|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-331 |
0e+00 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 562.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 5 SRDGKVLIEVKGMKKWFPIKGGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE 84
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIPD---RELRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSG 161
Cdd:COG4608 81 DITGLSGrelRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 162 GQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIA 241
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 242 NTADLFDKPAHPYTHALMSAIPEPSLEkASRERIVLSGDVPSPANPPPGCRFHTRCPIAVEgVCDVVDPPLETIDfDDHA 321
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDPE-RRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQD-RCATEEPPLREVG-PGHQ 317
|
330
....*....|
gi 663511184 322 VACHFPLGPG 331
Cdd:COG4608 318 VACHLAEEGS 327
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-327 |
3.45e-171 |
|
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: 478.78 E-value: 3.45e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP---ITDGSVLYDGEDIR 87
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 88 TIPDRELR----RRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK--REHMNRFPHEFSG 161
Cdd:COG0444 74 KLSEKELRkirgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 162 GQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIA 241
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 242 NTADLFDKPAHPYTHALMSAIPEPslEKASRERIVLSGDVPSPANPPPGCRFHTRCPIAVEgVCDVVDPPLETIDfDDHA 321
Cdd:COG0444 234 PVEELFENPRHPYTRALLSSIPRL--DPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMD-RCREEEPPLREVG-PGHR 309
|
....*.
gi 663511184 322 VACHFP 327
Cdd:COG0444 310 VACHLY 315
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-325 |
1.72e-138 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 396.26 E-value: 1.72e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 7 DGKVLIEVKGMKKWFPIKGGMLSEVKiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRvLLGLI-PITDGSVLYDGED 85
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKPER-LVKALDGVSFTLERGKTLAVVGESGCGKSTLAR-LLTMIeTPTGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 86 IrTIPDRE----LRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSG 161
Cdd:PRK11308 79 L-LKADPEaqklLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 162 GQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIA 241
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 242 NTADLFDKPAHPYTHALMSAIPEPSlEKASRERIVLSGDVPSPANPPPGCRFHTRCPIAVEgVCDVVDPPLEtiDFDDHA 321
Cdd:PRK11308 238 TKEQIFNNPRHPYTQALLSATPRLN-PDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFG-RCRQEQPQLR--DYDGRL 313
|
....
gi 663511184 322 VACH 325
Cdd:PRK11308 314 VACF 317
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-265 |
2.19e-138 |
|
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: 403.68 E-value: 2.19e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 7 DGKVLIEVKGMKKWFPIKGGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPiTDGSVLYDGEDI 86
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDRE---LRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAE-GAELTQKVADVLDSVGLKREHMNRFPHEFSGG 162
Cdd:COG4172 350 DGLSRRAlrpLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLsAAERRARVAEALEEVGLDPAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIAN 242
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
250 260
....*....|....*....|...
gi 663511184 243 TADLFDKPAHPYTHALMSAIPEP 265
Cdd:COG4172 510 TEQVFDAPQHPYTRALLAAAPLL 532
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-268 |
5.51e-138 |
|
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: 401.97 E-value: 5.51e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 2 TEESRDGKVLIEVKGMKKWFPIKGgmlsevKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY 81
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYPVRG------KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 82 DGEDIRTIPD---RELRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHE 158
Cdd:COG1123 325 DGKDLTKLSRrslRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 159 FSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
250 260 270
....*....|....*....|....*....|
gi 663511184 239 EIANTADLFDKPAHPYTHALMSAIPEPSLE 268
Cdd:COG1123 485 EDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
7-324 |
2.16e-128 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 370.96 E-value: 2.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 7 DGKVLIEVKGMKKWFPIKGG--MLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE 84
Cdd:PRK15079 4 GKKVLLEVADLKVHFDIKDGkqWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIPD---RELRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLA-EGAELTQKVADVLDSVGLKREHMNRFPHEFS 160
Cdd:PRK15079 84 DLLGMKDdewRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLLPNLINRYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEI 240
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 241 ANTADLFDKPAHPYTHALMSA--IPEPSLEKASRERIvLSGDVPSPANPPPGCRFHTRCPIAVEGvCDVVDPPLETIdfD 318
Cdd:PRK15079 244 GTYDEVYHNPLHPYTKALMSAvpIPDPDLERNKTIQL-LEGELPSPINPPSGCVFRTRCPIAGPE-CAKTRPVLEGS--F 319
|
....*.
gi 663511184 319 DHAVAC 324
Cdd:PRK15079 320 RHAVSC 325
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-263 |
1.23e-117 |
|
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: 340.24 E-value: 1.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:COG1124 1 MLEVRNLSVSYGQGGR-------RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DRELRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAEltqKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALA 170
Cdd:COG1124 74 RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 171 RALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|...
gi 663511184 251 AHPYTHALMSAIP 263
Cdd:COG1124 231 KHPYTRELLAASL 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-241 |
9.79e-116 |
|
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: 334.86 E-value: 9.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DREL---RRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQK-VADVLDSVGLKREHMNRFPHEFSGGQKQR 166
Cdd:cd03257 74 RRLRkirRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 167 LALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIA 241
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-283 |
7.54e-90 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 281.74 E-value: 7.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 7 DGKVLIEVKGMKKWFPIKGGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI 86
Cdd:PRK10261 309 DGEPILQVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDREL---RRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQ 163
Cdd:PRK10261 389 DTLSPGKLqalRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 164 KQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANT 243
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 663511184 244 ADLFDKPAHPYTHALMSAIPEPSLEKASRERIVLSGDVPS 283
Cdd:PRK10261 549 RAVFENPQHPYTRKLMAAVPVADPSRQRPQRVLLSDDLPS 588
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-289 |
1.71e-88 |
|
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: 275.80 E-value: 1.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGMlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP----ITDGSVLYDGEDI 86
Cdd:COG4172 6 LLSVEDLSVAFGQGGGT-------VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDRELRR----RMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK--REHMNRFPHEFS 160
Cdd:COG4172 79 LGLSERELRRirgnRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEI 240
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 663511184 241 ANTADLFDKPAHPYTHALMSAipEPSLEKAsrerivlsgdvPSPANPPP 289
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAA--EPRGDPR-----------PVPPDAPP 274
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-261 |
2.69e-84 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 256.30 E-value: 2.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGMLSEVKIHvrAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRT-- 88
Cdd:COG4167 4 LLEVRNLSKTFKYRTGLFRRQQFE--AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 IPDRELRRRMqiVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLA 168
Cdd:COG4167 82 YKYRCKHIRM--IFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 169 LARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFD 248
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|...
gi 663511184 249 KPAHPYTHALMSA 261
Cdd:COG4167 240 NPQHEVTKRLIES 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-329 |
6.14e-78 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 242.32 E-value: 6.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 1 MTEESRDGKVLIEVKGMKKWFPIKGGMlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP---ITDG 77
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 78 SVLYDGEDIRTIPDRELRR----RMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGL--KREH 151
Cdd:PRK09473 75 SATFNGREILNLPEKELNKlraeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 152 MNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAV 231
Cdd:PRK09473 155 MKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 232 MYLGKIVEIANTADLFDKPAHPYTHALMSAIPEpsLEKASRERIVLSGDVPSPANPPPGCRFHTRCPIAVEgVCDvVDPP 311
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPR--LDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAME-ICS-SAPP 310
|
330
....*....|....*...
gi 663511184 312 LETIDfDDHAVACHFPLG 329
Cdd:PRK09473 311 LEEFG-PGRLRACFKPVE 327
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-260 |
2.47e-76 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 244.23 E-value: 2.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 5 SRDGKVLIEVKGMKKWFPIKGGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPiTDGSVLYDGE 84
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIPDREL---RRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLA-EGAELTQKVADVLDSVGLKREHMNRFPHEFS 160
Cdd:PRK15134 348 PLHNLNRRQLlpvRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETRHRYPAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEI 240
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
250 260
....*....|....*....|
gi 663511184 241 ANTADLFDKPAHPYTHALMS 260
Cdd:PRK15134 508 GDCERVFAAPQQEYTRQLLA 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-278 |
6.46e-75 |
|
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: 240.19 E-value: 6.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPIT---DGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMNP 111
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQDPMTQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 rMSVRSIVGEPLQvNRLAEGAELTQKVADVLDSVGLKReHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:COG1123 99 -VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 192 SVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMSAIPEPSLEKAS 271
Cdd:COG1123 176 TTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAA 255
|
....*..
gi 663511184 272 RERIVLS 278
Cdd:COG1123 256 AAEPLLE 262
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-262 |
1.58e-72 |
|
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: 226.23 E-value: 1.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFpiKGGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIp 90
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DRE----LRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQ-VNRLAEGAELtQKVADVLDSVGLKREHMNRFPHEFSGGQKQ 165
Cdd:TIGR02769 79 DRKqrraFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRhLTSLDESEQK-ARIAELLDMVGLRSEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTAD 245
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
250
....*....|....*..
gi 663511184 246 LFDKpAHPYTHALMSAI 262
Cdd:TIGR02769 238 LLSF-KHPAGRNLQSAV 253
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-275 |
5.56e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 227.27 E-value: 5.56e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:COG1135 2 IELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 REL---RRRMQIVFQdpggSMN--PRMSVRSIVGEPLQVNRLaEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQR 166
Cdd:COG1135 75 RELraaRRKIGMIFQ----HFNllSSRTVAENVALPLEIAGV-PKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 167 LALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADL 246
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
250 260
....*....|....*....|....*....
gi 663511184 247 FDKPAHPYTHALMSAIPEPSLEKASRERI 275
Cdd:COG1135 229 FANPQSELTRRFLPTVLNDELPEELLARL 257
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
36-328 |
7.57e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 216.15 E-value: 7.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP----ITDGSVLYDGEDIRTIPDRELRR----RMQIVFQDPGG 107
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 SMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK--REHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMSAIPEP 265
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEF 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 266 SLEKASRERivLSGDVPSPANPPPGCRFHTRCPIAVEgVCDVVDPPLETIdfDDHAVACHFPL 328
Cdd:PRK11022 261 AQDKARLAS--LPGVVPGKYDRPNGCLLNPRCPYATD-RCRAEEPALNML--AGRQSKCHYPL 318
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-257 |
3.71e-66 |
|
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: 209.07 E-value: 3.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 7 DGKVLIEVKGMKKWFpikGGmlseVKIHvravDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI 86
Cdd:COG1127 1 MSEPMIEVRNLTKSF---GD----RVVL----DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDREL---RRRMQIVFQDPG--GSMNprmsvrsiVGE----PLQVN-RLAEgAELTQKVADVLDSVGLkREHMNRFP 156
Cdd:COG1127 70 TGLSEKELyelRRRIGMLFQGGAlfDSLT--------VFEnvafPLREHtDLSE-AEIRELVLEKLELVGL-PGAADKMP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 157 HEFSGGQKQRLALARALSLDPEFILLDEPTSALD-VSVqAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLG 235
Cdd:COG1127 140 SELSGGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250 260
....*....|....*....|..
gi 663511184 236 KIVEIANTADLFDKPaHPYTHA 257
Cdd:COG1127 219 KIIAEGTPEELLASD-DPWVRQ 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-254 |
3.88e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 212.65 E-value: 3.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI-RTIPDRelrRRMQIVFQDPggSMNPRM 113
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtGLPPEK---RNVGMVFQDY--ALFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:COG3842 93 TVAENVAFGLRMRGVPK-AEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITH----ALNvvnhISDRVAVMYLGKIVEIANTADLFDKPAHPY 254
Cdd:COG3842 171 REEMREELRRLQRELGITFIYVTHdqeeALA----LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-262 |
7.42e-65 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 206.46 E-value: 7.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPikGGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIp 90
Cdd:PRK10419 3 LLNVSGLSHHYA--HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DRE----LRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQ-VNRLAEgAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQ 165
Cdd:PRK10419 80 NRAqrkaFRRDIQMVFQDSISAVNPRKTVREIIREPLRhLLSLDK-AERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTAD 245
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
250
....*....|....*..
gi 663511184 246 LfDKPAHPYTHALMSAI 262
Cdd:PRK10419 239 K-LTFSSPAGRVLQNAV 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-261 |
2.24e-64 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 205.41 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 9 KVLIEVKGMKKWFPIKGGMLSevKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrT 88
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWFR--RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-H 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 IPDRELR-RRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRL 167
Cdd:PRK15112 79 FGDYSYRsQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 168 ALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
250
....*....|....
gi 663511184 248 DKPAHPYTHALMSA 261
Cdd:PRK15112 239 ASPLHELTKRLIAG 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-250 |
1.35e-63 |
|
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: 202.04 E-value: 1.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:cd03258 1 MIELKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DREL---RRRMQIVFQDpGGSMNPRmSVRSIVGEPLQVNRLaEGAELTQKVADVLDSVGLKREHmNRFPHEFSGGQKQRL 167
Cdd:cd03258 74 GKELrkaRRRIGMIFQH-FNLLSSR-TVFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 168 ALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 663511184 248 DKP 250
Cdd:cd03258 230 ANP 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
35-241 |
2.73e-62 |
|
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: 198.13 E-value: 2.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRelRRRMQIVFQDPggSMNPRMS 114
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDY--ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:cd03259 89 VAENIAFGLKLRGVPK-AEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIA 241
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-281 |
4.27e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 201.95 E-value: 4.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKGGmlsevKIHvrAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:PRK11153 2 IELKNISKVFPQGGR-----TIH--ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RELRR-RMQI--VFQdpggSMNpRMSVRSIVGE---PLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQ 165
Cdd:PRK11153 75 KELRKaRRQIgmIFQ----HFN-LLSSRTVFDNvalPLELAGTPK-AEIKARVTELLELVGLS-DKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTAD 245
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 663511184 246 LFDKPAHPYTHALMSA-----IPEPSLEKASRERIVLSGDV 281
Cdd:PRK11153 228 VFSHPKHPLTREFIQStlhldLPEDYLARLQAEPTTGSGPL 268
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-254 |
7.70e-62 |
|
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: 197.72 E-value: 7.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFpikggmlSEVKIHvravDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRT--- 88
Cdd:cd03261 1 IELRGLTKSF-------GGRTVL----KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 IPDRELRRRMQIVFQDpgGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHmNRFPHEFSGGQKQRLA 168
Cdd:cd03261 70 AELYRLRRRMGMLFQS--GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 169 LARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFD 248
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*.
gi 663511184 249 KPaHPY 254
Cdd:cd03261 227 SD-DPL 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
34-251 |
2.31e-60 |
|
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: 193.61 E-value: 2.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRelRRRMQIVFQDPggSMNPRM 113
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNY--ALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03300 88 TVFENIAFGLRLKKLPK-AEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITH----ALNVvnhiSDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHdqeeALTM----SDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-239 |
5.25e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.57 E-value: 5.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 9 KVLIEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRT 88
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 IPDRELR--RRMQI--VFQDPggsmN--PRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGG 162
Cdd:COG1136 75 LSERELArlRRRHIgfVFQFF----NllPELTALENVALPLLLAGVSR-KERRERARELLERVGLG-DRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVE 239
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-262 |
6.91e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 192.90 E-value: 6.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFpikGGMlsevkiHVraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrTIP 90
Cdd:COG1126 1 MIEIENLHKSF---GDL------EV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 D---RELRRRMQIVFQdpggSMN--PRMSVRSIVGE-PLQVNRLAEgAELTQKVADVLDSVGLkREHMNRFPHEFSGGQK 164
Cdd:COG1126 69 KkdiNKLRRKVGMVFQ----QFNlfPHLTVLENVTLaPIKVKKMSK-AEAEERAMELLERVGL-ADKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 165 QRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTA 244
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
250
....*....|....*...
gi 663511184 245 DLFDKPAHPYTHALMSAI 262
Cdd:COG1126 222 EFFENPQHERTRAFLSKV 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
35-247 |
1.99e-59 |
|
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: 191.39 E-value: 1.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGgsmnpRMS 114
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPD-----DQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGE-----PLqvNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:COG1122 89 FAPTVEEdvafgPE--NLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 190 DVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:COG1122 166 DPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-240 |
7.20e-59 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 190.69 E-value: 7.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 9 KVLIEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRt 88
Cdd:COG1116 5 APALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 ipdrELRRRMQIVFQDPggSMNPRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLA 168
Cdd:COG1116 77 ----GPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPK-AERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 169 LARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITH----ALnvvnHISDRVAVM--YLGKIVEI 240
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHdvdeAV----FLADRVVVLsaRPGRIVEE 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-237 |
1.38e-58 |
|
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: 188.85 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKGgmlsevkIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:cd03255 1 IELKNLSKTYGGGG-------EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 REL----RRRMQIVFQDPggsmN--PRMSVRSIVGEPLQVNRLaEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQ 165
Cdd:cd03255 74 KELaafrRRHIGFVFQSF----NllPDLTALENVELPLLLAGV-PKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKI 237
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
35-328 |
1.48e-58 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 192.43 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP----ITDGSVLYDGEDIRTIPDRELR----RRMQIVFQDPG 106
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRkiigREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSV-----RSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK--REHMNRFPHEFSGGQKQRLALARALSLDPEF 179
Cdd:COG4170 100 SCLDPSAKIgdqliEAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 180 ILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALM 259
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 260 SAIPEPSLEKASRERIV-LSGDVPSPANPPPGCRFHTRCPIAvEGVCdVVDPPLETIdfDDHAVACHFPL 328
Cdd:COG4170 260 RSMPDFRQPLPHKSRLNtLPGSIPPLQHLPIGCRLGPRCPYA-QKKC-VETPRLRKI--KGHEFACHFPL 325
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-243 |
5.01e-58 |
|
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: 187.39 E-value: 5.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPI-----TDGSVLYDGEDI 86
Cdd:cd03260 1 IELRDLNVYY---GD--------KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDR--ELRRRMQIVFQDPggsmNP-RMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNR-FPHEFSGG 162
Cdd:cd03260 70 YDLDVDvlELRRRVGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVMYLGKIVEIAN 242
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
.
gi 663511184 243 T 243
Cdd:cd03260 224 T 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
37-236 |
1.18e-57 |
|
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: 186.13 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsmnPRMSVR 116
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNP-----DDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPL---QVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03225 91 PTVEEEVafgLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 663511184 194 QAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGK 236
Cdd:cd03225 170 RRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-246 |
1.80e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 1.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPd 91
Cdd:COG1131 1 IEVRGLTKRY---GD--------KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RELRRRMQIVFQDPGgsMNPRMSVR-------SIVGEPlqvnrlaeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQK 164
Cdd:COG1131 69 AEVRRRIGYVPQEPA--LYPDLTVRenlrffaRLYGLP--------RKEARERIDELLELFGLT-DAADRKVGTLSGGMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 165 QRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTA 244
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
..
