|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-329 |
0e+00 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 506.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAqGTIDYRGQDLTKLkSNK 87
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITS-GEILFDGEDLLKL-SEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQR 167
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 248 FYDPRHPYTWSLLSSLPQLADDKGELYSIPGTPPSLYSQLQGDAFALRSDYAMEIDFEEKPPQIYVTDTHWAKTWLLHEN 327
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEE 318
|
..
gi 896625925 328 AP 329
Cdd:COG0444 319 AP 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-267 |
1.02e-130 |
|
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: 384.04 E-value: 1.02e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKLkSNK 87
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGL-SER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQR 167
Cdd:COG4172 85 ELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250 260
....*....|....*....|
gi 896625925 248 FYDPRHPYTWSLLSSLPQLA 267
Cdd:COG4172 245 FAAPQHPYTRKLLAAEPRGD 264
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-309 |
9.02e-114 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 333.62 E-value: 9.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKNVILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAqGTIDYRGQDL 80
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG-GSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 81 TKLKsNKDWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQY 160
Cdd:PRK09473 84 LNLP-EKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVE 240
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 241 YGTVEEVFYDPRHPYTWSLLSSLPQLADDKGELYSIPGTPPSLYSQLQGDAFALRSDYAMEIdFEEKPP 309
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEI-CSSAPP 310
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-242 |
1.08e-113 |
|
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: 329.47 E-value: 1.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKsnK 87
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLS--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVdYMNKVGIPDAEKRFNEYPFQYSGGMRQR 167
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-266 |
1.72e-105 |
|
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: 318.77 E-value: 1.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKNVILTARDIVVEFDVRDK-VLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQD 79
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL----RPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 80 LTKLKSnKDWEPIRGvKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPdaEKRFNEYPFQ 159
Cdd:COG1123 329 LTKLSR-RSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
250 260
....*....|....*....|....*..
gi 896625925 240 EYGTVEEVFYDPRHPYTWSLLSSLPQL 266
Cdd:COG1123 485 EDGPTEEVFANPQHPYTRALLAAVPSL 511
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-309 |
9.36e-103 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 305.51 E-value: 9.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKLkSNK 87
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRI-SEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQR 167
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 248 FYDPRHPYTWSLLSSLPQLADDKGELYSIPGTPPSLYSQLQGDAFALRSDYAMEIDFEEKPP 309
Cdd:PRK11022 242 FRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPA 303
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-319 |
5.41e-102 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 303.58 E-value: 5.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEFDVR-------DKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQD 79
Cdd:COG4608 6 PLLEVRDLKKHFPVRgglfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS----GEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 80 LTKLkSNKDWEPIRgVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGI-PDAEKRfneYPF 158
Cdd:COG4608 82 ITGL-SGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 159 QYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 239 VEYGTVEEVFYDPRHPYTWSLLSSLPQLADD--------KGELYSiPGTPPSlysqlqGDAFALRSDYAMEIDFEEKPPQ 310
Cdd:COG4608 237 VEIAPRDELYARPLHPYTQALLSAVPVPDPErrrerivlEGDVPS-PLNPPS------GCRFHTRCPYAQDRCATEEPPL 309
|
....*....
gi 896625925 311 IYVTDTHWA 319
Cdd:COG4608 310 REVGPGHQV 318
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-283 |
2.40e-94 |
|
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: 290.27 E-value: 2.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAqGTIDYRGQDLTKLKsnk 87
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwEPIRGVKIATIFQDPMTSLDPInTIGSQITEVIiKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQR 167
Cdd:COG1123 78 --EALRGRRIGMVFQDPMTQLNPV-TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 896625925 248 FYDPRhpytwsLLSSLPQLADDKGELYSIPGTPPSL 283
Cdd:COG1123 231 LAAPQ------ALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-267 |
1.07e-91 |
|
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: 283.88 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEFDVR-------DKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrvAQGTIDYRGQD 79
Cdd:COG4172 274 PLLEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 80 LTKLkSNKDWEPIRGvKIATIFQDPMTSLDPINTIGSQITEVIIKHQ-KKTPKEAKEMAVDYMNKVGI-PDAEKRfneYP 157
Cdd:COG4172 349 LDGL-SRRALRPLRR-RMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHR---YP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 158 FQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|
gi 896625925 238 IVEYGTVEEVFYDPRHPYTWSLLSSLPQLA 267
Cdd:COG4172 504 VVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-282 |
1.32e-89 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 272.35 E-value: 1.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKNVILTARDIVVEFDVRD---------KVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqG 71
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 72 TIDYRGQDLTKLkSNKDWEPIRGvKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPK-EAKEMAVDYMNKVGI-PDA 149
Cdd:PRK15079 77 EVAWLGKDLLGM-KDDEWRAVRS-DIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRqEVKDRVKAMMLKVGLlPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 150 ekrFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADK 229
Cdd:PRK15079 155 ---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 230 VAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLSSL----PQLADDK------GELYSiPGTPPS 282
Cdd:PRK15079 232 VLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVpipdPDLERNKtiqlleGELPS-PINPPS 293
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-271 |
4.88e-86 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 272.11 E-value: 4.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGT---IDYRGQDLTKL- 83
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmlLRRRSRQVIELs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 84 -KSNKDWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSG 162
Cdd:PRK10261 92 eQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....*....
gi 896625925 243 TVEEVFYDPRHPYTWSLLSSLPQLADDKG 271
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQLGAMKG 280
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-261 |
9.05e-84 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 253.83 E-value: 9.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKLKsnkdwepIRGVKIATIFQDPMT 106
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS-------IRGRHIATIMQNPRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPINTIGSQITEVIIKHQKKTpKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEP 186
Cdd:TIGR02770 74 AFNPLFTMGNHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 187 TTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLS 261
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-266 |
7.96e-83 |
|
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: 251.65 E-value: 7.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksnKD 88
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLE----RPWSGEVTFDGRPVTR----RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEPIRGvKIATIFQDPMTSLDPINTIGSQITEVIiKHQKKTpkEAKEMAVDYMNKVGIPDAEkRFNeYPFQYSGGMRQRI 168
Cdd:COG1124 74 RKAFRR-RVQMVFQDPYASLHPRHTVDRILAEPL-RIHGLP--DREERIAELLEQVGLPPSF-LDR-YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 169 VIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*...
