGLDE--DFLDRYV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 168 HQ-FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVqAQIMA-LLKELRTEhDMAVVLITHDLALVAE-EADRVAIMY 244
Cdd:COG0396 138 NEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHYQRILDYiKPDFVHVLV 215
|
....*...
gi 1993389136 245 AGNVVETG 252
Cdd:COG0396 216 DGRIVKSG 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
41-256 |
1.16e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiaditgGSVEMGDVDL----VTAKTKVRRTiaatelAIVFQDALt 116
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK------GVKGSGSVLLngmpIDAKEMRAIS------AYVQQDDL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 aLNPVYTVGTQL---AEpFRIHRGMSAKQ--ARVEAIALM--------ARVGIPEPESradsyphQFSGGMRQRLLIAMA 183
Cdd:TIGR00955 110 -FIPTLTVREHLmfqAH-LRMPRRVTKKEkrERVDEVLQAlglrkcanTRIGVPGRVK-------GLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 184 VALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSE 256
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-258 |
1.40e-15 |
|
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: 77.48 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVdlrTPSGVIRAV-DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaktkv 98
Cdd:COG4618 331 LSVENLTV---VPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP----TAGSVRLDGADL------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 rRTIAATELAIVF----QDalTALNPvytvGTqLAEpfRIHRGMSAKQARVEAIALMARV-----GIPEP-ESRADSYPH 168
Cdd:COG4618 397 -SQWDREELGRHIgylpQD--VELFD----GT-IAE--NIARFGDADPEKVVAAAKLAGVhemilRLPDGyDTRIGEGGA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 169 QFSGGMRQRllIAMAVAL--SPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAeEADRVAIMYAG 246
Cdd:COG4618 467 RLSGGQRQR--IGLARALygDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLA-AVDKLLVLRDG 542
|
250
....*....|..
gi 1993389136 247 NVVETGLVSEVF 258
Cdd:COG4618 543 RVQAFGPRDEVL 554
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
39-250 |
2.48e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGdvdlvtakTKVRrtiaateLAIVFQDaLTAL 118
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP----DSGTVKLG--------ETVK-------IGYFDQH-QEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVgtqLAEpfrIHRGMSAKQaRVEAIALMARVGIPePEsRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTT 198
Cdd:COG0488 391 DPDKTV---LDE---LRDGAPGGT-EQEVRGYLGRFLFS-GD-DAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 199 ALDV-TVQAQIMALLkelrtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVE 250
Cdd:COG0488 462 HLDIeTLEALEEALD-----DFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-267 |
2.64e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADI-TGGSVEMGDVDLVTAKTKVRRTiaATELAIVFQDAl 115
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrVEGRVEFFNQNIYERRVNLNRL--RRQVSMVHPKP- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 tALNPVyTVGTQLAEPFRIhRGMSAK---QARVEAiALMARVGIPEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:PRK14258 98 -NLFPM-SVYDNVAYGVKI-VGWRPKleiDDIVES-ALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYA-----GNVVETGLVSEVFGSPRHPYTK 267
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-246 |
2.87e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 25 LTVDLRTPSGVIravdNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRrtiaa 104
Cdd:PRK15439 269 LTVEDLTGEGFR----NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA----RGGRIMLNGKEINALSTAQR----- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 105 TELAIV-----------FQDALTALNPV-YTVGTQlaePFRIHRGmsAKQARVEAI--ALMARVGIPEPESRAdsyphqF 170
Cdd:PRK15439 336 LARGLVylpedrqssglYLDAPLAWNVCaLTHNRR---GFWIKPA--RENAVLERYrrALNIKFNHAEQAART------L 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-251 |
1.04e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEPIaditgGSVEmGDVdLVTAKTKVRRTIAATE---LAIV 110
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKS-TLMKVLSGVYPH-----GTYE-GEI-IFEGEELQASNIRDTEragIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 111 FQDalTALNPVYTVGTQL---AEPFRIHRgMSAKQARVEAIALMARVGIP-EPESRADSYphqfSGGMRQRLLIAMAVAL 186
Cdd:PRK13549 88 HQE--LALVKELSVLENIflgNEITPGGI-MDYDAMYLRAQKLLAQLKLDiNPATPVGNL----GLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVET 251
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-251 |
1.13e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.44 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTvdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEPIaditgGSVEmGDVDLvtaKTKVR 99
Cdd:NF040905 2 LEMRGIT---KTFPGV-KALDDVNLSVREGEIHALCGENGAGKS-TLMKVLSGVYPH-----GSYE-GEILF---DGEVC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 --RTIAATE---LAIVFQDalTALNPVYTVGTQLaepF----RIHRG-MSAKQARVEAIALMARVGIPE-PESRADSYph 168
Cdd:NF040905 68 rfKDIRDSEalgIVIIHQE--LALIPYLSIAENI---FlgneRAKRGvIDWNETNRRARELLAKVGLDEsPDTLVTDI-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 169 qfsgGMRQRLLIAMAVALSPSV--LLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:NF040905 141 ----GVGKQQLVEIAKALSKDVklLILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADSITVLRDG 215
|
....*
gi 1993389136 247 NVVET 251
Cdd:NF040905 216 RTIET 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-267 |
1.14e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 24 GLTVDLRTPS-----GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPI------ADIT--GGSVEMGDVD 90
Cdd:PRK14243 6 GTETVLRTENlnvyyGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrveGKVTfhGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 91 LVtaktKVRRTIAatelaIVFQDAltalNPV-YTVGTQLAEPFRIHrGMSAKQARVEAIALMARVGIPEPESRADSYPHQ 169
Cdd:PRK14243 86 PV----EVRRRIG-----MVFQKP----NPFpKSIYDNIAYGARIN-GYKGDMDELVERSLRQAALWDEVKDKLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLalvaEEADRVAIMYA---- 245
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM----QQAARVSDMTAffnv 225
|
250 260 270
....*....|....*....|....*....|.
gi 1993389136 246 ---------GNVVETGLVSEVFGSPRHPYTK 267
Cdd:PRK14243 226 eltegggryGYLVEFDRTEKIFNSPQQQATR 256
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
37-265 |
1.54e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.35 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLlepiadITGGSVEMGDVDLVTAKTK--------VRRTIAATelA 108
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLGRTVQregrlardIRKSRANT--G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 109 IVFQ-----DALTALNPVYtVGTQLAEPF-RIHRGMSAKQARVEAIALMARVGIPEpesradsYPHQ----FSGGMRQRL 178
Cdd:PRK09984 90 YIFQqfnlvNRLSVLENVL-IGALGSTPFwRTCFSWFTREQKQRALQALTRVGMVH-------FAHQrvstLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 179 LIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGlVSEVF 258
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG-SSQQF 240
|
....*....
gi 1993389136 259 GSPR--HPY 265
Cdd:PRK09984 241 DNERfdHLY 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-258 |
1.91e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLRTPSGVIRavdNVTFSARRGETLALLGESGCGKSMTAQAIVGLlepiaditggsVEMGDVDLVTAKTKV 98
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGF-----------VRLASGKISILGQPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAATELAIVFQDALTALN-PVYTVGTQLAEPFRiHRGM---SAKQARVEAIALMARVGIPEPESRADSyphQFSGGM 174
Cdd:PRK15056 72 RQALQKNLVAYVPQSEEVDWSfPVLVEDVVMMGRYG-HMGWlrrAKKRDRQIVTAALARVDMVEFRHRQIG---ELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVlITHDLALVAEEADrVAIMYAGNVVETGLV 254
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCD-YTVMVKGTVLASGPT 225
|
....