gi 663511184 245 DL 246
Cdd:COG1131 217 EL 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
36-264 |
2.37e-57 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 194.54 E-value: 2.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP-----ITDGSVLYDGEDIRTIPDRELRR----RMQIVFQDPG 106
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK--REHMNRFPHEFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMSAIPE 264
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-232 |
1.25e-56 |
|
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: 183.83 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKGGmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRtipd 91
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 rELRRRMQIVFQDPggSMNPRMSVRSIVGEPLQVNRLAeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALAR 171
Cdd:cd03293 70 -GPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVP-KAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511184 172 ALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVM 232
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
37-254 |
8.78e-56 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 183.23 E-value: 8.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDREL----RRRMQIVFQDPGgsMNPR 112
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFA--LLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLK-REHmnRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:cd03294 117 RTVLENVAFGLEVQGVPR-AEREERAAEALELVGLEgWEH--KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 192 SVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPY 254
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-236 |
2.02e-55 |
|
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: 179.31 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:cd03229 1 LELKNVSKRYG-----------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 --RELRRRMQIVFQDPGgsMNPRMSVRSIVGEPLqvnrlaegaeltqkvadvldsvglkrehmnrfphefSGGQKQRLAL 169
Cdd:cd03229 70 elPPLRRRIGMVFQDFA--LFPHLTVLENIALGL------------------------------------SGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 170 ARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGK 236
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
35-252 |
5.47e-55 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 183.74 E-value: 5.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrRRMQIVFQDPGgsMNPRMS 114
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQSYA--LYPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:COG3839 92 VYENIAFPLKLRKVPK-AEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITH----ALNvvnhISDRVAVMYLGKIVEIANTADLFDKPAH 252
Cdd:COG3839 170 VEMRAEIKRLHRRLGTTTIYVTHdqveAMT----LADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-259 |
8.98e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 183.04 E-value: 8.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRT-IP 90
Cdd:COG1118 3 IEVRNISKRFG-----------SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DRElrRRMQIVFQDPGgsMNPRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLAL 169
Cdd:COG1118 72 PRE--RRVGFVFQHYA--LFPHMTVAENIAFGLRVRPPSK-AEIRARVEELLELVQL--EGLaDRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 170 ARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITH----ALNVvnhiSDRVAVMYLGKIVEIANTAD 245
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHdqeeALEL----ADRVVVMNQGRIEQVGTPDE 220
|
250
....*....|....
gi 663511184 246 LFDKPAHPYTHALM 259
Cdd:COG1118 221 VYDRPATPFVARFL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
38-256 |
2.61e-54 |
|
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: 178.70 E-value: 2.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggSMNPRMSVRS 117
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP--PAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVG---EPLQVNRLAEGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:COG1120 95 LVAlgrYPHLGLFGRPSAEDREAVEEALERTGL--EHLaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV------EI---ANTADLFDKPAHPYTH 256
Cdd:COG1120 173 QLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaqgppeEVltpELLEEVYGVEARVIED 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
37-254 |
2.54e-53 |
|
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: 175.95 E-value: 2.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGgsMNPRMSVR 116
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIG--LFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRLAEgAELTQKVADVLDSVGLK-REHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:cd03295 94 ENIALVPKLLKWPK-EKIRERADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPY 254
Cdd:cd03295 173 QLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-255 |
1.17e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 174.84 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 1 MTEESRDGKVLIEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVL---LGLIPI--T 75
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYY---GD--------KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGarV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 76 DGSVLYDGEDI--RTIPDRELRRRMQIVFQDPggsmNP-RMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKRE-- 150
Cdd:COG1117 70 EGEILLDGEDIydPDVDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEvk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 151 -HMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD-VSVqAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDR 228
Cdd:COG1117 146 dRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|....*..
gi 663511184 229 VAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-254 |
1.77e-52 |
|
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: 173.68 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:cd03296 3 IEVRNVSKRFG-----------DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RElrRRMQIVFQDPggSMNPRMSVRSIVGEPLQVNRLAEG---AELTQKVADVLDSVGLKReHMNRFPHEFSGGQKQRLA 168
Cdd:cd03296 72 QE--RNVGFVFQHY--ALFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 169 LARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITH----ALNVvnhiSDRVAVMYLGKIVEIANTA 244
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHdqeeALEV----ADRVVVMNKGRIEQVGTPD 222
|
250
....*....|
gi 663511184 245 DLFDKPAHPY 254
Cdd:cd03296 223 EVYDHPASPF 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
37-239 |
9.59e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 168.69 E-value: 9.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRE---LRRRMQIVFQDpgGSMNPRM 113
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRIGVVFQD--FRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:COG2884 95 TVYENVALPLRVTGKSR-KEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 663511184 194 QAQVLNLLEEIQeKLGLTFVFITHALNVVNHISDRVAVMYLGKIVE 239
Cdd:COG2884 173 SWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
35-328 |
2.21e-50 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 171.14 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGL----IPITDGSVLYDGEDIRTIPDRELRR----RMQIVFQDPG 106
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNP-----RMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK--REHMNRFPHEFSGGQKQRLALARALSLDPEF 179
Cdd:PRK15093 100 SCLDPservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 180 ILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALM 259
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 260 SAIPEPSLEKASRERI-VLSGDVPSPANPPPGCRFHTRCPIAvEGVCdVVDPPLETIdfDDHAVACHFPL 328
Cdd:PRK15093 260 RAIPDFGSAMPHKSRLnTLPGAIPLLEHLPIGCRLGPRCPYA-QREC-IETPRLTGA--KNHLYACHFPL 325
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-249 |
7.53e-50 |
|
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: 166.96 E-value: 7.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:COG4555 1 MIEVENLSKKYG-----------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 dRELRRRMQIVFQDPGGSmnPRMSVRSIVGEPLQVNRLAeGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALA 170
Cdd:COG4555 70 -REARRQIGVLPDERGLY--DRLTVRENIRYFAELYGLF-DEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 171 RALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQeKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDK 249
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
36-262 |
8.12e-49 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 164.71 E-value: 8.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE-----DIRTIPDRELRRRMQ----IVFQDPG 106
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLRtewgFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSVRSIVGEPLqvnrLAEGA----ELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILL 182
Cdd:PRK11701 100 DGLRMQVSAGGNIGERL----MAVGArhygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMSAI 262
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-264 |
1.15e-48 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 173.12 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE----------DIRTIPDRELRR----RMQI 100
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHvrgaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 101 VFQDPGGSMNPRMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHM--NRFPHEFSGGQKQRLALARALSLDPE 178
Cdd:PRK10261 109 IFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 179 FILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHAL 258
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRAL 268
|
....*.
gi 663511184 259 MSAIPE 264
Cdd:PRK10261 269 LAAVPQ 274
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
39-237 |
1.54e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.29 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGgsMnPRMSVRSI 118
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA--L-WGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 VGEPLQvnrLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVL 198
Cdd:COG4619 94 LPFPFQ---LRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 663511184 199 NLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:COG4619 171 ELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
28-236 |
3.23e-48 |
|
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: 159.72 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQdpgg 107
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 smnprmsvrsivgeplqvnrlaegaeltqkvadvldsvglkrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTS 187
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 663511184 188 ALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGK 236
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-237 |
4.82e-48 |
|
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: 159.87 E-value: 4.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPd 91
Cdd:cd03230 1 IEVRNLSKRYG-----------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RELRRRMQIVFQDPggSMNPRMSVRsivgeplqvnrlaegaeltqkvadvldsvglkrEHMnrfphEFSGGQKQRLALAR 171
Cdd:cd03230 69 EEVKRRIGYLPEEP--SLYENLTVR---------------------------------ENL-----KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 172 ALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
37-254 |
7.76e-48 |
|
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: 171.56 E-value: 7.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSM--NP 111
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVflfSGTIreNI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIvgEPLQVNRLAEGAELTQKVadvldsvglkrehmNRFPH-----------EFSGGQKQRLALARALSLDPEFI 180
Cdd:COG2274 570 TLGDPDA--TDEEIIEAARLAGLHDFI--------------EALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 181 LLDEPTSALDVSVQAQVLNLLEEIqeKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKPAHPY 254
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-262 |
8.46e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 161.76 E-value: 8.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:COG3638 2 MLELRNLSKRYP--GG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DREL---RRRMQIVFQDPGgsMNPRMSV---------------RSIVGeplqvnRLAEgaELTQKVADVLDSVGLKrEHM 152
Cdd:COG3638 72 GRALrrlRRRIGMIFQQFN--LVPRLSVltnvlagrlgrtstwRSLLG------LFPP--EDRERALEALERVGLA-DKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 153 NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVM 232
Cdd:COG3638 141 YQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGL 220
|
250 260 270
....*....|....*....|....*....|
gi 663511184 233 YLGKIVeiantadlFDKPAHPYTHALMSAI 262
Cdd:COG3638 221 RDGRVV--------FDGPPAELTDAVLREI 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
35-241 |
7.22e-47 |
|
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: 158.19 E-value: 7.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrRRMQIVFQDPggSMNPRMS 114
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNY--ALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:cd03301 89 VYDNIAFGLKLRKVPK-DEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITH----ALNvvnhISDRVAVMYLGKIVEIA 241
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHdqveAMT----MADRIAVMNDGQIQQIG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
37-236 |
1.71e-46 |
|
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: 156.00 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSmnprm 113
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPflfSGT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 svrsivgeplqvnrlaegaeltqkVADVLdsvglkrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03228 92 ------------------------IRENI----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 663511184 194 QAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGK 236
Cdd:cd03228 132 EALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
38-261 |
1.87e-46 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 158.71 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP----ITDGSVLYDGEDIRTipdRELR-RRMQIVFQDPGGSMNPR 112
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAP---CALRgRKIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSIVGEPL-QVNRLAEGAELtqkvADVLDSVGLKREH--MNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:PRK10418 96 HTMHTHARETClALGKPADDATL----TAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 190 DVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMSA 261
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-238 |
2.28e-46 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 158.28 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 8 GKVLIEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIR 87
Cdd:COG0411 1 SDPLLEVRGLTKRF---GG--------LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 88 TIPDRElRRRMQIV--FQDPggSMNPRMSVR-------------SIVGEPLQVNR-LAEGAELTQKVADVLDSVGLkREH 151
Cdd:COG0411 70 GLPPHR-IARLGIArtFQNP--RLFPELTVLenvlvaaharlgrGLLAALLRLPRaRREEREARERAEELLERVGL-ADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 152 MNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAV 231
Cdd:COG0411 146 ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVV 225
|
....*..
gi 663511184 232 MYLGKIV 238
Cdd:COG0411 226 LDFGRVI 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-255 |
4.62e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 160.88 E-value: 4.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 1 MTEESRDGKVLIEVKGMKKWFPIKggmlsevkihvRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVL 80
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGK-----------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 81 YDGEDIRTIPDRelRRRMQIVFQDPggSMNPRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLkrEHM-NRFPHEF 159
Cdd:PRK09452 73 LDGQDITHVPAE--NRHVNTVFQSY--ALFPHMTVFENVAFGLRMQKTPA-AEITPRVMEALRMVQL--EEFaQRKPHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 160 SGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITH----ALNvvnhISDRVAVMYLG 235
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdqeeALT----MSDRIVVMRDG 221
|
250 260
....*....|....*....|
gi 663511184 236 KIVEIANTADLFDKPAHPYT 255
Cdd:PRK09452 222 RIEQDGTPREIYEEPKNLFV 241
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-237 |
7.34e-46 |
|
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: 155.77 E-value: 7.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKggmlsevkiHVraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrTIPD 91
Cdd:cd03262 1 IEIKNLHKSFGDF---------HV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 R---ELRRRMQIVFQdpggSMN--PRMSV-RSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQ 165
Cdd:cd03262 69 KninELRQKVGMVFQ----QFNlfPHLTVlENITLAPIKVKGMSK-AEAEERALELLEKVGLA-DKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
36-238 |
1.01e-45 |
|
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: 154.13 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQdpggsmnprmsv 115
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 rsivgeplqvnrlaegaeltqkvadVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:cd03214 81 -------------------------ALELLGL--AHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
34-247 |
1.74e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 156.44 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTiPDR--ELRRRMQIVFQDPGGSMnp 111
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EENlwEIRKKVGMVFQNPDNQF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 rmsVRSIVG-------EPLQVNRlaegAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:TIGR04520 91 ---VGATVEddvafglENLGVPR----EEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALN-VVNhiSDRVAVMYLGKIVEIANTADLF 247
Cdd:TIGR04520 163 ATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-251 |
4.16e-45 |
|
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: 154.65 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:cd03256 1 IEVENLSKTYP--NG--------KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 REL---RRRMQIVFQDPGgsMNPRMSVrsivGEPLQVNRLAE-----------GAELTQKVADVLDSVGLkREHMNRFPH 157
Cdd:cd03256 71 KALrqlRRQIGMIFQQFN--LIERLSV----LENVLSGRLGRrstwrslfglfPKEEKQRALAALERVGL-LDKAYQRAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 158 EFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
250
....*....|....
gi 663511184 238 VeiantadlFDKPA 251
Cdd:cd03256 224 V--------FDGPP 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
36-250 |
4.25e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 155.69 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD---RELRRRMQIVFQDPG------ 106
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklKDLRKKVGLVFQFPEhqlfee 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 --------GSMNPRMSvrsivgeplqvnrlaeGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPE 178
Cdd:TIGR04521 99 tvykdiafGPKNLGLS----------------EEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 179 FILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:TIGR04521 163 VLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-187 |
5.17e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 151.26 E-value: 5.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggSMNPRMSVRS 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 118 IVGEPLQVNRLAEgAELTQKVADVLDSVGLK---REHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTS 187
Cdd:pfam00005 79 NLRLGLLLKGLSK-REKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
53-288 |
1.01e-44 |
|
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: 156.11 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 53 IVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRelRRRMQIVFQDPggSMNPRMSVRSIVGEPLQVNRLAEgA 132
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSY--ALFPHMTVEENVAFGLKMRKVPR-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 133 ELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTF 212
Cdd:TIGR01187 76 EIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 213 VFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALM--SAIPEPSLEKASRERIVLSG----------D 280
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIgeINVFEATVIERKSEQVVLAGvegrrcdiytD 234
|
....*...
gi 663511184 281 VPSPANPP 288
Cdd:TIGR01187 235 VPVEKDQP 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-255 |
1.14e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 153.92 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLI-----PITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSm 109
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 nPRMSVRSIVGEPLQVNRLAEG-AELTQKVADVLDSVGLKREHMNRF---PHEFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK14247 95 -PNLSIFENVALGLKLNRLVKSkKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-238 |
1.21e-44 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 153.36 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:cd03219 1 LEVRGLTKRF---GG--------LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RElRRRMQIV--FQDPG--GSM----NPRMSVRSIVGEP-LQVNRLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGG 162
Cdd:cd03219 70 HE-IARLGIGrtFQIPRlfPELtvleNVMVAAQARTGSGlLLARARREEREARERAEELLERVGL-ADLADRPAGELSYG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
38-250 |
7.56e-43 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 148.64 E-value: 7.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRelRRRMQIVFQDPggSMNPRMSVRS 117
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNY--ALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVGEPLQvNRLAEGAELTQKVADVLDSVGLkrEH-MNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQ 196
Cdd:cd03299 91 NIAYGLK-KRKVDKKEIERKVLEIAEMLGI--DHlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 663511184 197 VLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
34-253 |
1.27e-42 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 148.32 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIR--TIPDRELRRRMQIVFQDpgGSMNP 111
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQ--FYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMS-VRSIVGEPLQVnRLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK09493 91 HLTaLENVMFGPLRV-RGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 191 VSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHP 253
Cdd:PRK09493 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
36-246 |
3.68e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 154.15 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP----Ggsmnp 111
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPylfaG----- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 rmSVRSIVgeplqvnRLAE-GAELTQkVADVLDSVGLkREHMNRFPHEF-----------SGGQKQRLALARALSLDPEF 179
Cdd:COG4988 426 --TIRENL-------RLGRpDASDEE-LEAALEAAGL-DEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 180 ILLDEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADL 246
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-253 |
4.75e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.44 E-value: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 42 DLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrRRMQIVFQDpggsmN---PRMSVRSI 118
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQE-----NnlfPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 VGEPLQVN-RLaeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQV 197
Cdd:COG3840 92 IGLGLRPGlKL--TAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 198 LNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHP 253
Cdd:COG3840 169 LDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
37-240 |
8.53e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.40 E-value: 8.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP----Ggsmnpr 112
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTflfsG------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 mSVRSivgeplqvN-RL----AEGAELTQ--KVADVLDSVglkrehmNRFPH-----------EFSGGQKQRLALARALS 174
Cdd:COG1132 429 -TIRE--------NiRYgrpdATDEEVEEaaKAAQAHEFI-------EALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 175 LDPEFILLDEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEI 240
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-246 |
9.50e-42 |
|
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: 145.21 E-value: 9.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPd 91
Cdd:cd03265 1 IEVENLVKKY---GD--------FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RELRRRMQIVFQDPggSMNPRMSVRsivgEPLQVN-RLA--EGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLA 168
Cdd:cd03265 69 REVRRRIGIVFQDL--SVDDELTGW----ENLYIHaRLYgvPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 169 LARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADL 246
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-238 |
2.81e-41 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 142.18 E-value: 2.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTI-P 90
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DRELRRRMQIVFQdpggsmnprmsvrsivgeplqvnrlaegaeltqkvadvldsvglkrehmnrfpheFSGGQKQRLALA 170
Cdd:cd03216 70 RDARRAGIAMVYQ-------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 171 RALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
38-251 |
8.65e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 146.40 E-value: 8.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI--RTIPDRELrrrmQIVFQDPggSMNPRMSV 115
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDI----CMVFQSY--ALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK11432 96 GENVGYGLKMLGVPK-EERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:PRK11432 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
37-254 |
1.82e-40 |
|
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: 149.53 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSmnprm 113
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPhlfDTT----- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 svrsiVGEPLqvnRLAEGAELTQKVADVLDSVGLkREHMNRFPH-----------EFSGGQKQRLALARALSLDPEFILL 182
Cdd:COG4987 425 -----LRENL---RLARPDATDEELWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEI-QEKlglTFVFITHALNVVNHIsDRVAVMYLGKIVEIANTADLFDKPAHPY 254
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEAlAGR---TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
34-257 |
5.87e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.38 E-value: 5.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRtipdrelRRRMQI--VFQDpgGSMNP 111
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRIgyVPQR--AEVDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 R--MSVRSIVGeplqVNRLAE-------GAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILL 182
Cdd:COG1121 89 DfpITVRDVVL----MGRYGRrglfrrpSRADREAVDEALERVGL-EDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVM-----YLGKIVEI---ANTADLFDKPAHPY 254
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLnrglvAHGPPEEVltpENLSRAYGGPVALL 242
|
...
gi 663511184 255 THA 257
Cdd:COG1121 243 AHG 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
41-241 |
6.48e-40 |
|
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: 140.12 E-value: 6.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKrGETLGIVGESGCGKTTLGRVLLGLIPIT------DGSVLYDGEDIRTIPDRelRRRMQIVFQDpgGSMNPRMS 114
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlNGTVLFDSRKKINLPPQ--QRKIGLVFQQ--YALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRlaeGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03297 92 VRENLAFGLKRKR---NREDRISVDELLDLLGL--DHLlNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIA 241
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-262 |
1.52e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 140.13 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:TIGR02315 1 MLEVENLSKVYP--NG--------KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DREL---RRRMQIVFQDpggsMN--PRMSVRsivgEPLQVNRLA------------EGAElTQKVADVLDSVGLKREHMN 153
Cdd:TIGR02315 71 GKKLrklRRRIGMIFQH----YNliERLTVL----ENVLHGRLGykptwrsllgrfSEED-KERALSALERVGLADKAYQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 154 RfPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMY 233
Cdd:TIGR02315 142 R-ADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLK 220
|
250 260
....*....|....*....|....*....
gi 663511184 234 LGKIVeiantadlFDKPAHPYTHALMSAI 262
Cdd:TIGR02315 221 AGEIV--------FDGAPSELDDEVLRHI 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
37-255 |
1.54e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.82 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPdrELRRRMQIVFQDPggSMNPRMSVR 116
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSY--ALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQ 196
Cdd:PRK11607 110 QNIAFGLKQDKLPK-AEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 197 VLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK11607 188 MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-238 |
2.76e-39 |
|
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: 138.65 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFpikggmlSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:cd03266 1 MITADALTKRF-------RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 dRELRRRMQIVFQDPGgsMNPRMSVRSIVGEPLQVNRLaEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALA 170
Cdd:cd03266 74 -AEARRRLGFVSDSTG--LYDRLTARENLEYFAGLYGL-KGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 171 RALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEkLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-238 |
7.62e-39 |
|
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: 137.00 E-value: 7.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDirtIPDRELRRRMQIVFQDPGGSMNpRMSV 115
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQDVDYQLF-TDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQvnRLAEGAELTQKVADVLDSVGLKREHmnrfPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:cd03226 90 REELLLGLK--ELDAGNEQAETVLKDLDLYALKERH----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 663511184 196 QVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03226 164 RVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-251 |
8.47e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 141.37 E-value: 8.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD 91
Cdd:PRK10851 3 IEIANIKKSFG-----------RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 RElrRRMQIVFQDPggSMNPRMSVRSIVGEPLQV---NRLAEGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRL 167
Cdd:PRK10851 72 RD--RKVGFVFQHY--ALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL--AHLaDRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 168 ALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
....