gi 896625925 249 YDPRHPYTWSLLSSLPQL 266
Cdd:COG1124 228 AGPKHPYTRELLAASLAF 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-309 |
2.03e-81 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 251.04 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEFDVR------DKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTgMLEENgrvAQGTIDYRGQDL 80
Cdd:PRK11308 4 PLLQAIDLKKHYPVKrglfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETP---TGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 81 tkLKSNKDWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGI-PDAEKRfneYPFQ 159
Cdd:PRK11308 80 --LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 240 EYGTVEEVFYDPRHPYTWSLLSSLPQLADD--------KGELYSiPGTPPSlysqlqGDAFALRSDYAMEIDFEEKPP 309
Cdd:PRK11308 235 EKGTKEQIFNNPRHPYTQALLSATPRLNPDdrreriklTGELPS-PLNPPP------GCAFNARCPRAFGRCRQEQPQ 305
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
8-283 |
1.64e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 246.36 E-value: 1.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKLkSNK 87
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKL-SPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTP-----KEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSG 162
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 896625925 243 TVEEVFYDPRHPYTWSLLSSLPQLADD---KGELYSIPGTPPSL 283
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPL 285
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-265 |
8.47e-78 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 248.08 E-value: 8.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRV-AQGTIDYRGQDLTKlKSN 86
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLH-ASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KDWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQ 166
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250
....*....|....*....
gi 896625925 247 VFYDPRHPYTWSLLSSLPQ 265
Cdd:PRK15134 244 LFSAPTHPYTQKLLNSEPS 262
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-263 |
2.64e-64 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 205.05 E-value: 2.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKNVILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRG--- 77
Cdd:COG4107 1 MTNEEQPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLA----PTSGSVYYRDrdg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 78 --QDLTKLKS-------NKDWepirGVkiatIFQDPMTSLDPINTIGSQITEVII----KHQKKTPKEAKemavDYMNKV 144
Cdd:COG4107 77 gpRDLFALSEaerrrlrRTDW----GM----VYQNPRDGLRMDVSAGGNIAERLMaageRHYGDIRARAL----EWLERV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 145 GIPDAekRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVA 224
Cdd:COG4107 145 EIPLE--RIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIR 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 896625925 225 SIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLSSL 263
Cdd:COG4107 223 LLADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-262 |
1.96e-63 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 202.62 E-value: 1.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEfdvRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKlksnkd 88
Cdd:PRK10418 5 IELRNIALQ---AAQPL--VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIiKHQKKTPKEAKEMAVdyMNKVGIPDAEKRFNEYPFQYSGGMRQRI 168
Cdd:PRK10418 74 -CALRGRKIATIMQNPRSAFNPLHTMHTHARETC-LALGKPADDATLTAA--LEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 169 VIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....
gi 896625925 249 YDPRHPYTWSLLSS 262
Cdd:PRK10418 230 NAPKHAVTRSLVSA 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-318 |
9.23e-63 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 203.11 E-value: 9.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKLkSNK 87
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRL-SPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTP-----KEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSG 162
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIKDHKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 243 TVEEVFYDPRHPYTWSLLSSLPQLADD---KGELYSIPGTPPSLYSQLQGDAFALRSDYAMEIDFEEkpPQIYVTDTHW 318
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET--PRLTGAKNHL 318
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-264 |
5.11e-60 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 203.55 E-value: 5.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLT-------AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDL 80
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 81 TKLKSNKdWEPIRGvKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGI-PDAEKRfneYPFQ 159
Cdd:PRK10261 389 DTLSPGK-LQALRR-DIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWR---YPHE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
250 260
....*....|....*....|....*
gi 896625925 240 EYGTVEEVFYDPRHPYTWSLLSSLP 264
Cdd:PRK10261 544 EIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-261 |
3.43e-59 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 199.55 E-value: 3.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKNVILTARDIVVEFDVRDKVL-------TAIRGVSLDLIEGEVLALVGESGSGKSVltktfTGMLEENGRVAQGTI 73
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKST-----TGLALLRLINSQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 74 DYRGQDLTKLkSNKDWEPIRGvKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAV-DYMNKVGIpDAEKR 152
Cdd:PRK15134 343 WFDGQPLHNL-NRRQLLPVRH-RIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQViAVMEEVGL-DPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 153 FnEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAV 232
Cdd:PRK15134 420 H-RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260
....*....|....*....|....*....
gi 896625925 233 MYAGEIVEYGTVEEVFYDPRHPYTWSLLS 261
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-265 |
3.38e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 186.44 E-value: 3.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 12 RDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLKSNKdwep 91
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LE---RPTSGSVLVDGVDLTALSERE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 92 IRGV--KIATIFQD---------------PMtsldpintigsqiteviiKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfn 154
Cdd:COG1135 77 LRAArrKIGMIFQHfnllssrtvaenvalPL------------------EIAGVPKAEIRKRVAELLELVGLSDKADA-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 155 eYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMY 234
Cdd:COG1135 137 -YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260 270
....*....|....*....|....*....|.
gi 896625925 235 AGEIVEYGTVEEVFYDPRHPYTWSLLSSLPQ 265
Cdd:COG1135 216 NGRIVEQGPVLDVFANPQSELTRRFLPTVLN 246
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-252 |
3.20e-54 |
|
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: 178.16 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLkSNK 87
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LE---RPTSGSVLVDGTDLTLL-SGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGvKIATIFQDpmtsldpINTIGSQ-ITEVI-----IKHQKKtpKEAKEMAVDYMNKVGIPDAEKRfneYPFQYS 161
Cdd:cd03258 76 ELRKARR-RIGMIFQH-------FNLLSSRtVFENValpleIAGVPK--AEIEERVLELLELVGLEDKADA---YPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEY 241
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
250
....*....|.