gi 1993389136 255 SEVF 258
Cdd:PRK15056 226 ETTF 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
38-252 |
1.96e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDLVTAK-TKVRRTIAATELAI-VFQDAL 115
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKS----TIANLLTRFYDIDEGEILLDGHDLRDYTlASLRNQVALVSQNVhLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 tALNPVYTVGTQLAepfrihrgmsakQARVEAIALMARVG--IPEPESRADSYPHQ----FSGGMRQRLLIAMAVALSPS 189
Cdd:PRK11176 434 -ANNIAYARTEQYS------------REQIEEAARMAYAMdfINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 190 VLLADEPTTALDVTVQAQIMALLKELRTehDMAVVLITHDLALVaEEADRVAIMYAGNVVETG 252
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
27-229 |
2.11e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIraVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTiaate 106
Cdd:PRK10247 13 VGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP----TSGTLLFEGEDISTLKPEIYRQ----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 107 laivfQDALTALNPVY---TVGTQLAEPFRIhRGMSAKQARVeaIALMARVGIpePESRADSYPHQFSGGMRQRLLIAMA 183
Cdd:PRK10247 82 -----QVSYCAQTPTLfgdTVYDNLIFPWQI-RNQQPDPAIF--LDDLERFAL--PDTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1993389136 184 VALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHD 229
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-256 |
2.17e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVALDVRGLTV-DLRTPSgvIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADitgGSVEMG 87
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLTCwDVINPH--RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFE---GNVFIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 88 --DVDLVTAKTKVRRTIA-----------ATELAIVFQDALTALNPvYTVGTQL---AEPFRIHRGMsaKQARVEAIALM 151
Cdd:TIGR02633 322 gkPVDIRNPAQAIRAGIAmvpedrkrhgiVPILGVGKNITLSVLKS-FCFKMRIdaaAELQIIGSAI--QRLKVKTASPF 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 152 ARVGipepesradsyphQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLA 231
Cdd:TIGR02633 399 LPIG-------------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELA 464
|
250 260
....*....|....*....|....*....
gi 1993389136 232 LVAEEADRVAIMYAG----NVVETGLVSE 256
Cdd:TIGR02633 465 EVLGLSDRVLVIGEGklkgDFVNHALTQE 493
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
40-257 |
2.31e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEM-GDVDLVTAKTKVRRTIAatelaIVFQDALTAL 118
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH----GHVWLdGEHIQHYASKEVARRIG-----LLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NpvYTVGTQLAEPFRIHRGMSAKQARVEAIAL---MARVGIPEpesRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADE 195
Cdd:PRK10253 95 D--ITVQELVARGRYPHQPLFTRWRKEDEEAVtkaMQATGITH---LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 196 PTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-247 |
2.63e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMG----------DVDLVTAKTkVRRTI--AATEL 107
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEP----DSGEVSIPkglrigylpqEPPLDDDLT-VLDTVldGDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 108 AivfqDALTALNPVYTvgtQLAEPFRIHRGMSAKQARVEAI----------ALMARVGIPEPESRADsyPHQFSGGMRQR 177
Cdd:COG0488 90 R----ALEAELEELEA---KLAEPDEDLERLAELQEEFEALggweaearaeEILSGLGFPEEDLDRP--VSELSGGWRRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 178 LLIAMAVALSPSVLLADEPTTALDvtVQAqIMALLKELRTeHDMAVVLITHDLALVAEEADRVA-------IMYAGN 247
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKN-YPGTVLVVSHDRYFLDRVATRILeldrgklTLYPGN 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
146-290 |
4.63e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 146 EAIALmarVGI-PEPESRADSyphqFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVV 224
Cdd:PRK10575 130 EAISL---VGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVI 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 225 LITHDLALVAEEADRVAIMYAGNVVETGlvsevfgsprhpytkglldsVPVHAVRGEDLKSIGGTP 290
Cdd:PRK10575 203 AVLHDINMAARYCDYLVALRGGEMIAQG--------------------TPAELMRGETLEQIYGIP 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-252 |
5.50e-14 |
|
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: 73.12 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVRRTIA-ATELAIVFQDALT 116
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKDIETNLDAVRQSLGmCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTvgTQLaepfrihRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:TIGR01257 1021 AEHILFY--AQL-------KGRSWEEAQLEMEAMLEDTGL---HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
41-248 |
5.53e-14 |
|
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: 70.19 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDLVTAKTK-VRRTIAA-TELAIVFQDALTAl 118
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLvGQEPVLFARSLQD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQlaePFrihrgMSAKQARVEA-----IALMARvgipEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLA 193
Cdd:cd03248 107 NIAYGLQSC---SF-----ECVKEAAQKAhahsfISELAS----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 194 DEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVaEEADRVAIMYAGNV 248
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-284 |
5.84e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLlepiADITGGSVEMGDV---DLVTAKTKVrrtiaatelAIVFQDalTA 117
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL----EDITSGDLFIGEKrmnDVPPAERGV---------GMVFQS--YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTV------GTQLAEPFRIHRgmsakQARVEAIALMARVGipepeSRADSYPHQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:PRK11000 86 LYPHLSVaenmsfGLKLAGAKKEEI-----NQRVNQVAEVLQLA-----HLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 192 LADEPTTALD----VTVQAQIMALLKELRTehdmAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVFGSPRHPYTK 267
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
|
250 260
....*....|....*....|....
gi 1993389136 268 GLLDS-------VPVHAVRGEDLK 284
Cdd:PRK11000 232 GFIGSpkmnflpVKVTATAIEQVQ 255
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
37-240 |
5.97e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvdlvtaktkvrrtiaatELAIVFQDALT 116
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAP----DEGVIKRNG-----------------KLRIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPvyTVGTQLAEPFRIHRGMSAKQ-----ARVEAIALMarvgipepesradSYPHQ-FSGGMRQRLLIAMAVALSPSV 190
Cdd:PRK09544 77 YLDT--TLPLTVNRFLRLRPGTKKEDilpalKRVQAGHLI-------------DAPMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1993389136 191 LLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRV 240
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
19-257 |
7.21e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.69 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 19 ALDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAqaivgLLEPIADITGGSVEMGDVDLVTAKTKV 98
Cdd:NF000106 13 AVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-----LPAHV*GPDAGRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTIAATE-LAIVFQDALTALNPVYTVGTQLaepfrihrGMSAKQARVEAIALMARVGIPEPESRADSyphQFSGGMRQR 177
Cdd:NF000106 84 RRTIG*HRpVR*GRRESFSGRENLYMIGR*L--------DLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 178 LLIAMAVALSPSVLLADEPTTALDVTVQAQIMallKELRTE-HDMAVVLITHDLALVAEE-ADRVAIMYAGNVVETGLVS 255
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW---DEVRSMvRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVD 229
|
..
gi 1993389136 256 EV 257
Cdd:NF000106 230 EL 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
38-293 |
7.58e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDL--VTAKTKVRRTIaatelAIVFQDAL 115
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK----GKVLVSGIDTgdFSKLQGIRKLV-----GIVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 TALnpvytVGTQLAEPFrihrGMSAKQARVEAIALMARVGIPEPESRADSY----PHQFSGGMRQRLLIAMAVALSPSVL 191
Cdd:PRK13644 88 TQF-----VGRTVEEDL----AFGPENLCLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 192 LADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVaEEADRVAIMYAGNVVETGLVSEVFGSPrhpytkglld 271
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV---------- 226
|
250 260
....*....|....*....|..