gi 663511184 248 DKPA 251
Cdd:PRK10851 226 REPA 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
39-217 |
1.75e-38 |
|
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: 136.07 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDrELRRRMQIVFQDPGgsMNPRMSVRsi 118
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHADG--LKPELTVR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 vgEPLQ-VNRLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQV 197
Cdd:COG4133 94 --ENLRfWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180
....*....|....*....|
gi 663511184 198 LNLLEEIQEKlGLTFVFITH 217
Cdd:COG4133 171 AELIAAHLAR-GGAVLLTTH 189
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-239 |
2.69e-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: 136.41 E-value: 2.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIKGGMLSevkihvrAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:COG4181 8 IIELRGLTKTVGTGAGELT-------ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DREL----RRRMQIVFQdpggSMN--PRMSVRSIVGEPLQvnrLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQK 164
Cdd:COG4181 81 EDARarlrARHVGFVFQ----SFQllPTLTALENVMLPLE---LAGRRDARARARALLERVGLG-HRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 165 QRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVE 239
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
37-249 |
3.74e-38 |
|
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: 136.20 E-value: 3.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPG---GSM--NP 111
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFlfsGTImeNI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIVGEplQVNRLAEGAELTQKVADVLDsvGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:cd03254 98 RLGRPNATDE--EVIEAAKEAGAHDFIMKLPN--GYD-TVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 192 SVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:cd03254 173 ETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
40-260 |
1.44e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.48 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRE-------------LRRRMQIVFQDpg 106
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSVRSIVGE-PLQVNRLAEgAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK10619 101 FNLWSHMTVLENVMEaPIQVLGLSK-QEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMS 260
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
37-238 |
1.77e-37 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 142.31 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPG---GSM--NP 111
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRlfyGTLrdNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIVGEplqvnRLAEGAELtqkvADVLDSVGLKREHMNRFPHE----FSGGQKQRLALARALSLDPEFILLDEPTS 187
Cdd:TIGR03375 560 ALGAPYADDE-----EILRAAEL----AGVTEFVRRHPDGLDMQIGErgrsLSGGQRQAVALARALLRDPPILLLDEPTS 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 188 ALDVSVQAQVL-NLLEEIQEKlglTFVFITH---ALNVVnhisDRVAVMYLGKIV 238
Cdd:TIGR03375 631 AMDNRSEERFKdRLKRWLAGK---TLVLVTHrtsLLDLV----DRIIVMDNGRIV 678
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-247 |
2.13e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.53 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE--DIRTIPDreLRRRMQIVFQDPG----GSmn 110
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWD--VRRQVGMVFQNPDnqfvGA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 prmSVRSIVGEPLQvNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK13635 98 ---TVQDDVAFGLE-NIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 191 VSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-246 |
2.24e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.15 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 9 KVLIEVKGMKKWFPikgGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRT 88
Cdd:COG1129 2 EPLLEMRGISKSFG---G--------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 IPDRE-LRRRMQIVFQDPggSMNPRMSV-------RSIVGEPLqVNRlaegAELTQKVADVLDSVGLkreHMNrfPH--- 157
Cdd:COG1129 71 RSPRDaQAAGIAIIHQEL--NLVPNLSVaeniflgREPRRGGL-IDW----RAMRRRARELLARLGL---DID--PDtpv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 158 -EFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGK 236
Cdd:COG1129 139 gDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGR 217
|
250
....*....|
gi 663511184 237 IVEIANTADL 246
Cdd:COG1129 218 LVGTGPVAEL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-237 |
2.54e-37 |
|
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: 133.30 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRE---LRRRMQIVFQDpgGSMNP 111
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIVGEPLQVNRlAEGAELTQKVADVLDSVGLKREHmNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:cd03292 92 DRNVYENVAFALEVTG-VPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 663511184 192 SVQAQVLNLLEEIQeKLGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:cd03292 170 DTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
34-232 |
3.51e-37 |
|
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: 133.04 E-value: 3.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdirtiPDRELRRRMQIVFQDPGGSMNPRM 113
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLqVNRLAEGAELT----QKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:cd03235 86 SVRDVVLMGL-YGHKGLFRRLSkadkAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 663511184 190 DVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVM 232
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
37-238 |
8.02e-37 |
|
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: 132.33 E-value: 8.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPG---GSMNPRM 113
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTlfyGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLK-REH-MNrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:cd03245 99 TLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQiGERgRG-----LSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663511184 192 SVQAQVL-NLLEEIQEKlglTFVFITH---ALNVVnhisDRVAVMYLGKIV 238
Cdd:cd03245 174 NSEERLKeRLRQLLGDK---TLIIITHrpsLLDLV----DRIIVMDSGRIV 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
41-250 |
1.58e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 132.06 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLlGLIPITDGSVLY---DGEDIRTIPD----RELRRRMQIVFQDPggSMNPRM 113
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNiagNHFDFSKTPSdkaiRELRRNVGMVFQQY--NLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVR-SIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK11124 98 TVQqNLIEAPCRVLGLSK-DQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 193 VQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIAnTADLFDKP 250
Cdd:PRK11124 176 ITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQP 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
34-254 |
1.58e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 131.89 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSM- 109
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPvlfDGTIa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 -NPRMSVRS-IVGEPLQVNRLAEGAELTQKVADVLDS-VGlkrehmnrfPH--EFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:cd03249 95 eNIRYGKPDaTDEEVEEAAKKANIHDFIMSLPDGYDTlVG---------ERgsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 185 PTSALDVSVQAQVLNLLEEIqeKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKPAHPY 254
Cdd:cd03249 166 ATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
36-247 |
1.70e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.25 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI--RTIPDRELRRRMQIVFQDPGGSMNPRM 113
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPlqVNRLAEGAELTQKVADVLDSVGLKREHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK13637 101 IEKDIAFGP--INLGLSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 193 VQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-255 |
3.39e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.50 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPIT-----DGSVLYDGEDIRTiPDR---ELRRRMQIVFQDPggSM 109
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYS-PDVdpiEVRREVGMVFQYP--NP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 NPRMSVRSIVGEPLQVNRLAEG-AELTQKVADVLDSVGLKREHMNR---FPHEFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSkKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
37-238 |
7.77e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 131.36 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDR-ELRRRMQIVFQDPGGSMnprmsV 115
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNPDNQI-----V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQV---NRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK13633 100 ATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 663511184 193 VQAQVLNLLEEIQEKLGLTFVFITHALN-VVNhiSDRVAVMYLGKIV 238
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEeAVE--ADRIIVMDSGKVV 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
37-246 |
9.49e-36 |
|
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: 129.55 E-value: 9.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDrELRRRMQIVFQDpgGSMNPRMSVR 116
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK-AARQSLGYCPQF--DALFDELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sivgEPLQ-------VNRLAEGAEltqkVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:cd03263 94 ----EHLRfyarlkgLPKSEIKEE----VELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 190 DVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADL 246
Cdd:cd03263 165 DPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
37-249 |
2.17e-35 |
|
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: 128.89 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLgrvlLGLIP----ITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSM 109
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTL----VNLIPrfydVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVflfNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 --NPRMSVRSIVGEP-LQVNRLAEGAELTQKVADVLDSV----GLKrehmnrfpheFSGGQKQRLALARALSLDPEFILL 182
Cdd:cd03251 93 aeNIAYGRPGATREEvEEAARAANAHEFIMELPEGYDTVigerGVK----------LSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
34-217 |
2.18e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.60 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrTIPDRElrrRmQIVFQDPGgsMNPRM 113
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGAD---R-GVVFQKDA--LLPWL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:COG4525 92 NVLDNVAFGLRLRGVPK-AERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170 180
....*....|....*....|....
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITH 217
Cdd:COG4525 170 REQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
32-238 |
2.20e-35 |
|
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: 128.71 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 32 KIHVraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElRRRMQIVFQDPGGSMNP 111
Cdd:cd03224 12 KSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRsivgEPLqvnRLAEGAELTQKVADVLDSVglkrehMNRFP--HEF--------SGGQKQRLALARALSLDPEFIL 181
Cdd:cd03224 89 ELTVE----ENL---LLGAYARRRAKRKARLERV------YELFPrlKERrkqlagtlSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 182 LDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-252 |
2.72e-35 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 128.74 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI-RTIPDRelrrrmQIVFQDPggSMNPRMSVR 116
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDR------MVVFQNY--SLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPL-QVNRLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:TIGR01184 73 ENIALAVdRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVM------YLGKIVEIAntadlFDKPAH 252
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVP-----FPRPRD 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-260 |
3.06e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 129.10 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFpiKGGmlsevkihvRAVDGVDLQIKRGETLGIVGESGCGKTTL------------GRVLLGLIPITDGSV 79
Cdd:PRK11264 4 IEVKNLVKKF--HGQ---------TVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcinlleqpeaGTIRVGDITIDTARS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 80 LydGEDIRTIpdRELRRRMQIVFQdpggSMN--P-RMSVRSIVGEPLQVNRLAEGaELTQKVADVLDSVGLKREHmNRFP 156
Cdd:PRK11264 73 L--SQQKGLI--RQLRQHVGFVFQ----NFNlfPhRTVLENIIEGPVIVKGEPKE-EATARARELLAKVGLAGKE-TSYP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 157 HEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEI-QEKlgLTFVFITHALNVVNHISDRVAVMYLG 235
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEK--RTMVIVTHEMSFARDVADRAIFMDQG 220
|
250 260
....*....|....*....|....*
gi 663511184 236 KIVEIANTADLFDKPAHPYTHALMS 260
Cdd:PRK11264 221 RIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-251 |
3.54e-35 |
|
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: 131.76 E-value: 3.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 27 MLsEVKIHVR----AVDgVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP-----IT-DGSVLYDGEDIRTIPDRelRR 96
Cdd:COG4148 2 ML-EVDFRLRrggfTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERpdsgrIRlGGEVLQDSARGIFLPPH--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 97 RMQIVFQDPggSMNPRMSVRSivgeplqvN-----RLAEGAELTQKVADVLDSVGLkrEH-MNRFPHEFSGGQKQRLALA 170
Cdd:COG4148 78 RIGYVFQEA--RLFPHLSVRG--------NllygrKRAPRAERRISFDEVVELLGI--GHlLDRRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 171 RALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
.
gi 663511184 251 A 251
Cdd:COG4148 226 D 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
27-238 |
3.66e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.12 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 27 MLSEVKIHVRA-----VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIV 101
Cdd:PRK13548 2 MLEARNLSVRLggrtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 102 FQDPggSMNPRMSVRSIVG---EPLQVNRlaegAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARAL---- 173
Cdd:PRK13548 82 PQHS--SLSFPFTVEEVVAmgrAPHGLSR----AEDDALVAAALAQVDL--AHLaGRDYPQLSGGEQQRVQLARVLaqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 174 --SLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK13548 154 epDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-255 |
3.89e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 129.01 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPI------TDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggSMNPRMS 114
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP--NPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKRE---HMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK14246 107 IYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEvydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 192 SVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK14246 187 VNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
37-247 |
4.40e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.34 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPG----GSmnpr 112
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDnqfiGA---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 mSVRSIVGEPLQvNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK13632 100 -TVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 193 VQAQVLNLLEEIQEKLGLTFVFITHALN-VVNhiSDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
37-262 |
1.68e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.92 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELR--RRMQIVFQDPGGSMNPRMS 114
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:PRK10070 123 VLDNTAFGMELAGIN-AEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALMSAI 262
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
40-250 |
2.42e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.84 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGL-IPiTDGSVLYDGEDIRTIPDRE-------------LRRRMQIVFQdp 105
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTP-DSGEIRVGGEEIRLKPDRDgelvpadrrqlqrIRTRLGMVFQ-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 106 ggSMN--PRMSVRSIVGE-PLQVNRLAEgAELTQKVADVLDSVGL--KREHmnrFPHEFSGGQKQRLALARALSLDPEFI 180
Cdd:COG4598 103 --SFNlwSHMTVLENVIEaPVHVLGRPK-AEAIERAEALLAKVGLadKRDA---YPAHLSGGQQQRAAIARALAMEPEVM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 181 LLDEPTSALDVSVQAQVL----NLLEEiqeklGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:COG4598 177 LFDEPTSALDPELVGEVLkvmrDLAEE-----GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-246 |
5.12e-34 |
|
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: 131.46 E-value: 5.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 3 EESRDGKVLIEVKGMKK-WFPIKGGMlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY 81
Cdd:TIGR03269 271 CEVEVGEPIIKVRNVSKrYISVDRGV-------VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 82 D-GEDI--RTIPDRELRRR----MQIVFQDPGgsMNPRMSVRSIVGEPLQVNRLAEGAELtqKVADVLDSVGLK----RE 150
Cdd:TIGR03269 344 RvGDEWvdMTKPGPDGRGRakryIGILHQEYD--LYPHRTVLDNLTEAIGLELPDELARM--KAVITLKMVGFDeekaEE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 151 HMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVA 230
Cdd:TIGR03269 420 ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*.
gi 663511184 231 VMYLGKIVEIANTADL 246
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEI 515
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
37-250 |
5.67e-34 |
|
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: 124.91 E-value: 5.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSMnpRM 113
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPvlfSGTI--RS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVrsivgEPLqvNRLAEGAeltqkVADVLDSVGLKREHMNRFPHE----------FSGGQKQRLALARALSLDPEFILLD 183
Cdd:cd03244 97 NL-----DPF--GEYSDEE-----LWQALERVGLKEFVESLPGGLdtvveeggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 184 EPTSALDVSVQAQVLNLleeIQEKL-GLTFVFITHALNVVNHiSDRVAVMYLGKIVEiantadlFDKP 250
Cdd:cd03244 165 EATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVE-------FDSP 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
37-249 |
6.51e-34 |
|
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: 125.29 E-value: 6.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQ----------DPG 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQenvlfnrsirDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSVRSIVgeplQVNRLAEGAELTQKVADVLDS------VGLkrehmnrfphefSGGQKQRLALARALSLDPEFI 180
Cdd:cd03252 97 ALADPGMSMERVI----EAAKLAGAHDFISELPEGYDTivgeqgAGL------------SGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 181 LLDEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
39-250 |
2.22e-33 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 130.85 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDpgGSMNPRMSVRSI 118
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQN--GRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 VG-EPLQVNRLAEGAELtqkvadvldsVGLKrEHMNRFP---H--------EFSGGQKQRLALARALSLDPEFILLDEPT 186
Cdd:TIGR03797 548 AGgAPLTLDEAWEAARM----------AGLA-EDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 187 SALDVSVQAQVLNLLeeiqEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:TIGR03797 617 SALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
38-237 |
2.41e-33 |
|
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: 121.55 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDpggsmnprmsvrs 117
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 ivgeplqvNRLAEGAeltqkVADVLdsvglkrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQV 197
Cdd:cd03246 85 --------DELFSGS-----IAENI----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 663511184 198 LNLLEEIQEKlGLTFVFITHALNVVNhISDRVAVMYLGKI 237
Cdd:cd03246 136 NQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-238 |
2.49e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.07 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 27 MLSEVKIHVRA-----VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIV 101
Cdd:COG4559 1 MLEAENLSVRLggrtlLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 102 FQDpgGSMNPRMSVRSIVG---EPLQvnrlAEGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARAL---- 173
Cdd:COG4559 81 PQH--SSLAFPFTVEEVVAlgrAPHG----SSAAQDRQIVREALALVGL--AHLaGRSYQTLSGGEQQRVQLARVLaqlw 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 174 ---SLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:COG4559 153 epvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
41-257 |
2.64e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.58 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVL-LGLIPiTDGSVLYDGE--DIRTIPD----RELRRRMQIVFQDPggSMNPRM 113
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLnLLETP-DSGQLNIAGHqfDFSQKPSekaiRLLRQKVGMVFQQY--NLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVR-SIVGEPLQVNRLAEgAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:COG4161 98 TVMeNLIEAPCKVLGLSK-EQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 193 VQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEiANTADLFdkpAHPYTHA 257
Cdd:COG4161 176 ITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHF---TQPQTEA 235
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
40-238 |
3.52e-33 |
|
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: 122.82 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDREL---RRRMQIVFQdpGGSMNPRMSVR 116
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLvqlRRRIGYIFQ--AHNLLGFLTAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQ 196
Cdd:TIGR02982 101 QNVQMALELQPNLSYQEARERARAMLEAVGLG-DHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663511184 197 VLNLLEEIQEKLGLTFVFITHAlNVVNHISDRVAVMYLGKIV 238
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
39-249 |
3.84e-33 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 123.11 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDpggsmnprmSV--R 116
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD---------TVlfN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRLA---EGAELTQKVADVLDSVglkrehmNRFPHEF-----------SGGQKQRLALARALSLDPEFILL 182
Cdd:cd03253 89 DTIGYNIRYGRPDatdEEVIEAAKAAQIHDKI-------MRFPDGYdtivgerglklSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
42-246 |
5.74e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.38 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 42 DLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRelRRRMQIVFQDpgGSMNPRMSVRSIVGE 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQE--NNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 122 PLQVNrLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLL 201
Cdd:PRK10771 95 GLNPG-LKLNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 663511184 202 EEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADL 246
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
37-250 |
8.00e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.26 E-value: 8.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipDR----ELRRRMQIVFQDPGGSMNPR 112
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY--DKksllEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSIVGEPLQVNRLAEgaELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKE--EVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 193 VQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
12-245 |
2.11e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.89 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKggmlseVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSV--LYDGEDIRTI 89
Cdd:PRK13651 3 IKVKNIVKIFNKK------LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 90 PDR----------------------ELRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNrlAEGAELTQKVADVLDSVGL 147
Cdd:PRK13651 77 TKEkekvleklviqktrfkkikkikEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMG--VSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 148 KREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISD 227
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTK 233
|
250
....*....|....*...