gi 896625925 242 GTVEEVFYDPR 252
Cdd:cd03258 223 GTVEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-255 |
9.08e-54 |
|
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: 177.09 E-value: 9.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFDVRdKVLtaiRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLkS 85
Cdd:COG1127 3 EPMIEVRNLTKSFGDR-VVL---DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL----RPDSGEILVDGQDITGL-S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 86 NKDWEPIRGvKIATIFQ-----DPMTSLD----PIntigsqiteviIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneY 156
Cdd:COG1127 74 EKELYELRR-RIGMLFQggalfDSLTVFEnvafPL-----------REHTDLSEAEIRELVLEKLELVGLPGAADK---M 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 157 PFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAG 236
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250
....*....|....*....
gi 896625925 237 EIVEYGTVEEVFyDPRHPY 255
Cdd:COG1127 219 KIIAEGTPEELL-ASDDPW 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
25-254 |
1.09e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 171.72 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLTKlkSNKDWEPIRGvKIATIFQD- 103
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEE---PDSGTITVDGEDLTD--SKKDINKLRR-KVGMVFQQf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 ---P-MTSLDpiNtigsqITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:COG1126 87 nlfPhLTVLE--N-----VTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHP 254
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-265 |
1.60e-51 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 171.65 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNK 87
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARL----APDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRGVKIAT----IFQDPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPdaEKRFNEYPFQYSGG 163
Cdd:PRK11701 78 LSEAERRRLLRTewgfVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEID--AARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGT 243
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250 260
....*....|....*....|..
gi 896625925 244 VEEVFYDPRHPYTWSLLSSLPQ 265
Cdd:PRK11701 236 TDQVLDDPQHPYTQLLVSSVLQ 257
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-238 |
2.85e-51 |
|
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: 169.98 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLkSNKD 88
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLD----RPTSGEVRVDGTDISKL-SEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEPIRGVKIATIFQDP-----MTSLDPIntigsqitEVIIKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGG 163
Cdd:cd03255 76 LAAFRRRHIGFVFQSFnllpdLTALENV--------ELPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLgVVASIADKVAVMYAGEI 238
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-255 |
1.99e-50 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 168.06 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 12 RDIVVEFDVRdKVLtaiRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLkSNKDWEP 91
Cdd:cd03261 4 RGLTKSFGGR-TVL---KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL----RPDSGEVLIDGEDISGL-SEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 92 IRgVKIATIFQDP--MTSLDPINTIGSQITEviikHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIV 169
Cdd:cd03261 75 LR-RRMGMLFQSGalFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 170 IAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFy 249
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR- 225
|
....*.
gi 896625925 250 DPRHPY 255
Cdd:cd03261 226 ASDDPL 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
27-263 |
2.03e-49 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 166.16 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSNKDWEPIRGVKIAT----IFQ 102
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLA----PDHGTATYIMRSGAELELYQLSEAERRRLMRTewgfVHQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 DPMTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAekRFNEYPFQYSGGMRQRIVIAIALACRPDILI 182
Cdd:TIGR02323 94 NPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPT--RIDDLPRAFSGGMQQRLQIARNLVTRPRLVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLSS 262
Cdd:TIGR02323 172 MDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSS 251
|
.
gi 896625925 263 L 263
Cdd:TIGR02323 252 I 252
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
26-252 |
2.31e-49 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 165.20 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksnKDWEPIRGvKIATIFQDPm 105
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL----KPTSGEVLVDGKDITK----KNLRELRR-KVGLVFQNP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tslDpintigSQITEVII--------KHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACR 177
Cdd:COG1122 85 ---D------DQLFAPTVeedvafgpENLGLPREEIRERVEEALELVGLEHLADR---PPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPR 252
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-240 |
1.87e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.91 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKS----VLtktftGMLEengRVAQGTIDYRGQDLT 81
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllnIL-----GGLD---RPTSGEVLIDGQDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 82 KLkSNKDWEPIRGVKIATIFQDP-----MTSLDPIntigsqitEVIIKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEY 156
Cdd:COG1136 74 SL-SERELARLRRRHIGFVFQFFnllpeLTALENV--------ALPLLLAGVSRKERRERARELLERVGLGD---RLDHR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 157 PFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLgVVASIADKVAVMYAG 236
Cdd:COG1136 142 PSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDG 220
|
....
gi 896625925 237 EIVE 240
Cdd:COG1136 221 RIVS 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-255 |
4.91e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.66 E-value: 4.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLKSNK 87
Cdd:COG3842 5 ALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FE---TPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwepiRGvkIATIFQD----P-MTSLDpiNtigsqitevI---IKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQ 159
Cdd:COG3842 77 -----RN--VGMVFQDyalfPhLTVAE--N---------VafgLRMRGVPKAEIRARVAELLELVGLEGLADR---YPHQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
250
....*....|....*.
gi 896625925 240 EYGTVEEVFYDPRHPY 255
Cdd:COG3842 216 QVGTPEEIYERPATRF 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-266 |
1.03e-47 |
|
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: 162.28 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLKSNKDWEPIRGVKIatIFQDP 104
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LE---KPAQGTVSFRGQDLYQLDRKQRRAFRRDVQL--VFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfnEYPFQYSGGMRQRIVIAIALACRPDILICD 184
Cdd:TIGR02769 98 PSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDAD--KLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 185 EPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFyDPRHPYTWSLLSS-L 263
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL-SFKHPAGRNLQSAvL 254
|
...
gi 896625925 264 PQL 266
Cdd:TIGR02769 255 PEH 257
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-246 |
5.10e-47 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 160.62 E-value: 5.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLKSnKDWEPIRGvKIATIFQDP 104
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LE---SPSQGNVSWRGEPLAKLNR-AQRKAFRR-DIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLDPINTIGSQITEVIiKHQKKTPKEAKEMAVDYM-NKVGIPD--AEKRfneyPFQYSGGMRQRIVIAIALACRPDIL 181
Cdd:PRK10419 99 ISAVNPRKTVREIIREPL-RHLLSLDKAERLARASEMlRAVDLDDsvLDKR----PPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 182 ICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-262 |
1.61e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 161.12 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 18 FDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTgMLEE--NGRVaqgTIDyrGQDLTKLkSNKDWEPIRGv 95
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCIN-LLERptSGRV---LVD--GQDLTAL-SEKELRKARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 96 KIATIFQD---------------PMTsLDpintigsqiteviikhqkKTPKEAKEMAVD-YMNKVGIpdAEKRfNEYPFQ 159
Cdd:PRK11153 83 QIGMIFQHfnllssrtvfdnvalPLE-LA------------------GTPKAEIKARVTeLLELVGL--SDKA-DRYPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250 260
....*....|....*....|...