gi 1993389136 272 svpvhavrgeDLKSIGGTPPDL 293
Cdd:PRK13644 227 ----------SLQTLGLTPPSL 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-249 |
8.75e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 69.12 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 17 SVALDVRGLTVDLRTPSGVIRA--VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAdiTGGSVemgdvdLVTA 94
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEV------LING 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 95 KTKVRRTIAAtELAIVFQDalTALNPVYTVgtqlaepfrihrgmsakqarVEAIALMARV-GIpepesradsyphqfSGG 173
Cdd:cd03213 73 RPLDKRSFRK-IIGYVPQD--DILHPTLTV--------------------RETLMFAAKLrGL--------------SGG 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 174 MRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDL-ALVAEEADRVAIMYAGNVV 249
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
54-258 |
1.38e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 54 LLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKtkvrRTIAA--TELAIVFQDALTALnpVYT-VGTQLAE 130
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRP----QKGAVLWQGKPLDYSK----RGLLAlrQQVATVFQDPEQQI--FYTdIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 131 PFRIHRGMSAKQARV--EAIALMarvgipepesRADSYPHQ----FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTV 204
Cdd:PRK13638 102 SLRNLGVPEAEITRRvdEALTLV----------DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 205 QAQIMALLKELRTEHDMaVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-258 |
1.97e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiADITGGSVEMGDVDLVTAKTKVRRTIA-ATELAIVFQDal 115
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP--RDAGNIIIDDEDISLLPLHARARRGIGyLPQEASIFRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 talnpvYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADE 195
Cdd:PRK10895 93 ------LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 196 PTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEVF 258
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-228 |
2.02e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 1 MSAPATSAPSARPDTGSvALDVRGLTvdLRTPSGVIRaVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLePIADit 80
Cdd:COG4178 345 ADALPEAASRIETSEDG-ALALEDLT--LRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW-PYGS-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 81 gGSVEMGDVDlvtaktkvrrtiaatELAIVFQDA-LtalnPVYTVGTQLAEPfRIHRGMSAKQARveaiALMARVGIPEP 159
Cdd:COG4178 418 -GRIARPAGA---------------RVLFLPQRPyL----PLGTLREALLYP-ATAEAFSDAELR----EALEAVGLGHL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 160 ESRAD---SYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKElrTEHDMAVVLITH 228
Cdd:COG4178 473 AERLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
38-261 |
3.32e-13 |
|
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: 67.90 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtakTKVRRTIAATELAIVFQDalta 117
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL----SSGSILIDGVDI----SKIGLHDLRSRISIIPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 lnPVYTVGTqLAE---PFRIHRGMSAKQArVEAIALMARVGIPEP--ESRADSYPHQFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:cd03244 87 --PVLFSGT-IRSnldPFGEYSDEELWQA-LERVGLKEFVESLPGglDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 193 ADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDLALVAeEADRVAIMYAGNVVEtglvsevFGSP 261
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTII-DSDRILVLDKGRVVE-------FDSP 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-252 |
5.48e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.47 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 8 APSARPDTGSVALDVRGltVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVemg 87
Cdd:PRK11160 327 PTTSTAAADQVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEI--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 88 dvdlvtaktkvrrTIAATELAIVFQDALTALnpvYTVGTQlaepfRIH------RG---MSAKQARVEA-IALMARVGIP 157
Cdd:PRK11160 398 -------------LLNGQPIADYSEAALRQA---ISVVSQ-----RVHlfsatlRDnllLAAPNASDEAlIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 158 ---EPESRADSY----PHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTehDMAVVLITHDL 230
Cdd:PRK11160 457 kllEDDKGLNAWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL 534
|
250 260
....*....|....*....|..
gi 1993389136 231 ALVaEEADRVAIMYAGNVVETG 252
Cdd:PRK11160 535 TGL-EQFDRICVMDNGQIIEQG 555
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-252 |
5.95e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVALDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEP---IADITGGSVE 85
Cdd:NF033858 256 PRPADDDDEPAIEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAsegEAWLFGQPVD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 86 MGDVDlvtaktkVRRTIA--------ATELaivfqdaltalnpvyTVGTQL---AEPFRIHRGMSAkqARVEaiALMARV 154
Cdd:NF033858 332 AGDIA-------TRRRVGymsqafslYGEL---------------TVRQNLelhARLFHLPAAEIA--ARVA--EMLERF 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 155 GIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLAlVA 234
Cdd:NF033858 386 DL---ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMN-EA 461
|
250
....*....|....*...
gi 1993389136 235 EEADRVAIMYAGNVVETG 252
Cdd:NF033858 462 ERCDRISLMHAGRVLASD 479
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-252 |
2.06e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMgDVDLVTAKTKVRRTIAATELAIVFQDAltALN 119
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP----DHGEILF-DGENIPAMSRSRLYTVRKRMSMLFQSG--ALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 120 PVYTVGTQLAEPFRIHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTA 199
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGL---RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 200 LDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETG 252
Cdd:PRK11831 174 QDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
40-252 |
3.26e-12 |
|
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: 67.15 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVDL--VTaKTKVRRTIAatelaIVFQDalTA 117
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKS----TLARLLFRFYDVTSGRILIDGQDIrdVT-QASLRAAIG-----IVPQD--TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 L-NPvyTVGtqlaepFRIHRG-MSAKQARVEAIALMARVG--IpepesraDSYPHQF-----------SGGMRQRLLIAM 182
Cdd:COG5265 443 LfND--TIA------YNIAYGrPDASEEEVEAAARAAQIHdfI-------ESLPDGYdtrvgerglklSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 183 AVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVvlITHDLALVAeEADRVAIMYAGNVVETG 252
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV--IAHRLSTIV-DADEILVLEAGRIVERG 574
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
38-252 |
7.97e-12 |
|
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: 66.30 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIA-DITGGSVEMGDVDlvtaKTKVRRTIAatelaIVFQDalt 116
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSgEILLNGFSLKDID----RHTLRQFIN-----YLPQE--- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 alnPVYTVGTQLAEPFrihrgMSAKQaRVEAIALMARVGIPEPESRADSYPHQF-----------SGGMRQRLLIAMAVa 185
Cdd:TIGR01193 557 ---PYIFSGSILENLL-----LGAKE-NVSQDEIWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARAL- 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 186 LSPS-VLLADEPTTALDVTVQAQImalLKELRTEHDMAVVLITHDLAlVAEEADRVAIMYAGNVVETG 252
Cdd:TIGR01193 627 LTDSkVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQG 690
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
165-240 |
8.77e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 62.08 E-value: 8.77e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 165 SYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTehdmAVVLITHDLALVAEEADRV 240
Cdd:cd03221 66 GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKI 137
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-246 |
1.30e-11 |
|
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: 65.81 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGllepIADITGGSVEMGDVDLVTAKTKVRRTIAATELAIVFQDALTA 117
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG----DTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVGtqlaepfRIhRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPT 197
Cdd:TIGR01257 2030 REHLYLYA-------RL-RGVPAEEIEKVANWSIQSLGL---SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 198 TALDVTVQAQ----IMALLKELRtehdmAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:TIGR01257 2099 TGMDPQARRMlwntIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-251 |