gi 663511184 228 RVAVMYLGKIVEIANTAD 245
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYD 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-249 |
2.28e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.58 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD----RELRRRMQIVFQDPGGSMNPR 112
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSIVGEPLQVNRLAEgaELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLD--EVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 193 VQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
35-251 |
3.18e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.41 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrRRMQIVFQdpggsmN---- 110
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQ------Nyaly 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 PRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK11650 89 PHMSVRENMAYGLKIRGMPK-AEIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 191 VSVQAQVLNLLEEIQEKLGLTFVFITH----ALNvvnhISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:PRK11650 167 AKLRVQMRLEIQRLHRRLKTTSLYVTHdqveAMT----LADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
42-238 |
3.77e-32 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 119.91 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 42 DLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrRRMQIVFQDpgGSMNPRMSVRSIVGE 121
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQE--NNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 122 PLqVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLL 201
Cdd:cd03298 94 GL-SPGLKLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 663511184 202 EEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-245 |
4.28e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.51 E-value: 4.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRA---VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLG-LIPI--TDGSVLYDGEDIRTIPDRelRRRMQIV 101
Cdd:COG4136 4 LENLTITLGGrplLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAE--QRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 102 FQDPggSMNPRMSVrsivGE------PLQVNRlaegAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALS 174
Cdd:COG4136 82 FQDD--LLFPHLSV----GEnlafalPPTIGR----AQRRARVEQALEEAGL--AGFaDRDPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 175 LDPEFILLDEPTSALDVSVQAQVLNL-LEEIQEkLGLTFVFITHALNvvnhisDRVAVmylGKIVEIANTAD 245
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFvFEQIRQ-RGIPALLVTHDEE------DAPAA---GRVLDLGNWQH 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
36-252 |
5.06e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 126.23 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGgSMNprmsv 115
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAG-LFN----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIvGEPLQVNR-------LAEGAELTQ------KVADVLDSVGLKREHMnrfpheFSGGQKQRLALARALSLDPEFILL 182
Cdd:PRK13657 423 RSI-EDNIRVGRpdatdeeMRAAAERAQahdfieRKPDGYDTVVGERGRQ------LSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKPAH 252
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGR 562
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
36-247 |
5.27e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 121.65 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDG----EDIRTIPD-RELRRRMQIVFQDPGGSMN 110
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEvKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 PRMSVRSIVGEPlqVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK13645 105 QETIEKDIAFGP--VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 191 VSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
36-255 |
5.52e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 120.65 E-value: 5.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVL--LG-LIP--ITDGSVLYDGEDI--RTIPDRELRRRMQIVFQDPggs 108
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 109 mNP-RMSVRSIVGEPLQVN------RLAEGAELTQKVADVLDSVglkREHMNRFPHEFSGGQKQRLALARALSLDPEFIL 181
Cdd:PRK14239 96 -NPfPMSIYENVVYGLRLKgikdkqVLDEAVEKSLKGASIWDEV---KDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 182 LDEPTSALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
36-238 |
7.99e-32 |
|
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: 118.83 E-value: 7.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGeTLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDrELRRRMQIVFQDPGGSmnPRMSV 115
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYLPQEFGVY--PNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSivgeplQVNRLA-----EGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:cd03264 90 RE------FLDYIAwlkgiPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 191 VSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03264 163 PEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-256 |
8.35e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 122.53 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP------ITDGSVLYDGEDIRTIPDRelRRRMQIVFQDpgGSMNPRMS 114
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRpdegeiVLNGRTLFDSRKGIFLPPE--KRRIGYVFQE--ARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRsivGEPLQVNRLAEGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:TIGR02142 92 VR---GNLRYGMKRARPSERRISFERVIELLGI--GHLlGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTH 256
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-268 |
1.20e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.22 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMnPRMSVRS 117
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQF-VGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVGEPLQvNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQV 197
Cdd:PRK13650 102 DVAFGLE-NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 198 LNLLEEIQEKLGLTFVFITHALNVVNhISDRVAVMYLGKIVEIANTADLFDKPAH--------PYTHALMSAIPEPSLE 268
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDllqlgldiPFTTSLVQSLRQNGYD 257
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
30-239 |
1.80e-31 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 118.63 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 30 EVK-IHVrAVD------GVDLQIKRGETLGIVGESGCGKTTLGRVLLGlIP---ITDGSVLYDGEDIRTIPDRElRRRMQ 99
Cdd:COG0396 2 EIKnLHV-SVEgkeilkGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyeVTSGSILLDGEDILELSPDE-RARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 100 I--VFQDP----GGSMNP--RMSVRSIVGEPLQVnrlaegAELTQKVADVLDSVGLKREHMNRFPHE-FSGGQKQRLALA 170
Cdd:COG0396 79 IflAFQYPveipGVSVSNflRTALNARRGEELSA------REFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511184 171 RALSLDPEFILLDEPTSALDV-SVQAqVLNLLEEIQEKlGLTFVFITHALNVVNHIS-DRVAVMYLGKIVE 239
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIKpDFVHVLVDGRIVK 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-249 |
3.56e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMnprmsVR 116
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQF-----VG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQV---NRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:PRK13648 99 SIVKYDVAFgleNHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
38-250 |
3.93e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 118.26 E-value: 3.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggSMNPRMSVRS 117
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN--HINSRLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVG---EPLQVNRLaeGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:COG4604 95 LVAfgrFPYSKGRL--TAEDREIIDEAIAYLDL--EDLaDRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:COG4604 171 SVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
34-251 |
7.18e-31 |
|
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: 117.01 E-value: 7.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRR-----MQI--VFqdpg 106
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgigyvPEGrrIF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 gsmnPRMSVRsivgEPLQVnrlaeGAEL---TQKVADVLDSVglkrehMNRFP--HEF--------SGGQKQRLALARAL 173
Cdd:COG0410 91 ----PSLTVE----ENLLL-----GAYArrdRAEVRADLERV------YELFPrlKERrrqragtlSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 174 SLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
37-250 |
9.36e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 9.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLI---PITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMnprm 113
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 sVRSIVGEPLQV---NRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK13640 98 -VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 191 VSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-326 |
1.09e-30 |
|
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: 111.69 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 236 KIVEIANTADLFDKPAHPYTHALMSAIPEPSleKASRERIVLSGDVPSPANPPPGCRFHTRCPIAVEgVCDVVDPPLETI 315
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIK--KRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQD-ECRKEPPALVEI 77
|
90
....*....|.
gi 663511184 316 DfDDHAVACHF 326
Cdd:TIGR01727 78 A-EGHRVACHL 87
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
34-239 |
1.68e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 115.39 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipDRELRRRMQIVFQDPGgsMNPRM 113
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPG--FYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRsivgEPLQVNRLAEGAElTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03268 88 TAR----ENLRLLARLLGIR-KKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 663511184 194 QAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVE 239
Cdd:cd03268 162 IKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-258 |
1.96e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.14 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYdGEDIRTIPDRE-----LRRRMQIVFQDPGGSMN 110
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeikpVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 PRMSVRSIVGEPLQVNRLAEGAEltQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAE--KIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 191 VSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHAL 258
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
35-247 |
2.20e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.73 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMnprms 114
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEG---AELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK13642 95 VGATVEDDVAFGMENQGiprEEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 192 SVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
36-219 |
4.03e-30 |
|
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: 120.54 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsmnprMSV 115
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDA-------HLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLqvnRLAEGAELTQKVADVLDSVGLKrEHMNRFPH-----------EFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:TIGR02868 422 DTTVRENL---RLARPDATDEELWAALERVGLA-DWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....*
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEklGLTFVFITHAL 219
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
37-246 |
4.12e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 114.93 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElRRRMQIVFQDPGGSMNPRMSVR 116
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sivgEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQ 196
Cdd:TIGR03410 94 ----ENLLTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 663511184 197 VLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADL 246
Cdd:TIGR03410 170 IGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-232 |
4.24e-30 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 114.84 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPI--KGGmlseVKIHVraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE---- 84
Cdd:COG4778 4 LLEVENLSKTFTLhlQGG----KRLPV--LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIPDRE---LRRR--------MQIVfqdpggsmnPRMSVRSIVGEPLqvnrLAEG---AELTQKVADVLDSVGLKRE 150
Cdd:COG4778 78 DLAQASPREilaLRRRtigyvsqfLRVI---------PRVSALDVVAEPL----LERGvdrEEARARARELLARLNLPER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 151 HMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVA 230
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVV 223
|
..
gi 663511184 231 VM 232
Cdd:COG4778 224 DV 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
35-250 |
4.84e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.06 E-value: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMNPRMS 114
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPlqVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:PRK13652 97 EQDIAFGP--INLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-251 |
7.16e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYdGEDIRTIPDRE-----LRRRMQIVFQDPGGSMN 110
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkpLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 PRMSVRSIVGEPLQVNRLAEGAEltQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK13634 100 EETVEKDICFGPMNFGVSEEDAK--QKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511184 191 VSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-245 |
1.26e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.02 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKGGMLSEVKI-----------HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVl 80
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLKElllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 81 ydgedirtipdrelRRRMQIVFQ-DPGGSMNPRMSVR-------SIVGEPLqvnrlaegAELTQKVADVLDSVGLKrEHM 152
Cdd:COG1134 84 --------------EVNGRVSALlELGAGFHPELTGReniylngRLLGLSR--------KEIDEKFDEIVEFAELG-DFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 153 NRfP-HEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAV 231
Cdd:COG1134 141 DQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|....
gi 663511184 232 MYLGKIVEIANTAD 245
Cdd:COG1134 219 LEKGRLVMDGDPEE 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
42-243 |
1.62e-29 |
|
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: 112.65 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 42 DLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPdrELRRRMQIVFQDpgGSMNPRMSVRSIVGE 121
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA--PYQRPVSMLFQE--NNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 122 PLQVNrLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLL 201
Cdd:TIGR01277 94 GLHPG-LKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663511184 202 EEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANT 243
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
11-229 |
1.98e-29 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 112.87 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPI--KGGMLSEVkihvraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE---- 84
Cdd:TIGR02324 1 LLEVEDLSKTFTLhqQGGVRLPV------LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEgawv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIPDRELR--RRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKREHMNRFPHEFSGG 162
Cdd:TIGR02324 75 DLAQASPREVLevRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPR-EAARARARELLARLNIPERLWHLPPATFSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRV 229
Cdd:TIGR02324 154 EQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
37-232 |
2.17e-29 |
|
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: 118.16 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPG---GSM--NP 111
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFlfaGTIaeNI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRsiVGEPLQVNRLAEGAELTQKVADVLDsvGLKREhMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:TIGR02857 417 RLARP--DASDAEIREALERAGLDEFVAALPQ--GLDTP-IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 663511184 192 SVQAQVLNLLEEIQEklGLTFVFITHALNVVnHISDRVAVM 232
Cdd:TIGR02857 492 ETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
36-237 |
2.64e-29 |
|
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: 111.37 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElRRRMQIVFqdpggsmnprmsv 115
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD-AIRAGIAY------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 rsiVGEplqvNRLAEGAELTQKVADVLdsvglkrehmnRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:cd03215 80 ---VPE----DRKREGLVLDLSVAENI-----------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663511184 196 QVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
35-250 |
8.39e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.32 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMNprMS 114
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFE--FD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIV--GEPLQVNRLAEGAEL-TQKVADVLDSVGLKReHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK09536 94 VRQVVemGRTPHRSRFDTWTETdRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 192 SVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PRK09536 173 NHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
37-249 |
8.83e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE--DIRTIPDRELRRRMQIVFQDPGGSMNPRMS 114
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVnRLAEgAELTQKVADVLDSVGLkrEHMNRFP-HEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:PRK13636 101 YQDVSFGAVNL-KLPE-DEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
35-252 |
3.04e-28 |
|
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: 115.20 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSM-- 109
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVvlfNDTIan 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 NPRMSVRSIVGEPlQVNRLAEGAELtQKVADVLD-----SVGLKREHMnrfphefSGGQKQRLALARALSLDPEFILLDE 184
Cdd:TIGR02203 425 NIAYGRTEQADRA-EIERALAAAYA-QDFVDKLPlgldtPIGENGVLL-------SGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKPAH 252
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGL 560
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
38-217 |
3.06e-28 |
|
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: 110.17 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVL------YDGEDIRtipdrELRRRMQIVFQDPGGSMNP 111
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVW-----ELRKRIGLVSPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIV--------GEPLQVnrlaeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLD 183
Cdd:COG1119 94 DETVLDVVlsgffdsiGLYREP-----TDEQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190
....*....|....*....|....*....|....
gi 663511184 184 EPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITH 217
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-245 |
3.17e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 8 GKVLIEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIR 87
Cdd:COG3845 2 MPPALELRGITKRFG-----------GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 88 tIPD-RELRRR---MqiVFQDPggSMNPRMSVRS--IVG-EPLQVNRLAEgAELTQKVADVLDSVGLKREhMNRFPHEFS 160
Cdd:COG3845 71 -IRSpRDAIALgigM--VHQHF--MLVPNLTVAEniVLGlEPTKGGRLDR-KAARARIRELSERYGLDVD-PDAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALdvsVQAQVLNLLEEIQE--KLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
....*..
gi 663511184 239 EIANTAD 245
Cdd:COG3845 221 GTVDTAE 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-240 |
5.08e-28 |
|
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: 109.16 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIKGGMLSEVK-----------IHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVl 80
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 81 ydgedirtipdrelRRRMQIV-FQDPGGSMNPRMSVRS---IVGEPLQVNRlaegAELTQKVADVLDSVGLKrEHMNRFP 156
Cdd:cd03220 80 --------------TVRGRVSsLLGLGGGFNPELTGREniyLNGRLLGLSR----KEIDEKIDEIIEFSELG-DFIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 157 HEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGK 236
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
....
gi 663511184 237 IVEI 240
Cdd:cd03220 220 IRFD 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-232 |
5.33e-28 |
|
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: 114.46 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSmnprms 114
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVelfDGT------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 vrsiVGEplqvN--RLAEG--AELTQ--KVADVLDSVGlkrehmnRFPHEF-----------SGGQKQRLALARALSLDP 177
Cdd:COG4618 422 ----IAE----NiaRFGDAdpEKVVAaaKLAGVHEMIL-------RLPDGYdtrigeggarlSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 178 EFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHiSDRVAVM 232
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVL 539
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-238 |
7.95e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.20 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrtipDRELRRRMqivfqdpgGSM----- 109
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRI--------GYLpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 -NPRMSvrsiVGEplQVNRLAE-----GAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLD 183
Cdd:COG4152 82 lYPKMK----VGE--QLVYLARlkglsKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 184 EPTSALD-VSVQAqVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:COG4152 155 EPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
39-250 |
1.34e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.08 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDREL---RRRMQIVFQDpgGSMNPRMSV 115
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQVNRLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK11831 102 FDNVAYPLREHTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
38-237 |
1.52e-27 |
|
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: 113.21 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQD----PG------G 107
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDvelfPGtvaeniA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 SMNPRMSVRSIVgeplQVNRLAEGAELTQKVADVLDSV------GLkrehmnrfphefSGGQKQRLALARALSLDPEFIL 181
Cdd:TIGR01842 414 RFGENADPEKII----EAAKLAGVHELILRLPDGYDTVigpggaTL------------SGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 182 LDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHIsDRVAVMYLGKI 237
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
39-237 |
1.84e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.61 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDgedirTIPDRELRRRMQIVFQDpgGSMNPRMSVRSI 118
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQD--ARLLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 VGEPLQVNRLAEGAEltqkvadVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVL 198
Cdd:PRK11247 102 VGLGLKGQWRDAALQ-------ALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 663511184 199 NLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
37-248 |
1.93e-27 |
|
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: 113.30 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsmnpRMSVR 116
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP------YIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRlaEGAElTQKVADVLDSVGLKREhMNRFPHEF-----------SGGQKQRLALARALSLDPEFILLDEP 185
Cdd:TIGR01193 563 SILENLLLGAK--ENVS-QDEIWAACEIAEIKDD-IENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKlglTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFD 248
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
36-238 |
1.97e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 107.65 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRE---LRRRMQIVFQDPGGSMNpr 112
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSIVGEPLQVNRlAEGAELTQKVADVLDSVGLKREHMNrFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK10908 94 RTVYDNVAIPLIIAG-ASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 663511184 193 VQAQVLNLLEEIQeKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
37-251 |
2.83e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.54 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD-RELRRRMQIVFQDPGGSMNPRMSV 115
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPlqVNRLAEGAELTQKVADVLDSVGLKReHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK13644 97 EDLAFGP--ENLCLPPIEIRKRVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 196 QVLNLLEEIQEKlGLTFVFITHALNVVnHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:PRK13644 174 AVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
37-260 |
2.94e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.95 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRV---LLGLIPI--TDGSVLYDGEDI--RTIPDRELRRRMQIVFQDPggsm 109
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 NP-RMSVRSIVGEPLQVN----RLAEGAELTQKVADVLDSVglkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:PRK14243 101 NPfPKSIYDNIAYGARINgykgDMDELVERSLRQAALWDEV---KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVM---------YLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255
|
....*
gi 663511184 256 HALMS 260
Cdd:PRK14243 256 RDYVS 260
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-238 |
3.51e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIkgGMLSEVkihvRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPd 91
Cdd:COG1101 2 LELKNLSKTFNP--GTVNEK----RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 92 rELRRRMQI--VFQDPggSMN--PRMSV------------------------RSIVGEplQVNRLAEGAE--LTQKVadv 141
Cdd:COG1101 75 -EYKRAKYIgrVFQDP--MMGtaPSMTIeenlalayrrgkrrglrrgltkkrRELFRE--LLATLGLGLEnrLDTKV--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 142 ldsvGLkrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITH---- 217
Cdd:COG1101 147 ----GL-----------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeq 211
|
250 260
....*....|....*....|.
gi 663511184 218 ALNVVNhisdRVAVMYLGKIV 238
Cdd:COG1101 212 ALDYGN----RLIMMHEGRII 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
30-229 |
4.00e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.82 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 30 EVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDR---ELR-RRMQIVFQdp 105
Cdd:PRK11629 17 EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQ-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 106 GGSMNPRMSVRSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKREHMNRfPHEFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK11629 95 FHHLLPDFTALENVAMPLLIGKKKP-AEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRV 229
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
37-239 |
5.08e-27 |
|
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: 105.09 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrtipdrelrrrmqivfQDPGGSMNPRMSVr 116
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV----------------SDLEKALSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sivgeplqvnrlaegaeLTQKV----ADVLDSVGLKrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:cd03247 80 -----------------LNQRPylfdTTLRNNLGRR----------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 193 VQAQVLNLL-EEIQEKlglTFVFITHALNVVNHIsDRVAVMYLGKIVE 239
Cdd:cd03247 133 TERQLLSLIfEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
38-239 |
6.91e-27 |
|
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: 105.30 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGlIP---ITDGSVLYDGEDIRTIPDRElRRRMQI--VFQDPggsmnPR 112
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDLPPEE-RARLGIflAFQYP-----PE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MsvrsivgeplqvnrlaEGAeltqKVADVLDSVGLKrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:cd03217 89 I----------------PGV----KNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 193 VQAQVLNLLEEIQEKlGLTFVFITHALNVVNHI-SDRVAVMYLGKIVE 239
Cdd:cd03217 139 ALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-250 |
8.14e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.04 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPI-----TDGSVLYDGEDI--RTIPDRELRRRMQIVFQDPggS 108
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKP--N 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 109 MNPrMSVR-------SIVG--EPLQVNRLAEGAeltQKVADVLDSVglkREHMNRFPHEFSGGQKQRLALARALSLDPEF 179
Cdd:PRK14258 99 LFP-MSVYdnvaygvKIVGwrPKLEIDDIVESA---LKDADLWDEI---KHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 180 ILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMY-----LGKIVEIANTADLFDKP 250
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSP 247
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
33-239 |
8.36e-27 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 106.19 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 33 IHVRAVD-----GVDLQIKRGETLGIVGESGCGKTTLGRVLLG--LIPITDGSVLYDGEDIRTI-PDRELRRRMQIVFQD 104
Cdd:TIGR01978 6 LHVSVEDkeilkGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELePDERARAGLFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 105 PggSMNPRMSVRSIVGEPLQVNRLAEG------AELTQKVADVLDSVGLKREHMNRFPHE-FSGGQKQRLALARALSLDP 177
Cdd:TIGR01978 86 P--EEIPGVSNLEFLRSALNARRSARGeepldlLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 178 EFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHIS-DRVAVMYLGKIVE 239
Cdd:TIGR01978 164 KLAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITHYQRLLNYIKpDYVHVLLDGRIVK 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-239 |
1.12e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 111.07 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQD-------------- 104
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDtvlfndtiayniay 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 105 --PGGSMNprmsvrsivgeplQVNRLAEGAELTQKVA---DVLDSV----GLKrehmnrfpheFSGGQKQRLALARALSL 175
Cdd:COG5265 455 grPDASEE-------------EVEAAARAAQIHDFIEslpDGYDTRvgerGLK----------LSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 176 DPEFILLDEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVE 239
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
35-238 |
1.64e-26 |
|
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: 104.67 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrtipDRELRRRMQIVFQDPGgsMNPRMS 114
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPEERG--LYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSivgeplQVNRLAEGAELTQKVA-----DVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:cd03269 87 VID------QLVYLAQLKGLKKEEArrridEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 663511184 190 DVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03269 160 DPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-255 |
3.29e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.56 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDG-----SVLYDGEDIRTIPD-RELRRRMQIVFQDPggsmNP 111
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvLEFRRRVGMLFQRP----NP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 -RMSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGL---KREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTS 187
Cdd:PRK14271 113 fPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 188 ALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYT 255
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
36-249 |
4.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD----RELRRRMQIVFQDPGGSMNP 111
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIVGEPLQVNRLAEGAELTQKvaDVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 192 SVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK13649 179 KGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-251 |
4.42e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.09 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSV----LYDGEDI-----------RTIPD-RELRRRM 98
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKnnhelitnpysKKIKNfKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 99 QIVFQDPGGSMNPRMSVRSIVGEPlqVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPE 178
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDIMFGP--VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 179 FILLDEPTSALDVSVQAQVLNLLEEiQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
36-251 |
4.50e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 104.16 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElRRRMQIVF--QDPggSMNPRM 113
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEA--SIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVR---SIVGEPLQVNRlaegAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:cd03218 91 TVEeniLAVLEIRGLSK----KEREEKLEELLEEFHI--THLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 190 D-VSVQaQVLNLLEEIQEK-LGltfVFIT-HALNVVNHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:cd03218 165 DpIAVQ-DIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-236 |
5.03e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.48 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP--ITDGSVLYDGEDIR- 87
Cdd:PRK13549 5 LLEMKNITKTFG-----------GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 88 -TIPDRElRRRMQIVFQDPggSMNPRMSVRS--IVGEPLQVNRLAEGAELTQKVADVLDSVGLkreHMNrfPH----EFS 160
Cdd:PRK13549 74 sNIRDTE-RAGIAIIHQEL--ALVKELSVLEniFLGNEITPGGIMDYDAMYLRAQKLLAQLKL---DIN--PAtpvgNLG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGK 236
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
36-241 |
5.69e-26 |
|
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: 103.26 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMNprmSV 115
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG---TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSivgeplQVNRLAEGAEltqkvADVLDSVGLKREHMNrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:cd03369 99 RS------NLDPFDEYSD-----EEIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 663511184 196 QVLNLLEEiqEKLGLTFVFITHALNVVNHIsDRVAVMYLGKIVEIA 241
Cdd:cd03369 163 LIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-217 |
2.07e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY-DGEDIRTIPDRelrrrmqivfqdpggsmnPRM--- 113
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQR------------------PYLplg 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEgaeltQKVADVLDSVGLKR--EHMN---RFPHEFSGGQKQRLALARALSLDPEFILLDEPTSA 188
Cdd:COG4178 441 TLREALLYPATAEAFSD-----AELREALEAVGLGHlaERLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*....