gi 896625925 240 EYGTVEEVFYDPRHPYTWSLLSS 262
Cdd:PRK11153 221 EQGTVSEVFSHPKHPLTREFIQS 243
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-233 |
6.18e-46 |
|
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: 156.09 E-value: 6.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGqdltklksnkd 88
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE----RPTSGEVLVDG----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wEPIRGV--KIATIFQDP-----MTSLDPInTIGsqiteviIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYS 161
Cdd:cd03293 66 -EPVTGPgpDRGYVFQQDallpwLTVLDNV-ALG-------LELQGVPKAEARERAEELLELVGLSGFENA---YPHQLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVM 233
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-237 |
1.39e-45 |
|
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: 154.93 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKdwepiRGV 95
Cdd:cd03225 5 LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT----SGEVLVDGKDLTKLSLKE-----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 96 KIATIFQDPMTSLdpintIGSQITEVII---KHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAI 172
Cdd:cd03225 76 KVGLVFQNPDDQF-----FGPTVEEEVAfglENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 173 ALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-247 |
8.58e-45 |
|
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: 153.49 E-value: 8.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEN-GRVAQGTIDYRGQDLTKLKSNK 87
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPIRgvkIATIFQDP----MTSLDPInTIGSQIteviikHQKKTPKEAKEMAVDYMNKVGIPDAEKRfNEYPFQYSGG 163
Cdd:cd03260 77 LELRRR---VGMVFQKPnpfpGSIYDNV-AYGLRL------HGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYAGEIVEYGT 243
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
....
gi 896625925 244 VEEV 247
Cdd:cd03260 224 TEQI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-255 |
1.43e-43 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 151.64 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLkSNKDWEPIRGVKIATIFQD--- 103
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS----GKVLIDGQDIAAM-SRKELRELRRKKISMVFQSfal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 -P-MTSLDPInTIGSQIteviikhQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDIL 181
Cdd:cd03294 114 lPhRTVLENV-AFGLEV-------QGVPRAEREERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 182 ICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPY 255
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-262 |
2.60e-43 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 150.71 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 21 RDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE--------ENGRVAQGTIDYRGQdltklksnkdwepi 92
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEptsgelliDDHPLHFGDYSYRSQ-------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 93 rgvKIATIFQDPMTSLDPINTIGsQITEVIIKHQKKTPKEAKEMAV-DYMNKVGI-PDaekRFNEYPFQYSGGMRQRIVI 170
Cdd:PRK15112 88 ---RIRMIFQDPSTSLNPRQRIS-QILDFPLRLNTDLEPEQREKQIiETLRQVGLlPD---HASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 171 AIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|..
gi 896625925 251 PRHPYTWSLLSS 262
Cdd:PRK15112 241 PLHELTKRLIAG 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-240 |
3.25e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.24 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKnVILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDL 80
Cdd:COG1116 1 MSAAA-PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLE----KPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 81 TKLksnkdwEPIRGVkiatIFQDP-----MTSLDPIntigsqitEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfne 155
Cdd:COG1116 76 TGP------GPDRGV----VFQEPallpwLTVLDNV--------ALGLELRGVPKAERRERARELLELVGLAGFEDA--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 156 YPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYA 235
Cdd:COG1116 135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA 214
|
....*..
gi 896625925 236 --GEIVE 240
Cdd:COG1116 215 rpGRIVE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
26-247 |
3.54e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 3.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksnkDWEPIRGvKIATIFQDPm 105
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL----RPTSGEVRVLGEDVAR-----DPAEVRR-RIGYVPQEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tSLDPINTiGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:COG1131 83 -ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGLTDAADR---KVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYefTTIFI-THDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEG--KTVLLsTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
1.56e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKnvILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDL 80
Cdd:COG1121 1 MMMMP--AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL----PPTSGTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 81 TKLKSnkdwepirgvKIATIFQdpMTSLDPintiGSQIT--EVI----IKHQ---KKTPKEAKEMAVDYMNKVGIPD-AE 150
Cdd:COG1121 71 RRARR----------RIGYVPQ--RAEVDW----DFPITvrDVVlmgrYGRRglfRRPSRADREAVDEALERVGLEDlAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 151 KRFNEYpfqySGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKV 230
Cdd:COG1121 135 RPIGEL----SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRV 209
|
250
....*....|....*...
gi 896625925 231 AVMyAGEIVEYGTVEEVF 248
Cdd:COG1121 210 LLL-NRGLVAHGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-188 |
1.65e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 142.40 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksnkDWEPIRGVKIATIFQDPmtS 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL----SPTEGTILLDGQDLTD-----DERKSLRKEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LDPINTIGSQITEV-IIKHQKKTPKEAKemAVDYMNKVGIPDAEKRF-NEYPFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:pfam00005 70 LFPRLTVRENLRLGlLLKGLSKREKDAR--AEEALEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 896625925 186 PTT 188
Cdd:pfam00005 148 PTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-251 |
1.81e-41 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 144.79 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKdwepiRGvkIATIFQDpmTS 107
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS----GKILLNGKDITNLPPEK-----RD--ISYVPQN--YA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LDPINTIGSQItEVIIKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPT 187
Cdd:cd03299 82 LFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 188 TALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
26-242 |
3.85e-41 |
|
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: 143.43 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLksnkdwePIRGVKIATIFQDP- 104
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-LE---RPDSGEILIDGRDVTGV-------PPERRNIGMVFQDYa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 ----MTSLDPInTIGsqiteviIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:cd03259 83 lfphLTVAENI-AFG-------LKLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-238 |
4.88e-41 |
|
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: 143.05 E-value: 4.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLTKLKsnKDWEPIRGvKIATIFQD- 103
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-LEE---PDSGTIIIDGLKLTDDK--KNINELRQ-KVGMVFQQf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 ---P-MTSLDpintigsQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:cd03262 86 nlfPhLTVLE-------NITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-248 |
8.00e-41 |
|
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: 143.65 E-value: 8.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNK 87
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL----KPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwepiRGVKIATIFQDPMTSLDpintigsqIT--EVI----IKHQK---KTPKEAKEMAVDYMNKVGIPD-AEKRFNEYp 157
Cdd:COG1120 73 -----LARRIAYVPQEPPAPFG--------LTvrELValgrYPHLGlfgRPSAEDREAVEEALERTGLEHlADRPVDEL- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 158 fqySGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:COG1120 139 ---SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
250
....*....|.