1.57e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTkvRRTIAATeLAIVFQD 113
Cdd:PRK11288 16 GV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP----DAGSILIDGQEMRFAST--TAALAAG-VAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 114 alTALNPVYTVGTQL---AEPFR---IHRgmsaKQARVEAIALMARVGIP-EPESRADSyphqFSGGMRQRLLIAMAVAL 186
Cdd:PRK11288 88 --LHLVPEMTVAENLylgQLPHKggiVNR----RLLNYEAREQLEHLGVDiDPDTPLKY----LSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 187 SPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVVET 251
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
37-257 |
1.57e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLePIADITGGSVEMGDVdlvtaktkvrrTIAATELAIVFQDALT 116
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGAPRGARVTGDV-----------TLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYTVGTQLAEPFRIHR----GMSAKQARVEAIALMARVGIPEPESRADSYP------HQFSGGMRQRLLIAMAVA- 185
Cdd:PRK13547 83 RLRAVLPQAAQPAFAFSAREivllGRYPHARRAGALTHRDGEIAWQALALAGATAlvgrdvTTLSGGELARVQFARVLAq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 186 --------LSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:PRK13547 163 lwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
38-257 |
2.36e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDN----VTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadiTGGSVEMGDVDLvtaktkvrRTIAATELAIVF-- 111
Cdd:PRK03695 7 AVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-----GSGSIQFAGQPL--------EAWSAAELARHRay 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 ---QDALTALNPVYTVgTQLAEPFRIHRGMSAKQAR--VEAIALMARVGIPepesradsyPHQFSGGMRQRLLIAmAVAL 186
Cdd:PRK03695 74 lsqQQTPPFAMPVFQY-LTLHQPDKTRTEAVASALNevAEALGLDDKLGRS---------VNQLSGGEWQRVRLA-AVVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 187 --SPSV------LLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:PRK03695 143 qvWPDInpagqlLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-249 |
4.64e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 12 RP-DTGSVALDVRGLTVD-LRTPsgviravdnVTFSARRGETLALLGESGCGKSMTAQAIVGllepiAD-ITGGSVEMGD 88
Cdd:PRK11288 249 RPrPLGEVRLRLDGLKGPgLREP---------ISFSVRAGEIVGLFGLVGAGRSELMKLLYG-----ATrRTAGQVYLDG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 89 VDLvtaktKVRRTIAATELAIVF------QDALTalnPVYTVGTQLA-------EPFR--IHRGMSAKQARvEAIALMaR 153
Cdd:PRK11288 315 KPI-----DIRSPRDAIRAGIMLcpedrkAEGII---PVHSVADNINisarrhhLRAGclINNRWEAENAD-RFIRSL-N 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 154 VGIPEPESRAdsypHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALV 233
Cdd:PRK11288 385 IKTPSREQLI----MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEV 459
|
250
....*....|....*.
gi 1993389136 234 AEEADRVAIMYAGNVV 249
Cdd:PRK11288 460 LGVADRIVVMREGRIA 475
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-257 |
2.18e-10 |
|
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: 61.59 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 27 VDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtaKTKVRRTIAATe 106
Cdd:TIGR01842 322 VTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP----TSGSVRLDGADL---KQWDRETFGKH- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 107 LAIVFQDalTALNPvYTVGTQLAepfRIHRGMSAkQARVEAiALMARVG--IPEPESRADSY----PHQFSGGMRQRLLI 180
Cdd:TIGR01842 394 IGYLPQD--VELFP-GTVAENIA---RFGENADP-EKIIEA-AKLAGVHelILRLPDGYDTVigpgGATLSGGQRQRIAL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 181 AMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVaEEADRVAIMYAGNVVETGLVSEV 257
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEV 540
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-233 |
2.74e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.91 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDlrtpSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKVR 99
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP----DSGEVRWNGTPLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAatelaivFQDALTALNPVYTVGTQLAEPFRIHRGmsakqARVEAIALMARVGIpepESRADSYPHQFSGGMRQRLL 179
Cdd:TIGR01189 73 ENIL-------YLGHLPGLKPELSALENLHFWAAIHGG-----AQRTIEDALAAVGL---TGFEDLPAAQLSAGQQRRLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKElRTEHDMAVVLITH-DLALV 233
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA-HLARGGIVLLTTHqDLGLV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-233 |
3.64e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGdvdlvtaktkvrrtiaaTELAIVFQDALTA- 117
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQA----DSGRIHCG-----------------TKLEVAYFDQHRAe 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVGTQLAEpfrihrgmsAKQarveaialmaRVGIPEPESRADSYPHQF--------------SGGMRQRLLIAmA 183
Cdd:PRK11147 394 LDPEKTVMDNLAE---------GKQ----------EVMVNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLA-R 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 184 VALSPSVLLA-DEPTTALDVtvqaQIMALLKELRTEHDMAVVLITHDLALV 233
Cdd:PRK11147 454 LFLKPSNLLIlDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-228 |
3.71e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 57.93 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 22 VRGLTvdLRTPSGVIRaVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadITGGSVEMgdvdlvtaktkvrrt 101
Cdd:cd03223 3 LENLS--LATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP----WGSGRIGM--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 102 IAATELAIVFQdaltalNPVYTVGTqlaepFRihrgmsakqarvEAIAlmarvgipepesradsYP--HQFSGGMRQRLL 179
Cdd:cd03223 61 PEGEDLLFLPQ------RPYLPLGT-----LR------------EQLI----------------YPwdDVLSGGEQQRLA 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtehdMAVVLITH 228
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
39-215 |
3.86e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiADITGGSVEMGDVDLvtAKTKVRRTiaatelAIVFQDALtaL 118
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ--GNNFTGTILANNRKP--TKQILKRT------GFVTQDDI--L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGTQL--AEPFRIHRGMSAKQARVEAIALMARVGIPEPESR--ADSYPHQFSGGMRQRLLIAMAVALSPSVLLAD 194
Cdd:PLN03211 152 YPHLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180
....*....|....*....|.
gi 1993389136 195 EPTTALDVTVQAQIMALLKEL 215
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSL 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-252 |
6.95e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 1 MSAPATSAPSAR---PDTGSVALDVRGLTVdlRTPSGViRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIA 77
Cdd:PRK11174 328 LETPLAHPQQGEkelASNDPVTIEAEDLEI--LSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 78 DITGGSVEMGDVDLvtakTKVRRtiaatELAIVFQdaltalNPVYTVGTqlaepFRIHRGMSAKQARVEAI-ALMARVGI 156
Cdd:PRK11174 405 SLKINGIELRELDP----ESWRK-----HLSWVGQ------NPQLPHGT-----LRDNVLLGNPDASDEQLqQALENAWV 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 157 PE-PESRADSYPHQ-------FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRteHDMAVVLITH 228
Cdd:PRK11174 465 SEfLPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTH 542
|
250 260
....*....|....*....|....
gi 1993389136 229 DLALVAeEADRVAIMYAGNVVETG 252
Cdd:PRK11174 543 QLEDLA-QWDQIWVMQDGQIVQQG 565
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
36-246 |
1.21e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.73 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 36 IRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDVDLVTAKTKVRRTIAATELAIVFQDAL 115
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLE----GKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 TaLNPVYTVGTQLAEPFRIHRgmsaKQARVEAIALmarvgipEPEsrADSYPH-----------QFSGGMRQRLLIAMAV 184
Cdd:cd03290 90 L-LNATVEENITFGSPFNKQR----YKAVTDACSL-------QPD--IDLLPFgdqteigergiNLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 185 ALSPSVLLADEPTTALDVTVQAQIM--ALLKELRtEHDMAVVLITHDLALVAeEADRVAIMYAG 246
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQ-DDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-251 |
3.76e-09 |
|
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: 57.91 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 20 LDVRGLTVDLrtpsGVIRAVDNVTFSARRGETLALLGESGCGKSmTAQAIVGLLEPIADITGgsvemgdvDLVTAKTKVR 99
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKS-TLMKILSGVYPHGTWDG--------EIYWSGSPLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 -RTIAATE---LAIVFQD-----ALTALNPVYtVGTQLAEPFRIhrgMSAKQARVEAIALMARVGIPE-PESRADSyphQ 169
Cdd:TIGR02633 69 aSNIRDTEragIVIIHQEltlvpELSVAENIF-LGNEITLPGGR---MAYNAMYLRAKNLLRELQLDAdNVTRPVG---D 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
..