gi 663511184 189 LDVSVQAQVLNLLEEiqEKLGLTFVFITH 217
Cdd:COG4178 516 LDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-251 |
3.22e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrRRMQIVFQDPggSMNPRMSVRSIVG 120
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSY--ALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 121 EPLQVNRlAEGAELTQKVADVLDSvgLKREHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLN 199
Cdd:PRK11000 98 FGLKLAG-AKKEEINQRVNQVAEV--LQLAHLlDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 663511184 200 LLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPA 251
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
38-227 |
7.50e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.56 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPG--GSmnprmSV 115
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTlfGD-----TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQVNRLAEGAeltQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDP---AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|..
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITHALNVVNHISD 227
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDEINHADK 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
36-217 |
8.24e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrTIPDRElrrrMQIVFQDPGgsMNPRMSV 115
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAE----RGVVFQNEG--LLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQVNRLAEgAELTQKVADVLDSVGLKREHmNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK11248 88 QDNVAFGLQLAGVEK-MQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|..
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITH 217
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITH 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-236 |
1.17e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.83 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFpikGGMLsevkihvrAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP 90
Cdd:PRK11300 5 LLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 DRELrRRMQIV--FQdpggsmNPR----MSVRS--IVGEPLQVN-------------RLAEgAELTQKVADVLDSVGLkR 149
Cdd:PRK11300 74 GHQI-ARMGVVrtFQ------HVRlfreMTVIEnlLVAQHQQLKtglfsgllktpafRRAE-SEALDRAATWLERVGL-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 150 EHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRV 229
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
....*..
gi 663511184 230 AVMYLGK 236
Cdd:PRK11300 225 YVVNQGT 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
37-258 |
1.38e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.52 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLgrvlLGLIP----ITDGSVLYDGEDIRTIPDRELRRRMQIVFQdpggsmnpR 112
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdPQQGEILLNGQPIADYSEAALRQAISVVSQ--------R 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSivgEPLQVN-RLAEGAELTQKVADVLDSVGLKR-----EHMNRFPHE----FSGGQKQRLALARALSLDPEFILL 182
Cdd:PRK11160 423 VHLFS---ATLRDNlLLAAPNASDEALIEVLQQVGLEKlleddKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 183 DEPTSALDVSVQAQVLNLLEE-IQEKlglTFVFITHALNVVNHIsDRVAVMYLGKIVEIANTADLFDKpaHPYTHAL 258
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEhAQNK---TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ--QGRYYQL 570
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
36-238 |
1.42e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.97 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPGGSMNPRMSV 115
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPlqVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK13647 99 DDVAFGP--VNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 663511184 196 QVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
36-238 |
1.51e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsMNPR-MS 114
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH---LTPEgIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIV--GEPLQVN---RLAEGAEltQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSA 188
Cdd:PRK11231 93 VRELVayGRSPWLSlwgRLSAEDN--ARVNQAMEQTRI--NHLaDRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 663511184 189 LDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-273 |
2.36e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD----RELRRRMQIVFQDPGGSMNP 111
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRSIVGEPLqvNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK13641 101 NTVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 192 SVQAQVLNLLEEIQeKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHALmsaiPEPSLEKAS 271
Cdd:PRK13641 179 EGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYL----DEPATSRFA 253
|
..
gi 663511184 272 RE 273
Cdd:PRK13641 254 SK 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-246 |
2.90e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 3 EESRDGKVLIEVKGMkkWFPIKGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYD 82
Cdd:COG3845 249 APAEPGEVVLEVENL--SVRDDRG--------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 83 GEDIrTIPDRELRRRMQIVF--QDPGGS-MNPRMSV------RSIVGEPLQVN---RLAEGAELTQKVADVLDsVglkre 150
Cdd:COG3845 319 GEDI-TGLSPRERRRLGVAYipEDRLGRgLVPDMSVaenlilGRYRRPPFSRGgflDRKAIRAFAEELIEEFD-V----- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 151 hmnRFPHE------FSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNH 224
Cdd:COG3845 392 ---RTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILA 467
|
250 260
....*....|....*....|..
gi 663511184 225 ISDRVAVMYLGKIVEIANTADL 246
Cdd:COG3845 468 LSDRIAVMYEGRIVGEVPAAEA 489
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-250 |
2.93e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSMNPRMSV- 115
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPvlfSGSVRENIAYg 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 --RSIVGEPLQVNRLAEGAELTQKVADVLDS-VGLKREHMnrfphefSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:TIGR00958 579 ltDTPDEEIMAAAKAANAHDFIMEFPNGYDTeVGEKGSQL-------SGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 193 VQAqvlnLLEEIQEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:TIGR00958 652 CEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
41-239 |
3.43e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.39 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITdGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsMNPRMSVRSIV- 119
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNP---QLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 120 -GEPL----QVNRLAEGA---ELTQKVADVLDS-VGlkrEHMNRFphefSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK11174 445 lGNPDasdeQLQQALENAwvsEFLPLLPQGLDTpIG---DQAAGL----SVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 663511184 191 VSVQAQVLNLLEeiQEKLGLTFVFITHALNVVNHIsDRVAVMYLGKIVE 239
Cdd:PRK11174 518 AHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
39-225 |
4.55e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlydgedirtipdrELRRRMQIVF--QDPGgsMNPRMSVR 116
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-------------SIPKGLRIGYlpQEPP--LDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIV----GEPLQV------------------NRLAE---------GAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQ 165
Cdd:COG0488 80 DTVldgdAELRALeaeleeleaklaepdedlERLAElqeefealgGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDV-SVQaqvlnLLEEIQEKLGLTFVFITH--AL--NVVNHI 225
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHdrYFldRVATRI 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-247 |
2.41e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.77 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE--DIRTIPDRELRRRMQIVFQDPGGSMNpRMSVRS 117
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPEQQIF-YTDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVGEPLQVNRLAEgAELTQKVADVLDSVglKREHMNRFPHE-FSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQ 196
Cdd:PRK13638 98 DIAFSLRNLGVPE-AEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663511184 197 VLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLF 247
Cdd:PRK13638 175 MIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
36-242 |
3.55e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.25 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIP-DRelRRRMQI--------VFQdpg 106
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHK--RARLGIgylpqeasIFR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 gsmnpRMSVR---SIVGEPLQVNRlaegAELTQKVADVLDSVGLkrEHMNRFP-HEFSGGQKQRLALARALSLDPEFILL 182
Cdd:COG1137 92 -----KLTVEdniLAVLELRKLSK----KEREERLEELLEEFGI--THLRKSKaYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 183 DEPTSALD-VSVqaqvlnllEEIQE--------KLGltfVFIT-H----ALNVVnhisDRVAVMYLGKIV------EIAN 242
Cdd:COG1137 161 DEPFAGVDpIAV--------ADIQKiirhlkerGIG---VLITdHnvreTLGIC----DRAYIISEGKVLaegtpeEILN 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-246 |
5.87e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 3 EESRDGKVLIEVKGmkkwfpikggmLSevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYD 82
Cdd:COG1129 248 RAAAPGEVVLEVEG-----------LS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 83 GE--DIRTIPDReLR---------RRMQIVFQDpggsmnprMSVR---SIVgeplQVNRLAEG-----AELTQKVADVLD 143
Cdd:COG1129 313 GKpvRIRSPRDA-IRagiayvpedRKGEGLVLD--------LSIReniTLA----SLDRLSRGglldrRRERALAEEYIK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 144 SVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVN 223
Cdd:COG1129 380 RLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELL 458
|
250 260
....*....|....*....|...
gi 663511184 224 HISDRVAVMYLGKIVEIANTADL 246
Cdd:COG1129 459 GLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-238 |
7.34e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 95.48 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPI---KGGMLSEVKIHVR-------AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY 81
Cdd:cd03267 1 IEVSNLSKSYRVyskEPGLIGSLKSLFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 82 DGEdirtIP---DRELRRRMQIVFqdpgGSMN-------PRMS---VRSIVG-EPLQV-NRLAEGAELTQkVADVLDSvg 146
Cdd:cd03267 81 AGL----VPwkrRKKFLRRIGVVF----GQKTqlwwdlpVIDSfylLAAIYDlPPARFkKRLDELSELLD-LEELLDT-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 147 lkrehmnrfP-HEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHI 225
Cdd:cd03267 150 ---------PvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAL 220
|
250
....*....|...
gi 663511184 226 SDRVAVMYLGKIV 238
Cdd:cd03267 221 ARRVLVIDKGRLL 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-238 |
1.17e-22 |
|
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: 98.74 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP--ITDGSVLYDGEDI-- 86
Cdd:TIGR02633 1 LLEMKGIVKTF---GG--------VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLka 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDRElRRRMQIVFQDPggSMNPRMSVRS--IVGEPLQVN-RLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQ 163
Cdd:TIGR02633 70 SNIRDTE-RAGIVIIHQEL--TLVPELSVAEniFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 164 KQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-238 |
2.88e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLI-P----IT-DGSVLYDGE-DIRTIPDRelrRRMQIVFQDpgGSMNPRM 113
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTrPqkgrIVlNGRVLFDAEkGICLPPEK---RRIGYVFQD--ARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSivgeplqvN-RLAEGAELTQKVADVLDSVGLkrEH-MNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK11144 92 KVRG--------NlRYGMAKSMVAQFDKIVALLGI--EPlLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 663511184 192 SVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
34-237 |
3.18e-22 |
|
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: 93.30 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSMN 110
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPvlfARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 PRMSVRSIVGEPLQVNRLAEGA---ELTQKVADVLDS-VGLKREHMnrfphefSGGQKQRLALARALSLDPEFILLDEPT 186
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKAhahSFISELASGYDTeVGEKGSQL-------SGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663511184 187 SALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHiSDRVAVMYLGKI 237
Cdd:cd03248 179 SALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
41-249 |
3.34e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.28 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQD---PGGsmnprMSVRS 117
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNattPGD-----ITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVG------EPLQVNRLAEGAELTQKVADVLDSVGLKREHMNrfphEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK10253 101 LVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 192 SVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV------EIAnTADLFDK 249
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVaqgapkEIV-TAELIER 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-232 |
4.72e-22 |
|
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: 92.53 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGedirtipdrelrrRMQIVFQDPGgSMNprMSVRS-I 118
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPW-IQN--GTIREnI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 V-GEPLQVNRLAEgaeltqkvadVLDSVGLKREhMNRFPH-------E----FSGGQKQRLALARALSLDPEFILLDEPT 186
Cdd:cd03250 87 LfGKPFDEERYEK----------VIKACALEPD-LEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 187 SALDVSVQAQVLNLLeeIQEKL--GLTFVFITHALNVVNHiSDRVAVM 232
Cdd:cd03250 156 SAVDAHVGRHIFENC--ILGLLlnNKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-235 |
5.10e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 3 EESRDGKVLIEVKGMKKWFPikggmlsEVKIhvraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlyd 82
Cdd:COG0488 307 PPERLGKKVLELEGLSKSYG-------DKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 83 gedirtipdrELRRRMQIVF--QDpGGSMNPRMSVRSIVGeplqvnRLAEGAElTQKVADVLDSVGLKREHMNRFPHEFS 160
Cdd:COG0488 373 ----------KLGETVKIGYfdQH-QEELDPDKTVLDELR------DGAPGGT-EQEVRGYLGRFLFSGDDAFKPVGVLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALDVsvqaQVLNLLEEiqeklGL-----TFVFITH---ALN-VVNHI---SDR 228
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEE-----ALddfpgTVLLVSHdryFLDrVATRIlefEDG 505
|
....*..
gi 663511184 229 VAVMYLG 235
Cdd:COG0488 506 GVREYPG 512
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-239 |
9.67e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 96.01 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPikgGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPIT--DGSVLYDGE--DI 86
Cdd:NF040905 1 ILEMRGITKTFP---G--------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEvcRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDRElRRRMQIVFQDPggSMNPRMSV-RSI-VGEPLQVNRLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQK 164
Cdd:NF040905 70 KDIRDSE-ALGIVIIHQEL--ALIPYLSIaENIfLGNERAKRGVIDWNETNRRARELLAKVGL-DESPDTLVTDIGVGKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 165 QRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVE 239
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
42-217 |
1.14e-21 |
|
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: 90.29 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 42 DLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSV-LYDGEDIRTIPDRelrrrmqivfqdpggSMNPRMSVRSIVG 120
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLPQR---------------PYLPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 121 EPLQvnrlaegaeltqkvaDVLdsvglkrehmnrfphefSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNL 200
Cdd:cd03223 86 YPWD---------------DVL-----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*..
gi 663511184 201 LEEiqekLGLTFVFITH 217
Cdd:cd03223 134 LKE----LGITVISVGH 146
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
36-223 |
1.47e-21 |
|
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: 90.88 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDrELRRRMQIVFQDPGgsMNPRMSV 115
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPG--LKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RsivgEPLQV-NRLAEGAELTqkVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:TIGR01189 91 L----ENLHFwAAIHGGAQRT--IEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|....*....
gi 663511184 195 AQVLNLLEEIQEKLGLTFVFITHALNVVN 223
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-249 |
1.64e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.61 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPIK----------GGMLSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY 81
Cdd:COG4586 2 IEVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 82 DGEDirtiP---DRELRRRMQIVF-QdpggsmnprmsvRS------IVGEPLQVNRL------AEGAELTQKVADVLDsV 145
Cdd:COG4586 82 LGYV----PfkrRKEFARRIGVVFgQ------------RSqlwwdlPAIDSFRLLKAiyripdAEYKKRLDELVELLD-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 146 GlkrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHI 225
Cdd:COG4586 145 G---ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260
....*....|....*....|....
gi 663511184 226 SDRVAVMYLGKIVEIANTADLFDK 249
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-238 |
2.50e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 11 LIEVKGMKKWFPIkggmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI-RTI 89
Cdd:PRK09700 5 YISMAGIGKSFGP-----------VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 90 PDRELRRRMQIVFQDPggSMNPRMSVRsivgEPLQVNRL----------AEGAELTQKVADVLDSVGLKREhMNRFPHEF 159
Cdd:PRK09700 74 HKLAAQLGIGIIYQEL--SVIDELTVL----ENLYIGRHltkkvcgvniIDWREMRVRAAMMLLRVGLKVD-LDEKVANL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 160 SGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQeKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
238-303 |
6.84e-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: 85.15 E-value: 6.84e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 238 VEIANTADLFDKPAHPYTHALMSAIPEPslEKASRERIVLSGDVPSPANPPPGCRFHTRCPIAVEG 303
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRL--DPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEE 64
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-217 |
7.39e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.84 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIpDRElrRRMQIVFQDPGGSMNPRMSVRSIV 119
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM-DEE--ARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 120 G-EPLQVNRLAEGA---ELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK10584 105 AlENVELPALLRGEssrQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|..
gi 663511184 196 QVLNLLEEIQEKLGLTFVFITH 217
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTH 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
40-203 |
1.49e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElrrrmQIVFQDPGGSMNPRMSVRsiv 119
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE-----ACHYLGHRNAMKPALTVA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 120 gEPLQVNRLAEGAELTQkVADVLDSVGLKR-EHMnRFpHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVL 198
Cdd:PRK13539 92 -ENLEFWAAFLGGEELD-IAAALEAVGLAPlAHL-PF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
....*
gi 663511184 199 NLLEE 203
Cdd:PRK13539 168 ELIRA 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-238 |
1.75e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.78 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 27 MLS--EVKIH---VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPD-RELRRRMQI 100
Cdd:PRK11614 5 MLSfdKVSAHygkIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 101 VfqdPGGSmnpRMSVRSIVGEPLQVNR-LAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEF 179
Cdd:PRK11614 85 V---PEGR---RVFSRMTVEENLAMGGfFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 180 ILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
37-249 |
5.29e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIV------FQDP----- 105
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVsqnvhlFNDTianni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 106 GGSMNPRMSVRSIVgeplQVNRLAEGAELTQKVADVLDSV----GLKrehmnrfpheFSGGQKQRLALARALSLDPEFIL 181
Cdd:PRK11176 438 AYARTEQYSREQIE----EAARMAYAMDFINKMDNGLDTVigenGVL----------LSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 182 LDEPTSALDVSVQAQVLNLLEEIQEKlgLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-237 |
6.84e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 90.65 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 2 TEESRDGKVLIEVKGMKKWFPIKGgmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP-ITDGSVL 80
Cdd:TIGR02633 248 HEPHEIGDVILEARNLTCWDVINP--------HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 81 YDGE--DIRTiPDRELRRRMQIVFQD-PGGSMNPRMSV-RSIVGEPLQ----VNRLAEGAELtqkvaDVLDSvGLKREHM 152
Cdd:TIGR02633 320 INGKpvDIRN-PAQAIRAGIAMVPEDrKRHGIVPILGVgKNITLSVLKsfcfKMRIDAAAEL-----QIIGS-AIQRLKV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 153 NRFpHEF------SGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHIS 226
Cdd:TIGR02633 393 KTA-SPFlpigrlSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLS 470
|
250
....*....|.