gi 896625925 238 IVEYGTVEEVF 248
Cdd:COG1120 216 IVAQGPPEEVL 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-260 |
2.32e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.29 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTklkSNKd 88
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LE---TPDSGRIVLNGRDLF---TNL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wePIRGVKIATIFQDP-----MTSLDPInTIGsqiteviIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGG 163
Cdd:COG1118 71 --PPRERRVGFVFQHYalfphMTVAENI-AFG-------LRVRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGT 243
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
250
....*....|....*..
gi 896625925 244 VEEVFYDPRHPYTWSLL 260
Cdd:COG1118 218 PDEVYDRPATPFVARFL 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-256 |
3.31e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 142.10 E-value: 3.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGM--LEENGRVaQGTIDYRGQDLtklkSNKDWEPI---RgvKIATIF 101
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGARV-EGEILLDGEDI----YDPDVDVVelrR--RVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDP----MTSLDPInTIGSQIteviikHQKKTPKEAKEMAVDYMNKVGIPDAEK-RFNEYPFQYSGGMRQRIVIAIALAC 176
Cdd:COG1117 99 QKPnpfpKSIYDNV-AYGLRL------HGIKSKSELDEIVEESLRKAALWDEVKdRLKKSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYT 256
Cdd:COG1117 172 EPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-255 |
7.72e-40 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 144.02 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVrdkvLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEENGRvaqGTIDYRGQDLTKLKSNKd 88
Cdd:TIGR03265 5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAG-LERQTA---GTIYQGGRDITRLPPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wepiRGVKIatIFQDpmTSLDPINTIGSQItEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRI 168
Cdd:TIGR03265 76 ----RDYGI--VFQS--YALFPNLTVADNI-AYGLKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 169 VIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:TIGR03265 144 ALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
....*..
gi 896625925 249 YDPRHPY 255
Cdd:TIGR03265 224 RHPATPF 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-254 |
6.22e-39 |
|
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: 138.59 E-value: 6.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDYRGQDLTKLKSnkdwepirgvKIATIFQDp 104
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVELRR----------KIGYVIQQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 mTSLDPINTIGSQITEVIiKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfNEYPFQYSGGMRQRIVIAIALACRPDILICD 184
Cdd:cd03295 84 -IGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAEFA-DRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 185 EPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFydpRHP 254
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL---RSP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
26-237 |
2.80e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 134.62 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLksNKDWEPIRGvKIATIFQDPm 105
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLTDL--EDELPPLRR-RIGMVFQDF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tSLDPINTIGSQITEVIikhqkktpkeakemavdymnkvgipdaekrfneypfqySGGMRQRIVIAIALACRPDILICDE 185
Cdd:cd03229 86 -ALFPHLTVLENIALGL--------------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-240 |
5.29e-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: 135.64 E-value: 5.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKNVILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDL 80
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LD---RPTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 81 TKLksnkDWEP---IRGVKIATIFQD----P-MTSLD----PINTIGSqiteviikhqkktpKEAKEMAVDYMNKVGIpd 148
Cdd:COG4181 77 FAL----DEDArarLRARHVGFVFQSfqllPtLTALEnvmlPLELAGR--------------RDARARARALLERVGL-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 149 aEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGvVASIAD 228
Cdd:COG4181 137 -GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCD 214
|
250
....*....|..
gi 896625925 229 KVAVMYAGEIVE 240
Cdd:COG4181 215 RVLRLRAGRLVE 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-260 |
9.86e-38 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 135.16 E-value: 9.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLksnkdwePIRGVKIATIFQD-- 103
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LE---RPDSGTILFGGEDATDV-------PVQERNVGFVFQHya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 ---PMTSLDPInTIGSQIteviiKHQKKTPKEA--KEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRP 178
Cdd:cd03296 85 lfrHMTVFDNV-AFGLRV-----KPRSERPPEAeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWS 258
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
..
gi 896625925 259 LL 260
Cdd:cd03296 236 FL 237
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-242 |
1.15e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 133.33 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKsnkdwepirgv 95
Cdd:cd03214 5 LSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----KPSSGEILLDGKDLASLS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 96 kiatifqdpmtsldpintigsqiteviikhqkktPKE-AKEMAV--DYMNKVGIPD-AEKRFNEYpfqySGGMRQRIVIA 171
Cdd:cd03214 68 ----------------------------------PKElARKIAYvpQALELLGLAHlADRPFNEL----SGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 172 IALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
26-260 |
1.97e-37 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 134.54 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLksnkdwePIRGVKIATIFQDpm 105
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPD----SGRIRLNGQDATRV-------HARDRKIGFVFQH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDPINTIGSQITeVIIKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:TIGR00968 81 YALFKHLTVRDNIA-FGLEIRKHPKAKIKARVEELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLL 260
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
18-254 |
2.81e-36 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 134.24 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 18 FDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTfTGMLEengRVAQGTIDYRGQDLTKLkSNKDWEPIRGvKI 97
Cdd:TIGR02314 11 FHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLE---RPTSGSVIVDGQDLTTL-SNSELTKARR-QI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 98 ATIFQ--DPMTSLDPINTIGSQIteviikHQKKTPKEAKEMAV-DYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIAL 174
Cdd:TIGR02314 85 GMIFQhfNLLSSRTVFGNVALPL------ELDNTPKDEIKRKVtELLALVGLGD---KHDSYPSNLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHP 254
Cdd:TIGR02314 156 ASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTP 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-252 |
1.75e-35 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 129.09 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVrdkvLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKD 88
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL----RPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEpiRGV----KIATIFQDpMTSLDPInTIGSQITE---VIIKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYS 161
Cdd:cd03219 73 AR--LGIgrtfQIPRLFPE-LTVLENV-MVAAQARTgsgLLLARARREEREARERAEELLERVGLAD---LADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEY 241
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|.