gi 1993389136 250 ET 251
Cdd:TIGR02633 221 AT 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
39-252 |
7.80e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIvgllepiaditggsveMGDVDLVTAKTKVRRTIAATELAIVFQDALTAL 118
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL----------------LAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYtvGTQLAEPFRihrgmsakQARVEAIALMARVGIPEPESRADSYPH--QFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:TIGR00957 718 NILF--GKALNEKYY--------QQVLEACALLPDLEILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993389136 197 TTALDVTVQAQI-------MALLKElRTEhdmavVLITHDLALVAeEADRVAIMYAGNVVETG 252
Cdd:TIGR00957 788 LSAVDAHVGKHIfehvigpEGVLKN-KTR-----ILVTHGISYLP-QVDVIIVMSGGKISEMG 843
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-228 |
1.28e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.17 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 23 RGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMtaqaivgLLEPIAD-ITGGSVEmGDVDLVTAKTKV--R 99
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT-------LLDVLAGrKTAGVIT-GEILINGRPLDKnfQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 100 RTIAATELaivfQDaltALNPVYTVgtqlAEPFRIH---RGMSAKQarveaialmarvgipepesradsyphqfsggmRQ 176
Cdd:cd03232 79 RSTGYVEQ----QD---VHSPNLTV----REALRFSallRGLSVEQ--------------------------------RK 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITH 228
Cdd:cd03232 116 RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIH 166
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-252 |
1.42e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 16 GSVAL-DVRG-LTVDLRT---PSGVIRAVDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDVD 90
Cdd:PRK10789 303 GSEPVpEGRGeLDVNIRQftyPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 91 LVTAKTKVRRTiaatELAIVFQdalTALNPVYTVGTQLA--EPfrihrgmSAKQARVEAIALMARVG-----IPEP-ESR 162
Cdd:PRK10789 379 LTKLQLDSWRS----RLAVVSQ---TPFLFSDTVANNIAlgRP-------DATQQEIEHVARLASVHddilrLPQGyDTE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 163 ADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdmAVVLITHDL-ALVaeEADRVA 241
Cdd:PRK10789 445 VGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLsALT--EASEIL 520
|
250
....*....|.
gi 1993389136 242 IMYAGNVVETG 252
Cdd:PRK10789 521 VMQHGHIAQRG 531
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-240 |
1.79e-08 |
|
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: 54.34 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 47 RRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEmgdVDLVTAKTKVRRTIAATE------LAIVFQDALTalNP 120
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKP----DEGDIE---IELDTVSYKPQYIKADYEgtvrdlLSSITKDFYT--HP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 121 VYTvgTQLAEPFRIhrgmsakqarveaialmarvgipepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTAL 200
Cdd:cd03237 94 YFK--TEIAKPLQI-------------------------EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1993389136 201 DVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRV 240
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-246 |
2.01e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 14 DTGSVALDVRGLTvdlrtPSGViravDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadITGGSVEMGDVDLVT 93
Cdd:PRK10762 252 APGEVRLKVDNLS-----GPGV----NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 94 aktkvRRTIAATELAIVF--QD----------------ALTALNPVYTVGTQLAEpfrihrgmSAKQARVEAIALMARVG 155
Cdd:PRK10762 319 -----RSPQDGLANGIVYisEDrkrdglvlgmsvkenmSLTALRYFSRAGGSLKH--------ADEQQAVSDFIRLFNIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 156 IPEPESRADsyphQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAE 235
Cdd:PRK10762 386 TPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLG 460
|
250
....*....|.
gi 1993389136 236 EADRVAIMYAG 246
Cdd:PRK10762 461 MSDRILVMHEG 471
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-228 |
3.03e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 37 RAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADitGGSVEMGDVDLvtaktkvrrtiaATELAIVfqDALT 116
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV--AGCVDVPDNQF------------GREASLI--DAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVytvgtqlaepfrihrgmsakqarVEAIALMARVGIPEPESRADSYPHqFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:COG2401 108 RKGDF-----------------------KDAVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|...
gi 1993389136 197 TTALDVTVqAQIMAL-LKELRTEHDMAVVLITH 228
Cdd:COG2401 164 CSHLDRQT-AKRVARnLQKLARRAGITLVVATH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-251 |
3.65e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 16 GSVALDVRGLTvDLRTPSgviraVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIA-DITGGSVEMGDVD---- 90
Cdd:PRK10982 247 GEVILEVRNLT-SLRQPS-----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAgTITLHGKKINNHNanea 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 91 ------LVTAKTkvRRTIAATELAIVFqDALTALNPVYTVGTQLAEPFRIHrgmSAKQARVEAIalmaRVGIPEPESRAD 164
Cdd:PRK10982 321 inhgfaLVTEER--RSTGIYAYLDIGF-NSLISNIRNYKNKVGLLDNSRMK---SDTQWVIDSM----RVKTPGHRTQIG 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 165 SyphqFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMY 244
Cdd:PRK10982 391 S----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMS 465
|
250
....*....|
gi 1993389136 245 AGNV---VET 251
Cdd:PRK10982 466 NGLVagiVDT 475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-239 |
4.12e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 48 RGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDlvtaktkvrrtiaatelaivfqdaltalnpvytvgtq 127
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP----PGGGVIYIDGE------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 128 laepfrihrgmsakqarveaiALMARVGIPEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQ 207
Cdd:smart00382 40 ---------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*..
gi 1993389136 208 IMAL-----LKELRTEHDMAVVLITHDLALVAEEADR 239
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-249 |
4.71e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGllEPIAdiTGGSVEMGDVDLVTAKTK--VRRTIA-ATELAIV 110
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRA--TSGRIVFDGKDITDWQTAkiMREAVAiVPEGRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 111 FQDALTALNpvYTVGTQLAEpfrihrgMSAKQARVEAIALMarvgIPEPESRADSYPHQFSGGMRQRLLIAMAVALSPSV 190
Cdd:PRK11614 92 FSRMTVEEN--LAMGGFFAE-------RDQFQERIKWVYEL----FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1993389136 191 LLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNVV 249
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-250 |
5.94e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVALDvrglTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEpiadITGGSVEMGD 88
Cdd:PLN03232 1226 VSGWPSRGSIKFE----DVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE----LEKGRIMIDD 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 89 VDLVT-AKTKVRRTiaateLAIVFQdaltalNPVYTVGTQL--AEPFRIHRGM----SAKQARVEAIALMARVGIpepES 161
Cdd:PLN03232 1298 CDVAKfGLTDLRRV-----LSIIPQ------SPVLFSGTVRfnIDPFSEHNDAdlweALERAHIKDVIDRNPFGL---DA 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 162 RADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMavVLITHDLALVAeEADRVA 241
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTII-DCDKIL 1440
|
....*....