gi 663511184 227 DRVAVMYLGKI 237
Cdd:TIGR02633 471 DRVLVIGEGKL 481
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
37-237 |
7.42e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 86.68 E-value: 7.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrtipDRELRRRMQIVFQDPGGSMNprMSVR 116
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW----TRKDLHKIGSLIESPPLYEN--LTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sivgEPLQVNRLAEGAElTQKVADVLDSVGLKREHMNRfPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD-VSVQa 195
Cdd:TIGR03740 89 ----ENLKVHTTLLGLP-DSRIDEVLNIVDLTNTGKKK-AKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDpIGIQ- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663511184 196 QVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:TIGR03740 162 ELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
35-266 |
7.61e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDREL----RRRMQIVFQDPggSMN 110
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRY--HLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 111 PRMSVRSIVGEPlQVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALD 190
Cdd:PRK10535 99 SHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 191 VSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHiSDRVAVMYLGKIVeiantADLFDKPAHPYTHALMSAIPEPS 266
Cdd:PRK10535 177 SHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV-----RNPPAQEKVNVAGGTEPVVNTAS 245
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-237 |
8.23e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 87.09 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElRRRMQIV--FQDPGG------ 107
Cdd:COG4674 24 KALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHE-IARLGIGrkFQKPTVfeeltv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 ------SMNPRMSVRSIVGEPLqvnrlaeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFIL 181
Cdd:COG4674 103 fenlelALKGDRGVFASLFARL-------TAEERDRIEEVLETIGLT-DKADRLAGLLSHGQKQWLEIGMLLAQDPKLLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 182 LDEPTSALDVSVQAQVLNLLEEIQEKlgltfvfitHALNVVNH-------ISDRVAVMYLGKI 237
Cdd:COG4674 175 LDEPVAGMTDAETERTAELLKSLAGK---------HSVVVVEHdmefvrqIARKVTVLHQGSV 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
37-229 |
9.53e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlydgedirtipDRELRRRMQIVFQdpggsmnprmsvR 116
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQ------------R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGE--PLQVNRLAE-------------GAELTQKVADVLDSVGLKREHMNRFpHEFSGGQKQRLALARALSLDPEFIL 181
Cdd:NF040873 64 SEVPDslPLTVRDLVAmgrwarrglwrrlTRDDRAAVDDALERVGLADLAGRQL-GELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 182 LDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRV 229
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
39-235 |
2.32e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.86 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDrELRRRMQIVFQDPGgsMNPRMSVRsi 118
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPG--IKTELTAL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 vgEPLQVN-RLAEGAElTQKVADVLDSVGLK-REHMnrfP-HEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK13538 93 --ENLRFYqRLHGPGD-DEALWEALAQVGLAgFEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 663511184 196 QVLNLLEEIQEKLGLTfVFITHALnvVNHISDRVAVMYLG 235
Cdd:PRK13538 167 RLEALLAQHAEQGGMV-ILTTHQD--LPVASDKVRKLRLG 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-239 |
3.96e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdirTIPDRELRRRMQIVFQDPGGSMNPRMSVRs 117
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE---PVPSRARHARQRVGVVPQFDNLDPDFTVR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 ivgEPLQVNRLAEG---AELTQKVADVLDSVGLKREHMNRFpHEFSGGQKQRLALARALSLDPEFILLDEPTSALDvsVQ 194
Cdd:PRK13537 99 ---ENLLVFGRYFGlsaAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD--PQ 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 195 AQVLnLLEEIQEKL--GLTFVFITHALNVVNHISDRVAVMYLG-KIVE 239
Cdd:PRK13537 173 ARHL-MWERLRSLLarGKTILLTTHFMEEAERLCDRLCVIEEGrKIAE 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
36-238 |
4.18e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRElRRRMQIVFQDPGGSMNPRMSV 115
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQVNRLAEGAELTQKVADVLDSVGLkrEHM-NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:PRK10895 96 YDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLrDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663511184 195 AQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK10895 174 IDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
35-238 |
4.56e-19 |
|
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: 84.63 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTL-----GRVLLGliPITDGSVLYDGEDIRtiPDrELRRRMQIVFQDpgGSM 109
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLldaisGRVEGG--GTTSGQILFNGQPRK--PD-QFQKCVAYVRQD--DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 NPRMSVRsivgEPLQ-VNRLAEGAELTQKVADVLD-SVGLKREHMNRFPHEF----SGGQKQRLALARALSLDPEFILLD 183
Cdd:cd03234 93 LPGLTVR----ETLTyTAILRLPRKSSDAIRKKRVeDVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 184 EPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-238 |
6.61e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.89 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRaVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPiTDGSVLYDGEDIRTIPDRELRRR-----MQivf 102
Cdd:COG4138 3 LNDVAVAGR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHraylsQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 103 QDPGGSMnPrmsvrsiVGEPLQVNRLAEG--AELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARAL-----SL 175
Cdd:COG4138 78 QSPPFAM-P-------VFQYLALHQPAGAssEAVEQLLAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLlqvwpTI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 176 DPE--FILLDEPTSALDVSVQAQVLNLLEEIQEkLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:COG4138 149 NPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
35-269 |
8.54e-19 |
|
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: 87.17 E-value: 8.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGL--IPITDGSVLY----------------DGE------------ 84
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGEpcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 --DIRTIPD---RELRRRMQIVFQDPGGSMNPRMSVRSIVGEPLQVNRlaEGAELTQKVADVLDSVGLkrEH-MNRFPHE 158
Cdd:TIGR03269 93 evDFWNLSDklrRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGY--EGKEAVGRAVDLIEMVQL--SHrITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 159 FSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
250 260 270
....*....|....*....|....*....|.
gi 663511184 239 EIANTADLFDKpahpythaLMSAIPEPSLEK 269
Cdd:TIGR03269 249 EEGTPDEVVAV--------FMEGVSEVEKEC 271
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
48-266 |
9.87e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 48 GETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQD-PGGSmnpRMSVRSIVG---EPL 123
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAE---GMTVRELVAigrYPW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 124 Q--VNRLaeGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLL 201
Cdd:PRK10575 114 HgaLGRF--GAADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 202 EEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDKPAHPYTHAL-MSAIPEPS 266
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIpMGILPHPA 256
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
40-239 |
1.04e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 84.31 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLiP---ITDGSVLYDGEDIRTIpDRELRRRMQI--VFQDP---GGSMNP 111
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykILEGDILFKGESILDL-EPEERAHLGIflAFQYPieiPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RM------SVRSIVGEPlQVNRLaegaELTQKVADVLDSVGLKREHMNRFPHE-FSGGQKQRLALARALSLDPEFILLDE 184
Cdd:CHL00131 103 DFlrlaynSKRKFQGLP-ELDPL----EFLEIINEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 185 PTSALDVS---VQAQVLNLLEEiQEKlglTFVFITHALNVVNHIS-DRVAVMYLGKIVE 239
Cdd:CHL00131 178 TDSGLDIDalkIIAEGINKLMT-SEN---SIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-237 |
1.17e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.98 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDR-----------ELRRRMQIVFqdpG 106
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisEDRKRDGLVL---G 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSV---RSIVGEPLQVNRLAEgaelTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLD 183
Cdd:PRK10762 345 MSVKENMSLtalRYFSRAGGSLKHADE----QQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 663511184 184 EPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
41-237 |
1.67e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRtipDRELRRRMQ--IVF-----QDPGGSMNPRM 113
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEIN---ALSTAQRLArgLVYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 S--VRSIVGE--PLQVNRLAEGAELTQKVAdvldSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:PRK15439 359 AwnVCALTHNrrGFWIKPARENAVLERYRR----ALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 663511184 190 DVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-240 |
2.98e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRavDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDgedirtIPDRELRRRMQIVFQ-DPG 106
Cdd:COG2401 38 LRVVERYVL--RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGREASLIDAiGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSVRSIVGeplqvnrlaegaeltqkvadvLDSVGLKRehmnRFPHEFSGGQKQRLALARALSLDPEFILLDEPT 186
Cdd:COG2401 110 GDFKDAVELLNAVG---------------------LSDAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 187 SALDVSVqAQVL--NLLEEIQeKLGLTFVFITHALNVVNHIS-DRVAVMYLGKIVEI 240
Cdd:COG2401 165 SHLDRQT-AKRVarNLQKLAR-RAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-270 |
3.84e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTiPDRELRRR---MQIVFqdpggsmnprm 113
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRvgyMSQAF----------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 svrSIVGEpLQV--N-----RL--AEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:NF033858 349 ---SLYGE-LTVrqNlelhaRLfhLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEKLGLTfVFI-THALNVVNHiSDRVAVMYLGKIVEIantadlfDKPAhpythALMSAIP 263
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLAS-------DTPA-----ALVAARG 489
|
....*..
gi 663511184 264 EPSLEKA 270
Cdd:NF033858 490 AATLEEA 496
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
53-249 |
4.83e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.15 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 53 IVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSMNPRMSV-RSIVGEPL-QVNR 127
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPvvlADTFLANVTLgRDISEEQVwQALE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 128 LAEGAELTQKVADVLDS-VGlkrEHMNRfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQE 206
Cdd:PRK10790 452 TVQLAELARSLPDGLYTpLG---EQGNN----LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE 524
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 663511184 207 KlgLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK10790 525 H--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
38-238 |
5.32e-18 |
|
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: 81.06 E-value: 5.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLI--PITDGSVLYDGediRTIPDRELRRRMQIVFQDpgGSMNPRMSV 115
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLING---RPLDKRSFRKIIGYVPQD--DILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RsivgEPLQVNrlaegAELTqkvadvldsvGLkrehmnrfphefSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:cd03213 100 R----ETLMFA-----AKLR----------GL------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663511184 196 QVLNLLEEIQeKLGLTFVFITHAL-NVVNHISDRVAVMYLGKIV 238
Cdd:cd03213 149 QVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-239 |
6.97e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdirTIPD--RELRRRMQIVFQ----DPGGSMNP 111
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPAraRLARARIGVVPQfdnlDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 ---------RMSVRSIvgEPLqVNRLAEGAELTQKvADVLDSvglkrehmnrfphEFSGGQKQRLALARALSLDPEFILL 182
Cdd:PRK13536 134 nllvfgryfGMSTREI--EAV-IPSLLEFARLESK-ADARVS-------------DLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 183 DEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLG-KIVE 239
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
40-246 |
2.92e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSMnpRMSVr 116
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPvlfSGTV--RFNL- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sivgEPLQVNRLAEGAELTQK--VADVL--DSVGLKREhMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PLN03130 1334 ----DPFNEHNDADLWESLERahLKDVIrrNSLGLDAE-VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 193 VQAQVLNLLEEiqEKLGLTFVFITHALNVVnhI-SDRVAVMYLGKIVEIANTADL 246
Cdd:PLN03130 1409 TDALIQKTIRE--EFKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
39-232 |
5.14e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.72 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGedirtipdrelrrrmqivfqdpggsmnprmsvrsi 118
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 vgeplqvnrlaegaelTQKVAdvldsvglkrehmnRFPHeFSGGQKQRLALARALSLDPEFILLDEPTSALDV-SVQAqv 197
Cdd:cd03221 62 ----------------TVKIG--------------YFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSIEA-- 108
|
170 180 190
....*....|....*....|....*....|....*
gi 663511184 198 lnLLEEIQEKLGlTFVFITHALNVVNHISDRVAVM 232
Cdd:cd03221 109 --LEEALKEYPG-TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-237 |
5.80e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 8 GKVLIEVKGMKKWFPikggmlseVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP-ITDGSVLYDGE-- 84
Cdd:PRK13549 256 GEVILEVRNLTAWDP--------VNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpv 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIPDR---------ELRRRMQIVfqdpggsmnPRMSV-RSIVGEPLQ----VNRLAEGAELTQkvadVLDSVglKRE 150
Cdd:PRK13549 328 KIRNPQQAiaqgiamvpEDRKRDGIV---------PVMGVgKNITLAALDrftgGSRIDDAAELKT----ILESI--QRL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 151 HMnRFPHEF------SGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNH 224
Cdd:PRK13549 393 KV-KTASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLG 470
|
250
....*....|...
gi 663511184 225 ISDRVAVMYLGKI 237
Cdd:PRK13549 471 LSDRVLVMHEGKL 483
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
28-237 |
1.21e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP----------ITDGSVLYDGEDIRTIpdRELRRR 97
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLARDI--RKSRAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 98 MQIVFQDpgGSMNPRMSVRSIV------GEPLQVNRLAEGAEL-TQKVADVLDSVGlkrehMNRFPHE----FSGGQKQR 166
Cdd:PRK09984 88 TGYIFQQ--FNLVNRLSVLENVligalgSTPFWRTCFSWFTREqKQRALQALTRVG-----MVHFAHQrvstLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511184 167 LALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
34-252 |
1.28e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 34 HVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIP---------ITdGSVLYDGEDIRTIPDRELRRRMQIVFQ- 103
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgarVT-GDVTLNGEPLAAIDAPRLARLRAVLPQa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 104 -DPGGSMnprmSVRSIV--GEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALS------ 174
Cdd:PRK13547 92 aQPAFAF----SAREIVllGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 175 ---LDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFdKPA 251
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPA 246
|
.
gi 663511184 252 H 252
Cdd:PRK13547 247 H 247
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-275 |
1.95e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 10 VLIEVKGMKKWFPIKGGMLSEVKIHVRAVDGVdlqIKRGETLGIVGESGCGKTTLGRVLLGLIP---ITDGSVLYDGedi 86
Cdd:TIGR00955 16 QDGSWKQLVSRLRGCFCRERPRKHLLKNVSGV---AKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDRELRRRMQIVFQDpggSMN-PRMSVRsivgEPLQVN-RLAEGAELTQK-----VADVLDSVGLKREHMNRFPHE- 158
Cdd:TIGR00955 90 MPIDAKEMRAISAYVQQD---DLFiPTLTVR----EHLMFQaHLRMPRRVTKKekrerVDEVLQALGLRKCANTRIGVPg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 159 ----FSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNV-VNHISDRVAVMY 233
Cdd:TIGR00955 163 rvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSeLFELFDKIILMA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 663511184 234 LGKIV---EIANTADLFDKPAHP----YTHA--LMSAIPE-PSLEKASRERI 275
Cdd:TIGR00955 242 EGRVAylgSPDQAVPFFSDLGHPcpenYNPAdfYVQVLAViPGSENESRERI 293
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-217 |
2.64e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.99 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipdrelrrRMQivfQDPggsmnPRM---SV 115
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA--------RLQ---QDP-----PRNvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQ------------------------VNRLAE---------GAELTQKVADVLDSVGLKREHMnrfPHEFSGG 162
Cdd:PRK11147 84 YDFVAEGIEeqaeylkryhdishlvetdpseknLNELAKlqeqldhhnLWQLENRINEVLAQLGLDPDAA---LSSLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVsvqaQVLNLLEEIQEKLGLTFVFITH 217
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISH 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-260 |
3.42e-16 |
|
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: 77.26 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 27 MLSEVKIHVRAVdgvdlqIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP- 105
Cdd:cd03288 32 NLKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 106 --GGSMNPRMSVRSIVGEplqvNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLD 183
Cdd:cd03288 106 lfSGSIRFNLDPECKCTD----DRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 184 EPTSALDVSVQaqvlNLLEEI--QEKLGLTFVFITHAlnvVNHI--SDRVAVMYLGKIVEIANTADLFDKPAHPYTHALM 259
Cdd:cd03288 182 EATASIDMATE----NILQKVvmTAFADRTVVTIAHR---VSTIldADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
.
gi 663511184 260 S 260
Cdd:cd03288 255 T 255
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-264 |
3.44e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 25 GGMLSEVKIHVR-------AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRR 97
Cdd:PLN03232 1232 RGSIKFEDVHLRyrpglppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 98 MQIVFQDP---GGSMnpRMSVrsivgEPLQVNRLAEGAELTQK--VADVLD--SVGLKREhMNRFPHEFSGGQKQRLALA 170
Cdd:PLN03232 1312 LSIIPQSPvlfSGTV--RFNI-----DPFSEHNDADLWEALERahIKDVIDrnPFGLDAE-VSEGGENFSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 171 RALSLDPEFILLDEPTSALDVSVQAQVLNLLEEiqEKLGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
250
....*....|....
gi 663511184 251 AHPYTHALMSAIPE 264
Cdd:PLN03232 1461 TSAFFRMVHSTGPA 1474
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-231 |
3.68e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 77.06 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 45 IKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDI-----RTIPDRELRRRMQIVFQDPGGSMNPRMsvRSIV 119
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqYIKADYEGTVRDLLSSITKDFYTHPYF--KTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 120 GEPLQVNRLaegaeltqkvadvldsvglkrehMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLN 199
Cdd:cd03237 100 AKPLQIEQI-----------------------LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|..