gi 896625925 242 GTVEEVFYDPR 252
Cdd:cd03219 225 GTPDEVRNNPR 235
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-240 |
2.14e-35 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 128.62 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleenGRVAQGTIDYRGQDLTKLKSNK 87
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL----DNPTSGEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEpIRGVKIATIFQDPMTSLDpINTIGSQITEVIIKHQKKtpKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQR 167
Cdd:TIGR02211 77 RAK-LRNKKLGFIYQFHHLLPD-FTALENVAMPLLIGKKSV--KEAKERAYEMLEKVGL---EHRINHRPSELSGGERQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIaDKVAVMYAGEIVE 240
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
26-247 |
2.32e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 129.22 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKdwepIRGV--KIATIFQD 103
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS----GSVLIDGTDINKLKGKA----LRQLrrQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PmtsldpiNTIGSQ--ITEVII-----KHQKKT-----PKEAKEMAVDYMNKVGIPD-AEKRFNeypfQYSGGMRQRIVI 170
Cdd:cd03256 87 F-------NLIERLsvLENVLSgrlgrRSTWRSlfglfPKEEKQRALAALERVGLLDkAYQRAD----QLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 171 AIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
26-251 |
3.94e-35 |
|
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: 128.12 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLTKLKSNKdwepiRGVKiaTIFQDpm 105
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-FET---PTSGEILLDGKDITNLPPHK-----RPVN--TVFQN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDPINTIGSQITeVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:cd03300 81 YALFPHLTVFENIA-FGLRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-256 |
5.01e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 128.42 E-value: 5.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE--ENGRVaQGTIDYRGQDLTklksNKDWEPIR-GVKIATIFQDP 104
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEARV-EGEVRLFGRNIY----SPDVDPIEvRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 -----MTSLDPInTIGSQITEVIikhqkKTPKEAKEMAVDYMNKVGIPDAEK-RFNEYPFQYSGGMRQRIVIAIALACRP 178
Cdd:PRK14267 95 npfphLTIYDNV-AIGVKLNGLV-----KSKKELDERVEWALKKAALWDEVKdRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYT 256
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-251 |
6.11e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 130.97 E-value: 6.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 21 RDKVLTAIrgvSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSnkdwepiRGVKIATI 100
Cdd:PRK10851 14 RTQVLNDI---SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTS----GHIRFHGTDVSRLHA-------RDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 101 FQD-----PMTSLDpinTIGSQITeVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALA 175
Cdd:PRK10851 80 FQHyalfrHMTVFD---NIAFGLT-VLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
31-251 |
1.36e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 128.41 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFQDPMTSLDP 110
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPETGNKNLKKLRK-KVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 111 iNTIGSQItEVIIKHQKKTPKEAKEMAVDYMNKVGIPdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTAL 190
Cdd:PRK13641 101 -NTVLKDV-EFGPKNFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 191 DVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-240 |
1.56e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.32 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKdwepIRGV--KIATIFQD 103
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE----RPTSGQVLVNGQDLSRLKRRE----IPYLrrRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 ---------------PMtsldpintigsqitEVIikhqKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRI 168
Cdd:COG2884 88 frllpdrtvyenvalPL--------------RVT----GKSRKEIRRRVREVLDLVGLSDKAKA---LPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 169 VIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFI-THDLGVVASIADKVAVMYAGEIVE 240
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIaTHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-242 |
3.51e-34 |
|
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: 124.95 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 13 DIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKL--------- 83
Cdd:cd03235 4 DLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL----KPTSGSIRVFGKPLEKErkrigyvpq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 84 KSNKDWE-PIrgvkiaTIFQDPMTSLDPIntigsqiteviIKHQKKTPKEAKEMAVDYMNKVGIPD-AEKRFNEYpfqyS 161
Cdd:cd03235 76 RRSIDRDfPI------SVRDVVLMGLYGH-----------KGLFRRLSKADKAKVDEALERVGLSElADRQIGEL----S 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMyAGEIVEY 241
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVAS 212
|
.
gi 896625925 242 G 242
Cdd:cd03235 213 G 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-261 |
4.96e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.02 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTgMLE--ENGRVAQG--TIDyRGQDLTKLKSNkdwepIRGVK--IAT 99
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEqpEAGTIRVGdiTID-TARSLSQQKGL-----IRQLRqhVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 100 IFQDpmTSLDPINTIGSQITE--VIIKhqkKTPKE-AKEMAVDYMNKVGIPDAEkrfNEYPFQYSGGMRQRIVIAIALAC 176
Cdd:PRK11264 90 VFQN--FNLFPHRTVLENIIEgpVIVK---GEPKEeATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYT 256
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*
gi 896625925 257 WSLLS 261
Cdd:PRK11264 241 RQFLE 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
26-238 |
7.06e-34 |
|
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: 122.89 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLtklksNKDWEPIRGvKIATIFQDPM 105
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS----GEIKVLGKDI-----KKEPEEVKR-RIGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TsldpintigsqiteviikHQKKTPKEAkemavdymnkvgipdaekrfneypFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:cd03230 84 L------------------YENLTVREN------------------------LKLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYefTTIFI-THDLGVVASIADKVAVMYAGEI 238
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEG--KTILLsSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-237 |
1.58e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.58 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKdwepirgvkiatifqdpm 105
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEE------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tsldpintigsqiteviikhqkktpkeakemavdYMNKVGipdaekrfneYPFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:cd00267 71 ----------------------------------LRRRIG----------YVPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-248 |
2.55e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.77 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSN-KDwepIRGvKIATIFQDPM 105
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT----SGKIIIDGVDITDKKVKlSD---IRK-KVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLdpintigsqITEVIIKHQKKTPK-------EAKEMAVDYMNKVGIpDAEKRFNEYPFQYSGGMRQRIVIAIALACRP 178
Cdd:PRK13637 94 YQL---------FEETIEKDIAFGPInlglseeEIENRVKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-255 |
5.42e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 126.69 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLkSNKDWEPIRGVKIATIFQD--- 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT----RGQVLIDGVDIAKI-SDAELREVRRKKIAMVFQSfal 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 --PMTSLDpiNT-IGSQITEViikhqkkTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:PRK10070 118 mpHMTVLD--NTaFGMELAGI-------NAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPY 255