gi 1993389136 242 IMYAGNVVE 250
Cdd:PLN03232 1441 VLSSGQVLE 1449
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-252 |
6.11e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.95 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 33 SGVIrAVDNVTFSARRGET--------------LALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTAKTKV 98
Cdd:PRK10790 338 SGRI-DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPL----TEGEIRLDGRPLSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 99 RRTiaatELAIVFQDaltalnPVYTVGTQLAEpFRIHRGMSAKQ--ARVEAIALMARV-GIPEP-ESRADSYPHQFSGGM 174
Cdd:PRK10790 413 LRQ----GVAMVQQD------PVVLADTFLAN-VTLGRDISEEQvwQALETVQLAELArSLPDGlYTPLGEQGNNLSVGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 175 RQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVlITHDLALVAEeADRVAIMYAGNVVETG 252
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR-EHTTLVV-IAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-240 |
6.97e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 46 ARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEmGDVDL------VTAKTKVRrtiaatelaivFQDALTALN 119
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKP----DEGEVD-PELKIsykpqyIKPDYDGT-----------VEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 120 PVYT---VGTQLAEPFRIHRgmsakqarveaiaLMarvgipepesraDSYPHQFSGGMRQRLLIAMAVALSPSVLLADEP 196
Cdd:PRK13409 426 DDLGssyYKSEIIKPLQLER-------------LL------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1993389136 197 TTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRV 240
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
171-246 |
7.13e-08 |
|
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: 52.09 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIM-----ALLKELRTehdmaVVLITHDLALVaEEADRVAIMYA 245
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFencilGLLLNNKT-----RILVTHQLQLL-PHADQIVVLDN 202
|
.
gi 1993389136 246 G 246
Cdd:cd03250 203 G 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
42-228 |
7.34e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.11 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 42 VTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditggsvemGDVDLV-TAKTKVRRTIAATELAIVFQDAL-TALN 119
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA---------GRVLLNgGPLDFQRDSIARGLLYLGHAPGIkTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 120 PVytvgtqlaEPFRIHRGMSAKQARVEAialMARVGIPEPESRAdsyPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTA 199
Cdd:cd03231 90 VL--------ENLRFWHADHSDEQVEEA---LARVGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 1993389136 200 LDVTVQAQIMALLKElRTEHDMAVVLITH 228
Cdd:cd03231 156 LDKAGVARFAEAMAG-HCARGGMVVLTTH 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-250 |
8.15e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVA----LDVRGLTvdlrtpSGVIRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLlEPIADitggsv 84
Cdd:PRK09700 251 NAMKENVSNLAhetvFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAG------ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 85 emGDVDLVTAKTKVRRTIAATELAIVF---QDALTALNPVYTVGTQLAEPFRIHRG-----MSAKQARVEA-IALMARVG 155
Cdd:PRK09700 318 --GEIRLNGKDISPRSPLDAVKKGMAYiteSRRDNGFFPNFSIAQNMAISRSLKDGgykgaMGLFHEVDEQrTAENQREL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 156 IPEPESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAE 235
Cdd:PRK09700 396 LALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIIT 474
|
250
....*....|....*
gi 1993389136 236 EADRVAIMYAGNVVE 250
Cdd:PRK09700 475 VCDRIAVFCEGRLTQ 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-240 |
9.60e-08 |
|
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: 53.63 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 45 SARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMgDVDL------VTAKTKVRrtiaatelaivFQDAL-TA 117
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKP----DEGEVDE-DLKIsykpqyISPDYDGT-----------VEEFLrSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNPVYTVG---TQLAEPFRIHRgmsakqarveaiaLMarvgipepesraDSYPHQFSGGMRQRLLIAMAVALSPSVLLAD 194
Cdd:COG1245 426 NTDDFGSSyykTEIIKPLGLEK-------------LL------------DKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1993389136 195 EPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVAEEADRV 240
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
169-244 |
1.36e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 1.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993389136 169 QFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMY 244
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-246 |
1.40e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 36 IRAVDNVTFSARRGETLALLGESGCGKSMTAQAIVGllepIADITGGSVE-MGDVdlVTAKTKvrRTIAATELAIVFQDa 114
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG----IYTRDAGSILyLGKE--VTFNGP--KSSQEAGIGIIHQE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 115 ltaLN--PVYTV------GTQLAEPF-RI-HRGMSAkqarvEAIALMARVGIPEPESRADSyphQFSGGMRQRLLIAMAV 184
Cdd:PRK10762 88 ---LNliPQLTIaeniflGREFVNRFgRIdWKKMYA-----EADKLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993389136 185 ALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHdMAVVLITHDLALVAEEADRVAIMYAG 246
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQG-RGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
38-257 |
1.47e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 38 AVDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEM-GDVDLVtaktkvrrtiaatelaivfqdALT 116
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSP----TVGKVDRnGEVSVI---------------------AIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 A-LNPVYTvGTQLAEPFRIHRGMSAKQARveaiALMarvgipePE----SRADSYPHQ----FSGGMRQRLLIAMAVALS 187
Cdd:PRK13546 94 AgLSGQLT-GIENIEFKMLCMGFKRKEIK----AMT-------PKiiefSELGEFIYQpvkkYSSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 188 PSVLLADEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLALVAEEADRVAIMYAGNVVETGLVSEV 257
Cdd:PRK13546 162 PDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
39-249 |
3.29e-07 |
|
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: 49.95 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIADITGgSVEMGDVDLVTAKTKVRRtiaatELAIVFQDALTal 118
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEG-DIHYNGIPYKEFAEKYPG-----EIIYVSEEDVH-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 119 NPVYTVGtQLAEpFRIhrgmsakqarveaialmarvgipepESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTT 198
Cdd:cd03233 95 FPTLTVR-ETLD-FAL-------------------------RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 199 ALDVTVQAQIMALLKELRTEHDMAVVLIthdLALVAEEA----DRVAIMYAGNVV 249
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVS---LYQASDEIydlfDKVLVLYEGRQI 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
41-233 |
5.61e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSVEMGDV-DLVTAKTKVRRTiaatELAIVFQDALTALN 119
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIINDShNLKDINLKWWRS----KIGVVSQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 120 PV--------YTV-------------GTQLAEPFRIHRGMSAKQARV--------------------------EAIALMA 152
Cdd:PTZ00265 475 SIknnikyslYSLkdlealsnyynedGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrknyqtikdsEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 153 RV-------GIPEP-ESRADSYPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVV 224
Cdd:PTZ00265 555 KVlihdfvsALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
....*....
gi 1993389136 225 LITHDLALV 233
Cdd:PTZ00265 635 IIAHRLSTI 643
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
171-244 |
5.92e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 5.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHDLALVAEEADRVAIMY 244
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
169-248 |
7.60e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 169 QFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTV-QAQIMALLkelrtEHDMAVVLITHDLALVAEEADRVAIMYAGN 247
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALI-----DFEGALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
.
gi 1993389136 248 V 248
Cdd:PRK10636 505 V 505
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-241 |
9.88e-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: 50.32 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditgGSVEMGDvdlvTAKtkvrrtiaateLAIVFQ--DALT 116
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS----GTIEIGE----TVK-----------LAYVDQsrDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYtvgtqlaepfrihrgmsakqarvEAIAL---MARVGIPEPESRAdsYPHQF--------------SGGMRQRLL 179
Cdd:TIGR03719 399 PNKTVW-----------------------EEISGgldIIKLGKREIPSRA--YVGRFnfkgsdqqkkvgqlSGGERNRVH 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDV-TVQAQIMALLkelrtehDMA--VVLITHDLALVaeeaDRVA 241
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVeTLRALEEALL-------NFAgcAVVISHDRWFL----DRIA 507
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
168-244 |
1.00e-06 |
|
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: 48.12 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 168 HQFSGGMRQRLLIAMAVAL-----SPSVLLaDEPTTALDVTVQAQIMALLKELRtEHDMAVVLITHDLaLVAEEADRVAI 242
Cdd:cd03227 76 LQLSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLP-ELAELADKLIH 152
|
..