gi 663511184 200 LLEEIQEKLGLTFVFITHALNVVNHISDRVAV 231
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
36-201 |
4.87e-16 |
|
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: 75.61 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAV-DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDrELRRRMQIVFQDPGgsMNPRMS 114
Cdd:cd03231 13 RALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPG--IKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRsivgEPLQVNRLAEGaelTQKVADVLDSVGLKR-EHmnRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03231 90 VL----ENLRFWHADHS---DEQVEEALARVGLNGfED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 663511184 194 QAQVLNLL 201
Cdd:cd03231 161 VARFAEAM 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-237 |
5.88e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipdrelrrRMQIVFQDPGgsMNPRMSV- 115
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--------NLDAVRQSLG--MCPQHNIl 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 --RSIVGEPLQV-----NRLAEGAELTQKVadVLDSVGLKREHmNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSA 188
Cdd:TIGR01257 1015 fhHLTVAEHILFyaqlkGRSWEEAQLEMEA--MLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 663511184 189 LDVSVQAQVLNLLeeIQEKLGLTFVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:TIGR01257 1092 VDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
36-229 |
7.19e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 36 RAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlydgedirtipDRELRRRMQIVFQDPggSMNPRMsv 115
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKL--YLDTTL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 rsivgePLQVNRLAEGAELTQKvADVLDSvgLKR---EHMNRFP-HEFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK09544 83 ------PLTVNRFLRLRPGTKK-EDILPA--LKRvqaGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 663511184 192 SVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRV 229
Cdd:PRK09544 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
37-250 |
1.21e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.83 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsmnprMSVR 116
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP-------FLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRLAEGAELTQKVADvLDSVglkREHMNRFPHEF-----------SGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK10789 403 DTVANNIALGRPDATQQEIEHVAR-LASV---HDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
41-232 |
1.28e-15 |
|
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: 75.06 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDG--EDIRTIPDRELRRRMQIVF--QDPGgSMNPRMSVR 116
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknESEPSFEATRSRNRYSVAYaaQKPW-LLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQvnrlaegaelTQKVADVLDSVGLKREhMNRFPH-----------EFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:cd03290 99 ITFGSPFN----------KQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 663511184 186 TSALDVSV-----QAQVLNLLEEIQEklglTFVFITHALNVVNHiSDRVAVM 232
Cdd:cd03290 168 FSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAM 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-231 |
1.85e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 2 TEESRDGKVLIEVKGMKKwfpikggMLSEVKIHVRAvdGvdlQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY 81
Cdd:PRK13409 331 PRDESERETLVEYPDLTK-------KLGDFSLEVEG--G---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 82 DgEDIRTIPdrelrrrmQIVFQDPGG-------SMNPRMS---VRSIVGEPLQVNRLaegaeLTQKVADVldsvglkreh 151
Cdd:PRK13409 399 E-LKISYKP--------QYIKPDYDGtvedllrSITDDLGssyYKSEIIKPLQLERL-----LDKNVKDL---------- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 152 mnrfphefSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAV 231
Cdd:PRK13409 455 --------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
37-247 |
1.99e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlydgeDIRTIPDRELRRRMQIVFQDPGGSMNPRMSVr 116
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKNLVAYVPQSEEVDWSFPV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sIVGEPLQVNRLAE-------GAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:PRK15056 96 -LVEDVVMMGRYGHmgwlrraKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 190 DVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDrVAVMYLGKIVEIANTADLF 247
Cdd:PRK15056 174 DVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-246 |
2.38e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP----GgsmnprmSV 115
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPvlfdG-------TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQvnrlAEGAEltqkVADVLDSVGLkREHMNRFPH-----------EFSGGQKQRLALARA-LSLDPEFILLD 183
Cdd:PTZ00243 1401 RQNVDPFLE----ASSAE----VWAALELVGL-RERVASESEgidsrvleggsNYSVGQRQLMCMARAlLKKGSGFILMD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 184 EPTS----ALDVSVQAQVLNLLEeiqeklGLTFVFITHALNVVNHIsDRVAVMYLGKIVEIANTADL 246
Cdd:PTZ00243 1472 EATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-249 |
4.17e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdIRTIPDrelrrrmQIVFQdpggsmNPRMSVRS 117
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQ-------QAWIQ------NDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQV 197
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 198 lnlLEEIQEKLGL----TFVFITHALNVVNHIsDRVAVMYLGKIVEIANTADLFDK 249
Cdd:TIGR00957 800 ---FEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-231 |
5.64e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 44 QIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlydGEDIRT-------IPDRELRRR---MQIVFQDPGGSMnprm 113
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKIsykpqyiSPDYDGTVEeflRSANTDDFGSSY---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 sVRSIVGEPLQVNRLaegaeLTQKVADVldsvglkrehmnrfphefSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:COG1245 435 -YKTEIIKPLGLEKL-----LDKNVKDL------------------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 663511184 194 QAQVLNLLEEIQEKLGLTFVFITHALNVVNHISDRVAV 231
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-238 |
6.11e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRAVDG------VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE--DIRTIPDR------- 92
Cdd:PRK11288 253 LGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAiragiml 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 93 --ELRRRMQIVfqdPGGSM--NPRMSVR---SIVGEPLQVNRLAEGAELTqkvadvLDSVGLKREHMNRFPHEFSGGQKQ 165
Cdd:PRK11288 333 cpEDRKAEGII---PVHSVadNINISARrhhLRAGCLINNRWEAENADRF------IRSLNIKTPSREQLIMNLSGGNQQ 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663511184 166 RLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-236 |
7.00e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 9 KVLIEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRt 88
Cdd:PRK10762 2 QALLQLKGIDKAFP-----------GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 89 ipdrelrrrmqivFQDPGGSMNPRMSvrsIVGEPLqvNRLAE---------GAELTQKV-----------ADVLdsvgLK 148
Cdd:PRK10762 70 -------------FNGPKSSQEAGIG---IIHQEL--NLIPQltiaeniflGREFVNRFgridwkkmyaeADKL----LA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 149 REHMNRFPH----EFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNH 224
Cdd:PRK10762 128 RLNLRFSSDklvgELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFE 206
|
250
....*....|..
gi 663511184 225 ISDRVAVMYLGK 236
Cdd:PRK10762 207 ICDDVTVFRDGQ 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-238 |
2.11e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 44 QIKRGETLGIVGESGCGKTTLGRVLLGLIPiTDGSVLYDGEDIRTIPDREL-RRRMQIVFQDPGGSMNP--------RMS 114
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPvfqyltlhQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEGAELTQKvadvldsvglkrehMNRFPHEFSGGQKQRLALARAL-----SLDPE--FILLDEPTS 187
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDK--------------LGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 663511184 188 ALDVSVQAQVLNLLEEIQEkLGLTFVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
27-239 |
3.70e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 71.36 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 27 MLSEVKIHVRAVD-----GVDLQIKRGETLGIVGESGCGKTTLGRVLLGL--IPITDGSVLYDGEDIRTI-PDRELRRRM 98
Cdd:PRK09580 1 MLSIKDLHVSVEDkailrGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELsPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 99 QIVFQDP------------GGSMNprmSVRSIVG-EPLQ----VNRLAEGAELTQKVADVLD-SVGLKrehmnrfpheFS 160
Cdd:PRK09580 81 FMAFQYPveipgvsnqfflQTALN---AVRSYRGqEPLDrfdfQDLMEEKIALLKMPEDLLTrSVNVG----------FS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 161 GGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHIS-DRVAVMYLGKIVE 239
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-184 |
3.98e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 73.29 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIrTIPDRE-LRRRMQIVFQD-------PGGSMNPr 112
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-TADNREaYRQLFSAVFSDfhlfdrlLGLDGEA- 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 113 msvrsivgEPLQVNRLAEGAELTQKVA---DVLDSVGLkrehmnrfphefSGGQKQRLALARALSLDPEFILLDE 184
Cdd:COG4615 429 --------DPARARELLERLELDHKVSvedGRFSTTDL------------SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
38-246 |
5.95e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIR-TIPDRELRRRMQIVFQD-------PGGSM 109
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESrrdngffPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 110 NPRMSV-RSIVGEPLQ--VNRLAEGAEltQKVADVL-DSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEP 185
Cdd:PRK09700 359 AQNMAIsRSLKDGGYKgaMGLFHEVDE--QRTAENQrELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEI-ANTADL 246
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQIlTNRDDM 497
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-217 |
9.43e-14 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 72.47 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 44 QIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGsvlydgedIRTIPDRelrrrmQIVFQDPggsMNPRMSVRSI---VG 120
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG--------RLTKPAK------GKLFYVP---QRPYMTLGTLrdqII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 121 EPLQVNRLAEGAELTQKVADVLDSVGL----KRE----HMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:TIGR00954 537 YPDSSEDMKRRGLSDKDLEQILDNVQLthilEREggwsAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|....*
gi 663511184 193 VQAQVLNLLEEIqeklGLTFVFITH 217
Cdd:TIGR00954 617 VEGYMYRLCREF----GITLFSVSH 637
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-282 |
1.60e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 1 MTEESRDGKVLIEVKGMKKWFpikGGmlsevkihVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVL 80
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQY---SG--------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 81 YDGEDI-RTIPDRELRRRMQIVFQDPggSMNPRMSVRSIVgeplqVNRLAEGAELTQKVADVLDSVGLkreHMNrfPHEF 159
Cdd:PRK15439 70 IGGNPCaRLTPAKAHQLGIYLVPQEP--LLFPNLSVKENI-----LFGLPKRQASMQKMKQLLAALGC---QLD--LDSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 160 SG----GQKQRLALARALSLDPEFILLDEPTSALdvsVQAQVLNLLEEIQE--KLGLTFVFITHALNVVNHISDRVAVMY 233
Cdd:PRK15439 138 AGslevADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMR 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 663511184 234 LGKIVEIANTADLFDKpahpythALMSAIPEPSLEKASRERIVLSGDVP 282
Cdd:PRK15439 215 DGTIALSGKTADLSTD-------DIIQAITPAAREKSLSASQKLWLELP 256
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-190 |
4.12e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLgrvlLGLIP----ITDGSVLYDGEDIRtipDRELRRRM--QIVF--QDPG 106
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIAgarkIQQGRVEVLGGDMA---DARHRRAVcpRIAYmpQGLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 107 GSMNPRMSVRsivgEPLQ-VNRL--AEGAELTQKVADVLDSVGLKRehmnrFPH----EFSGGQKQRLALARALSLDPEF 179
Cdd:NF033858 87 KNLYPTLSVF----ENLDfFGRLfgQDAAERRRRIDELLRATGLAP-----FADrpagKLSGGMKQKLGLCCALIHDPDL 157
|
170
....*....|.
gi 663511184 180 ILLDEPTSALD 190
Cdd:NF033858 158 LILDEPTTGVD 168
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
38-238 |
5.05e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.29 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPIT---DGSVLYDGEDIRTIPDRELRrrmQIVFQDPGGSMNPRMS 114
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG---EIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRsivgEPLQVNRLAEGaeltqkvadvldsvglkrehmNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:cd03233 100 VR----ETLDFALRCKG---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 663511184 195 AQVLNLLEEIQEKLGLT-FVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:cd03233 155 LEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-247 |
1.81e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 23 IKGGMLS-EVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLG-LIPITDGSVLYDGE-----DIRTIPDRELR 95
Cdd:PLN03232 617 IKNGYFSwDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSvayvpQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 96 RrmQIVFqdpGGSMNPRMSVRSIVGEPLQVN-RLAEGAELTQkvadvldsVGLKREHMnrfphefSGGQKQRLALARALS 174
Cdd:PLN03232 697 E--NILF---GSDFESERYWRAIDVTALQHDlDLLPGRDLTE--------IGERGVNI-------SGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511184 175 LDPEFILLDEPTSALDVSVQAQVLN--LLEEIQeklGLTFVFITHALNVVNHIsDRVAVMYLGKIVEIANTADLF 247
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-240 |
1.85e-12 |
|
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: 64.32 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 47 RGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY-DGEDIRTIPDRELRRrmqivfqdpggsmnprmsvrsivgeplqv 125
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 126 nrlaegaeltqkvadvldsvglkrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVL-----NL 200
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 663511184 201 LEEIQEKLGLTFVFITHalnVVNHISDRVAVMYLGKIVEI 240
Cdd:smart00382 108 LLLLKSEKNLTVILTTN---DEKDLGPALLRRRFDRRIVL 144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-276 |
1.90e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRE-LRRRMQIVFQDPggSMNPRM 113
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQEL--HLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVrsivGEPLQVNRLAE------GAELTQKVADVLDSVGLKREhmnrfPH----EFSGGQKQRLALARALSLDPEFILLD 183
Cdd:PRK11288 95 TV----AENLYLGQLPHkggivnRRLLNYEAREQLEHLGVDID-----PDtplkYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 184 EPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEiantadlfdkpahpyTHalmsaip 263
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA---------------TF------- 222
|
250
....*....|...
gi 663511184 264 ePSLEKASRERIV 276
Cdd:PRK11288 223 -DDMAQVDRDQLV 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-246 |
2.01e-12 |
|
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: 68.43 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQDP---GGSMNPRMSVRS 117
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPvlfSGSLRMNLDPFS 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVGEPlQVNRLAEGAELTQKVADVLDsvGLKREhMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVS----V 193
Cdd:TIGR00957 1385 QYSDE-EVWWALELAHLKTFVSALPD--KLDHE-CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLEtdnlI 1460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 663511184 194 QAQVLNLLEEIqeklglTFVFITHALNVVNHISdRVAVMYLGKIVEIANTADL 246
Cdd:TIGR00957 1461 QSTIRTQFEDC------TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
37-240 |
2.29e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRELRRRMQIVFQD---------PGG 107
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDfhlfdqllgPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 SmnprmsvrsiVGEPLQVNRLAEGAELTQKVadvldsvglkREHMNRFPH-EFSGGQKQRLALARALSLDPEFILLDEpt 186
Cdd:PRK10522 418 K----------PANPALVEKWLERLKMAHKL----------ELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDE-- 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 187 SALDVSVQAQ---VLNLLEEIQEKlGLTFVFITHALNVVNHiSDRVAVMYLGKIVEI 240
Cdd:PRK10522 476 WAADQDPHFRrefYQVLLPLLQEM-GKTIFAISHDDHYFIH-ADRLLEMRNGQLSEL 530
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-249 |
2.57e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 23 IKGGMLS-EVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLG-LIPITDGSVLYDGE-----DIRTIPDRELR 95
Cdd:PLN03130 617 IKNGYFSwDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvpQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 96 RrmQIVFqdpGGSMNPRMSVRSIVGEPLQVN-RLAEGAELTQkvadvldsvgLKREHMNrfpheFSGGQKQRLALARALS 174
Cdd:PLN03130 697 D--NILF---GSPFDPERYERAIDVTALQHDlDLLPGGDLTE----------IGERGVN-----ISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 175 LDPEFILLDEPTSALDVSVQAQVLN--LLEEIQEKlglTFVFITHALNVVNHIsDRVAVMYLGKIVE------IANTADL 246
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMIKEegtyeeLSNNGPL 832
|
...
gi 663511184 247 FDK 249
Cdd:PLN03130 833 FQK 835
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-224 |
2.77e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 1 MTEESRDGKVLIEVKGMKkwfpikggmLSEVKIH------VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPI 74
Cdd:PTZ00265 367 LVENNDDGKKLKDIKKIQ---------FKNVRFHydtrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 75 TDGSVLY-DGEDIRTIPDRELRRRMQIVFQDP-----------------------------------GGSMNPRMSVRSI 118
Cdd:PTZ00265 438 TEGDIIInDSHNLKDINLKWWRSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 VGEPLQ-VNRLAEGAELTQ-----------KVADVLDSVgLKREHMNRFPHEF-----------SGGQKQRLALARALSL 175
Cdd:PTZ00265 518 CAGDLNdMSNTTDSNELIEmrknyqtikdsEVVDVSKKV-LIHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIR 596
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 663511184 176 DPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNH 224
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
41-250 |
4.77e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDgedirtipdrelrRRMQIVFQDPGgSMNPrmSVRS--I 118
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAW-IMNA--TVRGniL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 119 VGEPLQVNRLAEGAELTQKVADV-LDSVGLKREhMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQV 197
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLEADLaQLGGGLETE-IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 663511184 198 LNllEEIQEKL-GLTFVFITHALNVVNHiSDRVAVMYLGKIVEIANTADLFDKP 250
Cdd:PTZ00243 822 VE--ECFLGALaGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-235 |
4.84e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.35 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipdrelrrRMQIVFQDPG-----GSMNP 111
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--------NISDVHQNMGycpqfDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 112 RMSVRsivgEPLQVNRLAEG--AELTQKVAD-VLDSVGLKReHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSA 188
Cdd:TIGR01257 2026 LLTGR----EHLYLYARLRGvpAEEIEKVANwSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 663511184 189 LDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLG 235
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-233 |
1.12e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRAVDGVDL----QIKRGETLGIVGESGCGKTTLGRVLLG-LIP---ITDGSV-------------------- 79
Cdd:PRK13409 75 LEEEPVHRYGVNGFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGeLIPnlgDYEEEPswdevlkrfrgtelqnyfkk 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 80 LYDGEdIRTIpdrelrRRMQIVFQDPggsmnprMSVRSIVGEplqvnrLAEGAELTQKVADVLDSVGLkREHMNRFPHEF 159
Cdd:PRK13409 155 LYNGE-IKVV------HKPQYVDLIP-------KVFKGKVRE------LLKKVDERGKLDEVVERLGL-ENILDRDISEL 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511184 160 SGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEklGLTFVFITHALNVVNHISDRVAVMY 233
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-231 |
1.24e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 76 DGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsMNPRMSV---------RSIVGEPLQVNRLAEGAELTQKVADVLDSvg 146
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEP---MLFNMSIyenikfgkeDATREDVKRACKFAAIDEFIESLPNKYDT-- 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 147 lkreHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLTFVFITHALNVVNHiS 226
Cdd:PTZ00265 1351 ----NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-S 1425
|
....*
gi 663511184 227 DRVAV 231
Cdd:PTZ00265 1426 DKIVV 1430
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-233 |
3.00e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRAVDGVDL----QIKRGETLGIVGESGCGKTTLGRVLLG-LIP-------------ITD---GSVLYDgeDI 86
Cdd:COG1245 75 LEEDPVHRYGENGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGeLKPnlgdydeepswdeVLKrfrGTELQD--YF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 87 RTIPDRELR--RRMQIVFQDPggsmnprMSVRSIVGEplqvnrLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQK 164
Cdd:COG1245 153 KKLANGEIKvaHKPQYVDLIP-------KVFKGTVRE------LLEKVDERGKLDELAEKLGLE-NILDRDISELSGGEL 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 165 QRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMY 233
Cdd:COG1245 219 QRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-233 |
4.38e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITD--GSVLYDGEDirtiPDRELRRRMQIVFQDpgGSMNPRMSV 115
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK----PTKQILKRTGFVTQD--DILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RS--IVGEPLQVNRLAEGAELTQKVADVLDSVGL-KREHM---NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSAL 189
Cdd:PLN03211 158 REtlVFCSLLRLPKSLTKQEKILVAESVISELGLtKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663511184 190 DVSVQAQVLNLLEEIQEKlGLTFVFITHalnvvnHISDRVAVMY 233
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQK-GKTIVTSMH------QPSSRVYQMF 274
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-233 |
6.80e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.00 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 46 KRGETLGIVGESGCGKTTLGRVLLG-LIPitdGSVLYDGE-DIRTIPDRELRRRMQIVFQD-PGGSMNPRMSVRSIVGEP 122
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGkLKP---NLGKFDDPpDWDEILDEFRGSELQNYFTKlLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 123 LQVN----RLAEGAELTQKVADVLDSVGLkREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSvqaQVL 198
Cdd:cd03236 101 KAVKgkvgELLKKKDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK---QRL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 663511184 199 NLLEEIQE--KLGLTFVFITHALNVVNHISDRVAVMY 233
Cdd:cd03236 177 NAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
37-248 |
2.32e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlydgeDIRTipdrelrrrmQIVFQDPGGSMNPRMS-V 115
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG----------SAALIAISSGLNGQLTgI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 116 RSIVGEPLQVNRLAEG-AELTQKVADVLDsVGlkrEHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQ 194
Cdd:PRK13545 104 ENIELKGLMMGLTKEKiKEIIPEIIEFAD-IG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 663511184 195 AQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFD 248
Cdd:PRK13545 180 KKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
45-233 |
9.53e-10 |
|
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: 57.20 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 45 IKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPdrelrrrmqivfqdpggsmnprmsvrsivgeplq 124
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP---------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 125 vnrlaegaeltQKVadvldsvglkrehmnrfphEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEI 204
Cdd:cd03222 68 -----------QYI-------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 663511184 205 QEKLGLTFVFITHALNVVNHISDRVAVMY 233
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
41-190 |
1.77e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipdRELRRRMQIVFQDPGgsMNPRMSVRsivg 120
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPG--LKADLSTL---- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511184 121 EPLQVNRLAEGAELTQKVADVLDSVGLKrEHMNRFPHEFSGGQKQRLALARaLSLDPEFI-LLDEPTSALD 190
Cdd:PRK13543 101 ENLHFLCGLHGRRAKQMPGSALAIVGLA-GYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-229 |
2.87e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGE-------------DIRTIP-----DRELR---R 96
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALEyvidgDREYRqleA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 97 RMQIVFQDPGGSmnprmSVRSIVGEPLQVNRLAegaeLTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLD 176
Cdd:PRK10636 97 QLHDANERNDGH-----AIATIHGKLDAIDAWT----IRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 663511184 177 PEFILLDEPTSALDVSVqaqVLNLLEEIQEKLGlTFVFITHALNVVNHISDRV 229
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-204 |
4.44e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 3 EESRDGKVLIEVKGMKkwFPIKGGMLsevkihvraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVlYD 82
Cdd:PRK11147 311 EASRSGKIVFEMENVN--YQIDGKQL---------VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 83 GEdirtipdrelrrRMQIVFQDP-GGSMNPRMSVrsivgeplqVNRLAEGaelTQKVadvldSVGLKREHMNRFPHEF-- 159
Cdd:PRK11147 379 GT------------KLEVAYFDQhRAELDPEKTV---------MDNLAEG---KQEV-----MVNGRPRHVLGYLQDFlf 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 160 ------------SGGQKQRLALARaLSLDP-EFILLDEPTSALDVsvqaQVLNLLEEI 204
Cdd:PRK11147 430 hpkramtpvkalSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV----ETLELLEEL 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-244 |
5.32e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 21 FPIKGGMLSEVKIHVR--------AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDR 92
Cdd:PRK10982 239 FPDKENKPGEVILEVRnltslrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 93 EL----------RRRMQIVFQDPGGSMNprmSVRSIVGEPLQVNRLAEGAELTQKVADVLDSVGLKREHMNRFPHEFSGG 162
Cdd:PRK10982 319 EAinhgfalvteERRSTGIYAYLDIGFN---SLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 163 QKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIAN 242
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIVD 474
|
..