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
26-253 |
1.23e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLTKLKSNKdwepiRGvkIATIFQDP- 104
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LED---PTSGEILIGGRDVTDLPPKD-----RN--IAMVFQSYa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 ----MTSLDpiNtIGS--QIteviikhqKKTPKEAKEMAVDYMNK-VGIPDAEKRfneYPFQYSGGMRQRIVIAIALACR 177
Cdd:COG3839 86 lyphMTVYE--N-IAFplKL--------RKVPKAEIDRRVREAAElLGLEDLLDR---KPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLgVVA-SIADKVAVMYAGEIVEYGTVEEVFYDPRH 253
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ-VEAmTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-246 |
1.26e-32 |
|
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: 121.32 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksnkdwEPiRGVK--IATIFQD 103
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL----KPTSGRATVAGHDVVR-------EP-REVRrrIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PmtSLDPINTiGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYpfqYSGGMRQRIVIAIALACRPDILIC 183
Cdd:cd03265 82 L--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 184 DEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-247 |
1.34e-32 |
|
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: 121.89 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksnkD 88
Cdd:COG4555 2 IEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL----KPDSGSILIDGEDVRK-----E 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEPIRGvKIATIFQDPMtsLDPINTIGSQItEVIIKHQKKTPKEAKEMAVDYMNKVGIPD-AEKRFNEYpfqySGGMRQR 167
Cdd:COG4555 69 PREARR-QIGVLPDERG--LYDRLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEEfLDRRVGEL----STGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-276 |
3.11e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.20 E-value: 3.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFQDPMT 106
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDITITHKTKDKYIRPVRK-RIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPiNTIGSQItEVIIKHQKKTPKEAKEMAVDYMNKVGIPdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEP 186
Cdd:PRK13646 97 QLFE-DTVEREI-IFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 187 TTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSL-LSSLPQ 265
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIgLPEIVQ 252
|
250
....*....|.
gi 896625925 266 LADDKGELYSI 276
Cdd:PRK13646 253 LQYDFEQKYQT 263
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-238 |
3.37e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.92 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIvvEFDVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTklksnkD 88
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLD----PPTSGEIYLDGKPLS------A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEPI--RGvKIATIFQDP-MTSldpiNTIGSQITEV-IIKHQKKTPKEAKEMavdyMNKVGIPDA--EKRFNEYpfqySG 162
Cdd:COG4619 67 MPPPewRR-QVAYVPQEPaLWG----GTVRDNLPFPfQLRERKFDRERALEL----LERLGLPPDilDKPVERL----SG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
28-261 |
4.42e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 4.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTgMLEengRVAQGTIDYRGQDLT---------KLKSNKDWEPIRgVKIA 98
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-FLE---KPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLLR-TRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 99 TIFQ-----DPMTSLDpintigsQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKrfNEYPFQYSGGMRQRIVIAIA 173
Cdd:PRK10619 96 MVFQhfnlwSHMTVLE-------NVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 174 LACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRH 253
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*...
gi 896625925 254 PYTWSLLS 261
Cdd:PRK10619 246 PRLQQFLK 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-250 |
9.08e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKdwepIRGv 95
Cdd:PRK13632 13 VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ----SGEIKIDGITISKENLKE----IRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 96 KIATIFQDPMTSLdpintIGSQITEVI---IKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAI 172
Cdd:PRK13632 84 KIGIIFQNPDNQF-----IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGMEDYLDK---EPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 173 ALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGvVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-251 |
1.01e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.90 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFQDPMT 106
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT----SGTVTIGERVITAGKKNKKLKPLRK-KVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SL-----------DPINTIGSQiteviikhqkktpKEAKEMAVDYMNKVGIPdaEKRFNEYPFQYSGGMRQRIVIAIALA 175
Cdd:PRK13634 97 QLfeetvekdicfGPMNFGVSE-------------EDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-256 |
1.16e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 119.50 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEknvILTARDIVVEFDVRDkvltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVA-QGTIDYRGQD 79
Cdd:PRK14239 1 MTEP---ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTiTGSIVYNGHN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 80 LtkLKSNKDWEPIRGvKIATIFQDP----MTSLDpiNTI-GSQITEViikHQKKTPKEAKEMAvdyMNKVGIPDAEK-RF 153
Cdd:PRK14239 74 I--YSPRTDTVDLRK-EIGMVFQQPnpfpMSIYE--NVVyGLRLKGI---KDKQVLDEAVEKS---LKGASIWDEVKdRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 154 NEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVM 233
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFF 220
|
250 260
....*....|....*....|...
gi 896625925 234 YAGEIVEYGTVEEVFYDPRHPYT 256
Cdd:PRK14239 221 LDGDLIEYNDTKQMFMNPKHKET 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-256 |
1.72e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 119.25 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEF-DVRdkvltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE--ENGRVAqGTIDYRGQDLTKLks 85
Cdd:PRK14247 4 IEIRDLKVSFgQVE-----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEARVS-GEVYLDGQDIFKM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 86 nkDWEPIRGvKIATIFQDPmtslDPINTIgsQITEVIIKHQK-----KTPKEAKEMAVDYMNKVGIPDAEK-RFNEYPFQ 159
Cdd:PRK14247 76 --DVIELRR-RVQMVFQIP----NPIPNL--SIFENVALGLKlnrlvKSKKELQERVRWALEKAQLWDEVKdRLDAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyeFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
250
....*....|....*..
gi 896625925 240 EYGTVEEVFYDPRHPYT 256
Cdd:PRK14247 225 EWGPTREVFTNPRHELT 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-248 |
5.31e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKlksNKDWEpIRGvKIATIFQDPMT 106
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL----LPEAGTITVGGMVLSE---ETVWD-VRR-QVGMVFQNPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLdpintIGSQITEVI---IKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILIC 183
Cdd:PRK13635 93 QF-----VGATVQDDVafgLENIGVPREEMVERVDQALRQVGMEDFLNR---EPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 184 DEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
27-247 |
9.30e-31 |
|
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: 123.02 E-value: 9.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVaqgTIDyrGQDLTKLksNKDWepIRGvKIATIFQDPM 105
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRI---LID--GIDLRQI--DPAS--LRR-QIGVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 ----TSLDPInTIG-SQIT--EVIikhqkktpkEAKEMAvdymnkvGI-PDAEKRfneyPFQY-----------SGGMRQ 166
Cdd:COG2274 560 lfsgTIRENI-TLGdPDATdeEII---------EAARLA-------GLhDFIEAL----PMGYdtvvgeggsnlSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQeyEFTTIFITHDLGVVAsIADKVAVMYAGEIVEYGTVEE 246
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEE 695
|
.