gi 1993389136 243 MY 244
Cdd:cd03227 153 IK 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-246 |
1.42e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 14 DTGSVALDVRGLTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKSMtaqaivgLLEPIAD-ITGGSVEMGDVdLV 92
Cdd:TIGR00956 754 ESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTT-------LLNVLAErVTTGVITGGDR-LV 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 93 TAK---TKVRRTIAATELaivfQDALTalnPVYTV------GTQLAEPFRIHRgmSAKQARVEAIalmarVGIPEPESRA 163
Cdd:TIGR00956 826 NGRpldSSFQRSIGYVQQ----QDLHL---PTSTVreslrfSAYLRQPKSVSK--SEKMEYVEEV-----IKLLEMESYA 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 164 DSYPHQFSGGM----RQRLLIAMAVALSPSVLL-ADEPTTALDVTVQAQIMALLKELrTEHDMAVVLITHD-LALVAEEA 237
Cdd:TIGR00956 892 DAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQpSAILFEEF 970
|
....*....
gi 1993389136 238 DRVAIMYAG 246
Cdd:TIGR00956 971 DRLLLLQKG 979
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
166-242 |
1.85e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 1.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 166 YPHQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDMAVVLITHDLALVaEEADRVAI 242
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVV 1430
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
169-244 |
2.81e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 2.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993389136 169 QFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVtVQAQIMA-LLKELRTEHdmAVVLITHDLALVAEEADRVAIMY 244
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI-RQRLNVArLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
41-232 |
5.70e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.41 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLVTakTKVRrtiaateLAIVFQDALTALNP 120
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP----AAGTIKLDGGDIDD--PDVA-------EACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 121 VYTVGTQLAEPFRIHRGmsakqARVEAIALMARVGIPEPESRADSYphqFSGGMRQRLLIA-MAVALSPsVLLADEPTTA 199
Cdd:PRK13539 87 ALTVAENLEFWAAFLGG-----EELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALArLLVSNRP-IWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|....
gi 1993389136 200 LDVTVQAQIMALLKElRTEHDMAVVLITH-DLAL 232
Cdd:PRK13539 158 LDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
171-252 |
9.03e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIA--MAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEHDmAVVLITHDLAlVAEEADRVAIM----- 243
Cdd:cd03238 89 SGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD-VLSSADWIIDFgpgsg 166
|
90
....*....|
gi 1993389136 244 -YAGNVVETG 252
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
147-244 |
1.03e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 147 AIALMArvGIPEPESRADSYPH----------QFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELR 216
Cdd:cd03222 41 AVKILA--GQLIPNGDNDEWDGitpvykpqyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
90 100
....*....|....*....|....*...
gi 1993389136 217 TEHDMAVVLITHDLALVAEEADRVAIMY 244
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
171-257 |
1.34e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEH-DMAVvlithdlaLVA----EEADR----VA 241
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSV--------LVAtaymEEAERfdwlVA 209
|
90
....*....|....*.
gi 1993389136 242 iMYAGNVVETGLVSEV 257
Cdd:NF033858 210 -MDAGRVLATGTPAEL 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
112-247 |
1.55e-05 |
|
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: 46.47 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 112 QDALTALNPVYTvgtQLAEPFRIHRGMSAKQARVEAI-------ALMARVGI-------PEPESRADSyphqFSGGMRQR 177
Cdd:TIGR03719 97 KDALDRFNEISA---KYAEPDADFDKLAAEQAELQEIidaadawDLDSQLEIamdalrcPPWDADVTK----LSGGERRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 178 lliamaVAL------SPSVLLADEPTTALDvtvqAQIMALLKELRTEHDMAVVLITHD---LALVAE---EADR-VAIMY 244
Cdd:TIGR03719 170 ------VALcrlllsKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDryfLDNVAGwilELDRgRGIPW 239
|
...
gi 1993389136 245 AGN 247
Cdd:TIGR03719 240 EGN 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-255 |
5.09e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 41 NVTFSARRGETLALLGESGCGKSMTAQAIVGllEPIADITGGSVEMGDVDlVTAKTKVRRTIAATELAivFQdaltalNP 120
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILEGDILFKGES-ILDLEPEERAHLGIFLA--FQ------YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 121 VYTVGTQLAEPFRI---HRGMSAKQARVEAIA----LMARVGIPEPESradSYPHQ-----FSGGMRQRLLIAMAVALSP 188
Cdd:CHL00131 94 IEIPGVSNADFLRLaynSKRKFQGLPELDPLEfleiINEKLKLVGMDP---SFLSRnvnegFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 189 SVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAE-EADRVAIMYAGNVVETGLVS 255
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYiKPDYVHVMQNGKIIKTGDAE 237
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
124-202 |
6.64e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 124 VGTQLAEPFRIHRGMSAKQARVEAIALMARVGI-PEPESRADSyphQFSGGMRQRLLIAMAVALSPSVLLADEPTTALDV 202
Cdd:PLN03073 301 VSQRLEEIYKRLELIDAYTAEARAASILAGLSFtPEMQVKATK---TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
40-236 |
9.49e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.87 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 40 DNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDVDLvtakTKVRRTIAATELAIVFQ----DAL 115
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP----DAGEVLWQGEPI----RRQRDEYHQDLLYLGHQpgikTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 116 TALnpvytvgtqlaEPFRIHRGMSAKQARVEAIALMARVGIpepESRADSYPHQFSGGMRQRllIAMA-VALSPSVL-LA 193
Cdd:PRK13538 90 TAL-----------ENLRFYQRLHGPGDDEALWEALAQVGL---AGFEDVPVRQLSAGQQRR--VALArLWLTRAPLwIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1993389136 194 DEPTTALDVTVQAQIMALLkELRTEHDMAVVLITH-DLALVAEE 236
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALL-AQHAEQGGMVILTTHqDLPVASDK 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-260 |
1.02e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 9 PSARPDTGSVALDVRGLTVDLRTPSGVIravDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPIAditggsvemgd 88
Cdd:PLN03232 606 PPLQPGAPAISIKNGYFSWDSKTSKPTL---SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 89 vdlvTAKTKVRRTIA-ATELAIVFqDALTALNPVYtvGTQLaEPFRIHRGMSAKqARVEAIALMARVGIPEPESRADSyp 167
Cdd:PLN03232 672 ----TSSVVIRGSVAyVPQVSWIF-NATVRENILF--GSDF-ESERYWRAIDVT-ALQHDLDLLPGRDLTEIGERGVN-- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 168 hqFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIM--ALLKELRTEHDMAVVLITHDLALVaeeaDRVAIMYA 245
Cdd:PLN03232 741 --ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdsCMKDELKGKTRVLVTNQLHFLPLM----DRIILVSE 814
|
250
....*....|....*
gi 1993389136 246 GNVVETGLVSEVFGS 260
Cdd:PLN03232 815 GMIKEEGTFAELSKS 829
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
171-240 |
2.18e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 2.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTehdmAVVLITHDLALVAEEADRV 240
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
170-250 |
2.32e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMallKELRTEHDMAVVL-ITHDLALVAeEADRVAIMYAGNV 248
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ---KTIREEFKSCTMLiIAHRLNTII-DCDRILVLDAGRV 1450
|
..