gi 663511184 243 TA 244
Cdd:PRK10982 475 TK 476
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-249 |
5.98e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 137 KVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVqaqVLnLLEEIQEKLGLTFVFIT 216
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VL-WLETYLLKWPKTFIVVS 398
|
90 100 110
....*....|....*....|....*....|...
gi 663511184 217 HALNVVNHISDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PLN03073 399 HAREFLNTVVTDILHLHGQKLVTYKGDYDTFER 431
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-246 |
8.31e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTIPDRE-LRRRMQIVFQDpggsMNprM 113
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQE----LN--L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRSIVGEPLQVNRLAEGAEL---------TQKVADVLDSVGLKREHMNrfphEFSGGQKQRLALARALSLDPEFILLDE 184
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFvdqdkmyrdTKAIFDELDIDIDPRAKVA----TLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511184 185 PTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADL 246
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
38-198 |
9.48e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.63 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPiTDGSVLYDGEDIRTIPDRELRRRMQIVFQDPggsmnprmsvrS 117
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKV-----------F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 118 IVGEPLQVNRLAEGAELTQKVADVLDSVGLKREhMNRFPHEF-----------SGGQKQRLALARALSLDPEFILLDEPT 186
Cdd:cd03289 88 IFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSV-IEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170
....*....|..
gi 663511184 187 SALDvSVQAQVL 198
Cdd:cd03289 167 AHLD-PITYQVI 177
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-221 |
1.18e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.87 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 28 LSEVKIHVRAVDGVDLQIKRGETLGIVGESGCGKTTLgrvllglipITDGsvLYDGEDIRTIPDRELRRRMQIVFQDpgg 107
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL---------VNEG--LYASGKARLISFLPKFSRNKLIFID--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 smnprmsvrsivgeplQVNRLAEgaeltqkvadvldsVGLKREHMNRFPHEFSGGQKQRLALARALSLDPE--FILLDEP 185
Cdd:cd03238 67 ----------------QLQFLID--------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190
....*....|....*....|....*....|....*.
gi 663511184 186 TSALDVSVQAQVLNLLEEIQEkLGLTFVFITHALNV 221
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDV 151
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-217 |
2.17e-08 |
|
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: 55.71 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 6 RDGKVLIEVKGMKKWFPIKggMLsevkihvraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYdGED 85
Cdd:TIGR03719 317 RLGDKVIEAENLTKAFGDK--LL---------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 86 IrtipdrelrrrmQIVFQDPG-GSMNPRMSVRSIVGEPL--------QVNRLAEGAELTQKVADVLDSVGlkrehmnrfp 156
Cdd:TIGR03719 385 V------------KLAYVDQSrDALDPNKTVWEEISGGLdiiklgkrEIPSRAYVGRFNFKGSDQQKKVG---------- 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511184 157 hEFSGGQKQRLALARALSLDPEFILLDEPTSALDVsvqaQVLNLLEEIQEKLGLTFVFITH 217
Cdd:TIGR03719 443 -QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISH 498
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-252 |
2.96e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 5 SRDGKVLIEVKGMKKWFPikggmlsevkiHVRAVDGVDLQIKRGETLGIVGESGCGKTTlgrvllGLIPitdgsVLYDGE 84
Cdd:NF000106 7 SNGARNAVEVRGLVKHFG-----------EVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALP-----AHV*GP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 85 DIRTIP---------DRELRRRM---QIVFQDPGGSMNPRMSVRsIVGEPLQVNRlaegAELTQKVADVLDSVGLKrEHM 152
Cdd:NF000106 65 DAGRRPwrf*twcanRRALRRTIg*hRPVR*GRRESFSGRENLY-MIGR*LDLSR----KDARARADELLERFSLT-EAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 153 NRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVM 232
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVI 217
|
250 260
....*....|....*....|....*....
gi 663511184 233 YLGKIVEIANTADLFDK---------PAH 252
Cdd:NF000106 218 DRGRVIADGKVDELKTKvggrtlqirPAH 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-245 |
3.41e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 12 IEVKGMKKWFPikGGMLsevkihvraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLY-DGEDIRTIP 90
Cdd:PRK15064 320 LEVENLTKGFD--NGPL---------FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 91 ---------DRELRRRMQiVFQDPGGSmnpRMSVRSIVGeplqvnRLAEGAELTQKVADVLdsvglkrehmnrfphefSG 161
Cdd:PRK15064 389 qdhaydfenDLTLFDWMS-QWRQEGDD---EQAVRGTLG------RLLFSQDDIKKSVKVL-----------------SG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 162 GQKQRLALARALSLDPEFILLDEPTSALDV-SVQAqvLNL-LEEIQeklGlTFVFITHALNVVNHISDRVAVMYLGKIVE 239
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNMaLEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
....*.
gi 663511184 240 IANTAD 245
Cdd:PRK15064 516 FSGTYE 521
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-237 |
6.95e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 38 VDGVDLQIKRGETLGIVGESGCGKTTLGRVLLG-LIPITDGSVLYDGEDIRTIPDRELRrrmqivFQDPGGSmnprmsvr 116
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLGYFAQHQLE------FLRADES-------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 sivgePLQ-VNRLAEgAELTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQA 195
Cdd:PRK10636 394 -----PLQhLARLAP-QELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663511184 196 QVLNLLEEIQEKLgltfVFITHALNVVNHISDRVAVMYLGKI 237
Cdd:PRK10636 468 ALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-238 |
8.38e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 4 ESRDGKVLIEVKGMKKWFPIKggmlSEVKIhvraVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGL---IPITdGSVL 80
Cdd:NF040905 250 TPKIGEVVFEVKNWTVYHPLH----PERKV----VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNIS-GTVF 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 81 YDGE--DIRTIPD---------RELRRRMQIVFQDP-----GGSMNPRMSVRSIVGEPLQVnRLAEG--AELTQKVADVL 142
Cdd:NF040905 321 KDGKevDVSTVSDaidaglayvTEDRKGYGLNLIDDikrniTLANLGKVSRRGVIDENEEI-KVAEEyrKKMNIKTPSVF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 143 DSVGlkrehmnrfphEFSGGQKQRLALARALSLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVV 222
Cdd:NF040905 400 QKVG-----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPEL 467
|
250
....*....|....*.
gi 663511184 223 NHISDRVAVMYLGKIV 238
Cdd:NF040905 468 LGMCDRIYVMNEGRIT 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
48-217 |
9.55e-08 |
|
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: 53.40 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 48 GETLGIVGESGCGKTTLGRVLLGLipitDGSvlYDGEdIRTIPDRelrrRMQIVFQDPggSMNPRMSVRSIVGEPLQ--V 125
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGV----DKD--FNGE-ARPQPGI----KVGYLPQEP--QLDPTKTVRENVEEGVAeiK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 126 NRLAEGAELTQKVAD-----------------VLDSVG---LKRE---HMN--RFP------HEFSGGQKQRLALARALS 174
Cdd:TIGR03719 98 DALDRFNEISAKYAEpdadfdklaaeqaelqeIIDAADawdLDSQleiAMDalRCPpwdadvTKLSGGERRRVALCRLLL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 663511184 175 LDPEFILLDEPTSALDvsvqAQVLNLLEE-IQEKLGlTFVFITH 217
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD----AESVAWLERhLQEYPG-TVVAVTH 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
41-197 |
1.01e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.55 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdIRTIPdrelrrrmQIVFQDPG--------GSMNPR 112
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS--------QFSWIMPGtikeniifGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 113 MSVRSIVgeplQVNRLAEG-AELTQKVADVLDSVGLKrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:cd03291 127 YRYKSVV----KACQLEEDiTKFPEKDNTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*.
gi 663511184 192 SVQAQV 197
Cdd:cd03291 193 FTEKEI 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
41-206 |
1.04e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 41 VDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEDIRTipDRELRRRmQIVFQDPGGSMNPRMSVRSIVG 120
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQK-QLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 121 EPLQVNRLAEGAELTQKVadvldsvgLKREHMNRFP-HEFSGGQKQRLALARALSLDPEFILLDEPTSALDvsvQAQVLN 199
Cdd:PRK13540 97 YDIHFSPGAVGITELCRL--------FSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLT 165
|
....*..
gi 663511184 200 LLEEIQE 206
Cdd:PRK13540 166 IITKIQE 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-232 |
1.22e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 42 DLQIKRGETLGIVGESGCGKTTLGRVLLGLIPitdgsvLYDGE---DIRTIPDRELRRRMQIV---FQD-------PGGS 108
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP------LLSGErqsQFSHITRLSFEQLQKLVsdeWQRnntdmlsPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 109 MNPRMSVRSIVGEPLQVNRLAEGAELTQkVADVLDsvglkrehmNRFPHeFSGGQKQRLALARALSLDPEFILLDEPTSA 188
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPARCEQLAQQFG-ITALLD---------RRFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 663511184 189 LDVSVQAQVLNLLEEIQEKlGLTFVFIthaLNVVNHISD---RVAVM 232
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLV---LNRFDEIPDfvqFAGVL 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-198 |
1.86e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 25 GGMLSEVKIHVRAV-DGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdIRTIPdrelrrrmQIVFQ 103
Cdd:TIGR01271 428 GLFFSNFSLYVTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP--------QTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 104 DPG--------GSMNPRMSVRSIVgeplQVNRLAEG-AELTQKVADVLDSVGLKrehmnrfpheFSGGQKQRLALARALS 174
Cdd:TIGR01271 499 MPGtikdniifGLSYDEYRYTSVI----KACQLEEDiALFPEKDKTVLGEGGIT----------LSGGQRARISLARAVY 564
|
170 180
....*....|....*....|....
gi 663511184 175 LDPEFILLDEPTSALDVSVQAQVL 198
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKEIF 588
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
53-227 |
2.10e-07 |
|
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: 50.68 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 53 IVGESGCGKTT----LGRVLLGLIPITDGSVLYDGEDIRtipdrELRRRMQIvfqdpggsmnpRMSVRSIVGEPLQVNRl 128
Cdd:cd03240 27 IVGQNGAGKTTiieaLKYALTGELPPNSKGGAHDPKLIR-----EGEVRAQV-----------KLAFENANGKKYTITR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 129 aegaeltqKVADVLDSVGLKREHMN----RFPHEFSGGQKQ------RLALARALSLDPEFILLDEPTSALDV-SVQAQV 197
Cdd:cd03240 90 --------SLAILENVIFCHQGESNwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESL 161
|
170 180 190
....*....|....*....|....*....|
gi 663511184 198 LNLLEEIQEKLGLTFVFITHALNVVNHISD 227
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDEELVDAADH 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-201 |
4.55e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 30 EVKI---HVRAVDGVDLQIKRGETLGIVGESGCGKTTL-----GRVLLGLipITDGSVLYDGEDIrtipDRELRRRMQIV 101
Cdd:TIGR00956 768 EVKIkkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGV--ITGGDRLVNGRPL----DSSFQRSIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 102 FQdpggsmNPRMSVRSIVGEPLQVN-RLAEGAELT--------QKVADVLDS-------VGLKREHMNRfphefsgGQKQ 165
Cdd:TIGR00956 842 QQ------QDLHLPTSTVRESLRFSaYLRQPKSVSksekmeyvEEVIKLLEMesyadavVGVPGEGLNV-------EQRK 908
|
170 180 190
....*....|....*....|....*....|....*..
gi 663511184 166 RLALARALSLDPEFIL-LDEPTSALDVSVQAQVLNLL 201
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLM 945
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
37-249 |
1.02e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 37 AVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYDGEdIRTIpdrelrrrmqivfqdpggSMNPRMSVR 116
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVI------------------AISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 117 SIVGEPLQVNRLAEGaeLTQKVADVLDSVGLKREHMNRFPHE----FSGGQKQRLALARALSLDPEFILLDEPTSALDVS 192
Cdd:PRK13546 100 LTGIENIEFKMLCMG--FKRKEIKAMTPKIIEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 663511184 193 VQAQVLNLLEEIQEKlGLTFVFITHALNVVNHISDRVAVMYLGKIVEIANTADLFDK 249
Cdd:PRK13546 178 FAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
39-204 |
3.23e-06 |
|
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: 47.24 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 39 DGVDLQIKRGETLGIVGESGCGKTTLGRVL-----LGLIpitDGSVLYDGEDIrtipDRELRRRMQIVFQDPggSMNPRM 113
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPL----DKNFQRSTGYVEQQD--VHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 114 SVRsivgEPLQVNRLAEGaeltqkvadvldsvglkrehmnrfpheFSGGQKQRLALARALSLDPEFILLDEPTSALDVSV 193
Cdd:cd03232 95 TVR----EALRFSALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170
....*....|.
gi 663511184 194 QAQVLNLLEEI 204
Cdd:cd03232 144 AYNIVRFLKKL 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
52-227 |
4.37e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 52 GIVGESGCGKTTLGRVLLG-LIPiTDGSVLYDG--------------EDIRTIP-----DRELRRRMQ----IVfqdpgg 107
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGdLEP-SAGNVSLDPnerlgklrqdqfafEEFTVLDtvimgHTELWEVKQerdrIY------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 108 sMNPRMS----VRsiVGEpLQVnRLAE----GAEltQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEF 179
Cdd:PRK15064 104 -ALPEMSeedgMK--VAD-LEV-KFAEmdgyTAE--ARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 663511184 180 ILLDEPTSALDVSvqaqVLNLLEEIQEKLGLTFVFITHA---LN-VVNHISD 227
Cdd:PRK15064 177 LLLDEPTNNLDIN----TIRWLEDVLNERNSTMIIISHDrhfLNsVCTHMAD 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
160-233 |
5.99e-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: 45.81 E-value: 5.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 160 SGGQKQRLALARALSL-----DPeFILLDEPTSALDVSVQAQVLNLLEEiQEKLGLTFVFITHALNVVNhISDRVAVMY 233
Cdd:cd03227 79 SGGEKELSALALILALaslkpRP-LYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-191 |
9.15e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 6 RDGKVLIEVKGMKKWFpikGGMLsevkihvrAVDGVDLQIKRGETLGIVGESGCGKTTLGRVLLGLIPITDGSVLYdGED 85
Cdd:PRK11819 319 RLGDKVIEAENLSKSF---GDRL--------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 86 IrtipdrelrrrmQIVFQDPG-GSMNPRMSVRSIVGEPL--------QVNRLA-------EGAElTQKVADVLdsvglkr 149
Cdd:PRK11819 387 V------------KLAYVDQSrDALDPNKTVWEEISGGLdiikvgnrEIPSRAyvgrfnfKGGD-QQKKVGVL------- 446
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 663511184 150 ehmnrfphefSGGQKQRLALARALSLDPEFILLDEPTSALDV 191
Cdd:PRK11819 447 ----------SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-201 |
8.54e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 40 GVDLQIKrgetLGIVGESGCGKTTLGRVLLGLIPITDGSVLydgedirtipdRELRRRMQIVFQDPGGSMNprMSVRSIv 119
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHVDGLD--LSSNPL- 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 120 gepLQVNRLAEGAeLTQKVADVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSLDPEFILLDEPTSALDV-SVQAQVL 198
Cdd:PLN03073 593 ---LYMMRCFPGV-PEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQ 668
|
...
gi 663511184 199 NLL 201
Cdd:PLN03073 669 GLV 671
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-238 |
9.08e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 35 VRAVDGVdlqIKRGETLGIVGESGCGKTTLGRVLLGLIP----ITDGSVLYDGedirtIPDRELRR--RMQIVFQDPGGS 108
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDG-----ITPEEIKKhyRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 109 MNPRMSV----------RSIVGEPLQVNRLaegaELTQKVADV-LDSVGLKREHMNRFPHEF----SGGQKQRLALARAL 173
Cdd:TIGR00956 149 HFPHLTVgetldfaarcKTPQNRPDGVSRE----EYAKHIADVyMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEAS 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 174 SLDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKLGLT-FVFITHALNVVNHISDRVAVMYLGKIV 238
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQI 290
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-222 |
1.19e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.99 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 140 DVLDSVGLKREHMNRFPHEFSGGQKQRLALARALSL---DPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFIT 216
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIE 229
|
....*.
gi 663511184 217 HALNVV 222
Cdd:cd03271 230 HNLDVI 235
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
160-222 |
1.89e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511184 160 SGGQKQRLALARALS---LDPEFILLDEPTSALDVSVQAQVLNLLEEIQEKlGLTFVFITHALNVV 222
Cdd:TIGR00630 831 SGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIEHNLDVI 895
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
53-217 |
2.17e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 53 IVGESGCGKTTL---------GRVLlGLIPITDGSVLYDGEDIR-----TIPDRELR-RRMQ---IVFQDPGGSmnprmS 114
Cdd:COG0419 28 IVGPNGAGKSTIleairyalyGKAR-SRSKLRSDLINVGSEEASvelefEHGGKRYRiERRQgefAEFLEAKPS-----E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 115 VRSIVGEPLQVNRLAEG--------AELTQKVADVLDSVGLKREHMNRF-----PHEFSGGQKQRLALARALSLdpefiL 181
Cdd:COG0419 102 RKEALKRLLGLEIYEELkerlkeleEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALADLLSL-----I 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 663511184 182 LDepTSALDVSVQAQVLNLLEEIQeklgltfvFITH 217
Cdd:COG0419 177 LD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-229 |
2.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 142 LDSVGLKREHMNRFPHEFSGGQKQRLALARAL---SLDPEFILLDEPTSAL---DVSVQAQVLNLLEEiqekLGLTFVFI 215
Cdd:PRK00635 793 LCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTH----QGHTVVII 868
|
90
....*....|....
gi 663511184 216 THALNVVNhISDRV 229
Cdd:PRK00635 869 EHNMHVVK-VADYV 881
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
160-217 |
3.90e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 3.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511184 160 SGGQKQRLALARALSLDPEFILLDEPTSALDvsvqAQVLNLLEE-IQEKLGlTFVFITH 217
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQfLHDYPG-TVVAVTH 218
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-203 |
4.18e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.76 E-value: 4.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663511184 139 ADVLDSVGLKREHMNRFpHEFSGGQKQRLA-LARALSL------------DPEFILLDEPTSALDVSVQAQVLNLLEE 203
Cdd:pfam13558 14 VEVRDEDGSEVETYRRS-GGLSGGEKQLLAyLPLAAALaaqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
160-236 |
1.29e-03 |
|
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: 40.80 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 160 SGGQKQ------RLALARALSLDPEFILLDEPTSALDVS-VQAQVLNLLEEIQEK---LGLTFVFITHALNVVNHI--SD 227
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDREnIESLAHALVEIIKSRsqqRNFQLLVITHDEDFVELLgrSE 1280
|
90
....*....|
gi 663511184 228 RVAVMY-LGK 236
Cdd:TIGR00606 1281 YVEKFYrLKK 1290
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
48-126 |
3.37e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 38.52 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511184 48 GETLGIVGESGCGKTTL----------GRVLLGLIPITDGSVLY-DGEDirtiPDRELRRRMQIVFQDPGGSMNPRmsVR 116
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLaldlavavatGRDWLGERRVKQGRVVYlAAED----PRDGLRRRLKAIGAHLGDEDAAL--AE 74
|
90
....*....|
gi 663511184 117 SIVGEPLQVN 126
Cdd:cd01125 75 NLVIENLRGK 84
|
|
|