gi 1993389136 249 VE 250
Cdd:PLN03130 1451 VE 1452
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
171-247 |
2.51e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRlliamaVAL------SPSVLLADEPTTALDvtvqAQIMALLKELRTEHDMAVVLITHD---LALVAE---EAD 238
Cdd:PRK11819 165 SGGERRR------VALcrllleKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLDNVAGwilELD 234
|
90
....*....|
gi 1993389136 239 R-VAIMYAGN 247
Cdd:PRK11819 235 RgRGIPWEGN 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
34-229 |
2.98e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 34 GVIRAVDNVTFSARRGETLALLGESGCGKSmtaqAIVGLLEPIADITGGSV------------------EMGDVDLVTAK 95
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKS----TLLALLKNEISADGGSYtfpgnwqlawvnqetpalPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 96 TKVRRTIAAtELAIVfqdalTALNPVYTVGTqlaepfrIHRGMSAKQA---RVEAIALMARVGIPEPE-SRADSyphQFS 171
Cdd:PRK10636 88 DREYRQLEA-QLHDA-----NERNDGHAIAT-------IHGKLDAIDAwtiRSRAASLLHGLGFSNEQlERPVS---DFS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 172 GGMRQRLLIAMAVALSPSVLLADEPTTALDVTVqaqIMALLKELRTeHDMAVVLITHD 229
Cdd:PRK10636 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKS-YQGTLILISHD 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
171-256 |
3.85e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIM--ALLKELRTEhdmAVVLITHDLALVAeEADRVAIMYAGNV 248
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkCIKDELRGK---TRVLVTNQLHFLS-QVDRIILVHEGMI 817
|
....*...
gi 1993389136 249 VETGLVSE 256
Cdd:PLN03130 818 KEEGTYEE 825
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
54-229 |
5.96e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 54 LLGESGCGKSMTAQAIVGLLEPiadiTGGSVE---------------------------MGDVDLVTAKTKVRRTIA--- 103
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEP----SAGNVSldpnerlgklrqdqfafeeftvldtviMGHTELWEVKQERDRIYAlpe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 104 ATElaivfQDALTALNpvytVGTQLAEpfrihrgMSAKQARVEAIALMARVGIPEpesradsypHQFSGGMRQ------- 176
Cdd:PRK15064 108 MSE-----EDGMKVAD----LEVKFAE-------MDGYTAEARAGELLLGVGIPE---------EQHYGLMSEvapgwkl 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALDV-TVQaqimaLLKELRTEHDMAVVLITHD 229
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDVLNERNSTMIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
171-257 |
6.07e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 171 SGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKElrtehdmaVVLITHDLALVA-----EEA----DRVA 241
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKT--------SANILDTTPLVAiyqcsQDAyelfDKVI 282
|
90
....*....|....*.
gi 1993389136 242 IMYAGNVVETGLVSEV 257
Cdd:TIGR00956 283 VLYEGYQIYFGPADKA 298
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-241 |
6.36e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 39 VDNVTFSARRGETLALLGESGCGKSMTAQAIVGLLEPiadiTGGSVEMGDvdlvTAKtkvrrtiaateLAIVFQ--DALT 116
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQP----DSGTIKIGE----TVK-----------LAYVDQsrDALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 117 ALNPVYtvgtqlaepfrihrgmsakqarvEAI---ALMARVGIPEPESRAdsYPHQF--------------SGGMRQRLL 179
Cdd:PRK11819 401 PNKTVW-----------------------EEIsggLDIIKVGNREIPSRA--YVGRFnfkggdqqkkvgvlSGGERNRLH 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993389136 180 IAMAVALSPSVLLADEPTTALDV-TVQAQIMALLkelrtehDMA--VVLITHD---LalvaeeaDRVA 241
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVeTLRALEEALL-------EFPgcAVVISHDrwfL-------DRIA 509
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
169-252 |
6.98e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 169 QFSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAQIMALLKELRTEhDMAVVLITHDLALVAEEADRVAIMYAGNV 248
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
....
gi 1993389136 249 VETG 252
Cdd:PRK10938 214 AETG 217
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
177-233 |
9.76e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 9.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 177 RLLIAMAVALSPSVLLADEPTTALD---VTVQAQIMA-LLKELRTEHDMAVVLITHDLALV 233
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDrenIESLAHALVeIIKSRSQQRNFQLLVITHDEDFV 1273
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
171-234 |
1.47e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993389136 171 SGGMRQ------RLLIAMAVALSPSVLLADEPTTALDV-TVQAQIMALLKELRTEHDMAVVLITHDLALVA 234
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVD 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-262 |
3.09e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 4 PAtSAPSARPDT---GSVALDvrglTVDLRTPSGVIRAVDNVTFSARRGETLALLGESGCGKS---MTAQAIVgllepia 77
Cdd:PTZ00243 1293 PA-SPTSAAPHPvqaGSLVFE----GVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKStllLTFMRMV------- 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 78 DITGGSV-----EMGDVDLvtakTKVRRtiaatELAIVFQDaltalnPVYTVGT--QLAEPFrihrgMSAKQARV----E 146
Cdd:PTZ00243 1361 EVCGGEIrvngrEIGAYGL----RELRR-----QFSMIPQD------PVLFDGTvrQNVDPF-----LEASSAEVwaalE 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 147 AIALMARV-----GIpepESRADSYPHQFSGGMRQrlLIAMAVAL---SPSVLLADEPTT----ALDVTVQAQIMALLKE 214
Cdd:PTZ00243 1421 LVGLRERVaseseGI---DSRVLEGGSNYSVGQRQ--LMCMARALlkkGSGFILMDEATAnidpALDRQIQATVMSAFSA 1495
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1993389136 215 lrtehdMAVVLITHDLALVAeEADRVAIMYAGNVVEtglvsevFGSPR 262
Cdd:PTZ00243 1496 ------YTVITIAHRLHTVA-QYDKIIVMDHGAVAE-------MGSPR 1529
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
42-209 |
5.52e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.67 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 42 VTFSARRGETLALLGESGCGKSMTAQAIVGllepiaDITGGSVEmGDVDlVTAKTKVRRTIAAT----ELAIVFQDALTA 117
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTLMDVLAG------RKTGGYIE-GDIR-ISGFPKKQETFARIsgycEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 118 LNP-VYTVGTQLAEPFRIHRGMSAKQARVEAIALM----ARVGIPEPESradsyphqFSGGMRQRLLIAMAVALSPSVLL 192
Cdd:PLN03140 971 RESlIYSAFLRLPKEVSKEEKMMFVDEVMELVELDnlkdAIVGLPGVTG--------LSTEQRKRLTIAVELVANPSIIF 1042
|
170
....*....|....*..
gi 1993389136 193 ADEPTTALDVTVQAQIM 209
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVM 1059
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
170-266 |
7.16e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.58 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993389136 170 FSGGMRQRLLIAMAVALSPSVLLADEPTTALDVTVQAqimALLKELRTEH-DMAVVLITHDLALVAeEADRVAIMYAGNV 248
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN---ILQKVVMTAFaDRTVVTIAHRVSTIL-DADLVLVLSRGIL 232
|
90
....*....|....*...
gi 1993389136 249 VETGLVSEVFGSPRHPYT 266
Cdd:cd03288 233 VECDTPENLLAQEDGVFA 250
|
|
| |