gi 896625925 247 V 247
Cdd:COG2274 696 L 696
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
27-245 |
9.62e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.04 E-value: 9.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTgMLEengrVAQ-GTIDYRGQ--DLTKLKSNKDWEPIRGvKIATIFQD 103
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLE----TPDsGQLNIAGHqfDFSQKPSEKAIRLLRQ-KVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 pmTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDILIC 183
Cdd:COG4161 91 --YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF---PLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 184 DEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVE 245
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
27-246 |
1.22e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 118.26 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKlksnkdwEPiRGVK--IATIFQDP 104
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS----GTARVAGYDVVR-------EP-RKVRrsIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 mtSLDPINTiGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYpfqYSGGMRQRIVIAIALACRPDILICD 184
Cdd:TIGR01188 76 --SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 185 EPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-243 |
3.74e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.11 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTgmLEENGRVAQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFQDpmTSLDP 110
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLN--LLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRR-NVGMVFQQ--YNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 111 INTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDILICDEPTTAL 190
Cdd:PRK11124 96 HLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRF---PLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 896625925 191 DVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGT 243
Cdd:PRK11124 173 DPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-250 |
2.18e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.07 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFQDPMT 106
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT----QGSVRVDDTLITSTSKNKDIKQIRK-KVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLdpintigsqITEVIIKHQKKTP-------KEAKEMAVDYMNKVGIpdAEKRFNEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:PRK13649 97 QL---------FEETVLKDVAFGPqnfgvsqEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-251 |
2.58e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDvrdKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRV--AQGTIDYRGQDLTKLK 84
Cdd:PRK13639 1 ILETRDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVliKGEPIKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 85 SnkdwepirgvKIATIFQDPMTSL-----------DPINtIGSQITEViikhqKKTPKEAkemavdyMNKVGIPDAEKRf 153
Cdd:PRK13639 78 K----------TVGIVFQNPDDQLfaptveedvafGPLN-LGLSKEEV-----EKRVKEA-------LKAVGMEGFENK- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 154 neYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVM 233
Cdd:PRK13639 134 --PPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVM 210
|
250
....*....|....*...
gi 896625925 234 YAGEIVEYGTVEEVFYDP 251
Cdd:PRK13639 211 SDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-251 |
5.10e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.18 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 5 KNVILTARDIVVEFDVR-DKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTID----YRGQD 79
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK----YGTIQvgdiYIGDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 80 LTKLKSNKDWEP--IRGVK-----IATIFQDPMTSLDPiNTIGSQIT--EVIIKHQKKtpkEAKEMAVDYMNKVGIPDAE 150
Cdd:PRK13631 94 KNNHELITNPYSkkIKNFKelrrrVSMVFQFPEYQLFK-DTIEKDIMfgPVALGVKKS---EAKKLAKFYLNKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 151 KRFNeyPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKV 230
Cdd:PRK13631 170 LERS--PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEV 246
|
250 260
....*....|....*....|.
gi 896625925 231 AVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
26-242 |
6.32e-29 |
|
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: 111.19 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLTKLKSNKdwepiRGvkIATIFQD-- 103
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-LEE---PTSGRIYIGGRDVTDLPPKD-----RD--IAMVFQNya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 --P-MTSLDPIntigsqitEVIIKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:cd03301 83 lyPhMTVYDNI--------AFGLKLRKVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-237 |
1.87e-28 |
|
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: 108.62 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLksnkDWEPIRGvKIATIFQDP-- 104
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDL----DLESLRK-NIAYVPQDPfl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 --MTsldpintigsqITEVIIkhqkktpkeakemavdymnkvgipdaekrfneypfqySGGMRQRIVIAIALACRPDILI 182
Cdd:cd03228 88 fsGT-----------IRENIL-------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVAsIADKVAVMYAGE 237
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-307 |
2.06e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKlksNKDWEpIRGvKIATIFQDPMTS 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE----SGQIIIDGDLLTE---ENVWD-IRH-KIGMVFQNPDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LdpintIGSQITEVI---IKHQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILICD 184
Cdd:PRK13650 94 F-----VGATVEDDVafgLENKGIPHEEMKERVNEALELVGMQDFKER---EPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 185 EPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVAsIADKVAVMYAGEIVEYGTVEEVFydprhpytwSLLSSLP 264
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF---------SRGNDLL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 896625925 265 QLADDkgelysIPGTpPSLYSQLQGDAFALRSDYAMEIDFEEK 307
Cdd:PRK13650 236 QLGLD------IPFT-TSLVQSLRQNGYDLPEGYLTEKELEEQ 271
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-242 |
2.78e-28 |
|
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: 109.31 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLiEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDL--TKLKSNKdwePIRGVKIATIFQDpmTSL 108
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLfdSRKKINL---PPQQRKIGLVFQQ--YAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 109 DPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMnkvGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILICDEPTT 188
Cdd:cd03297 87 FPHLNVRENLAFGLKRKRNREDRISVDELLDLL---GLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 896625925 189 ALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-248 |
2.98e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTklksn 86
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGEL----SPDSGEVRLNGRPLA----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 kDWEP-----IRGVkiatifqdpM---TSLD-PINtigsqITEVI----IKHQKkTPKEAKEMAVDYMNKVGIPDAEKRF 153
Cdd:PRK13548 68 -DWSPaelarRRAV---------LpqhSSLSfPFT-----VEEVVamgrAPHGL-SRAEDDALVAAALAQVDLAHLAGRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 154 neYPfQYSGGMRQRIVIAIALA------CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIA 227
Cdd:PRK13548 132 --YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYA 208
|
250 260
....*....|....*....|.
gi 896625925 228 DKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVL 229
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-255 |
5.46e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 110.95 E-value: 5.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVaqgTIDyrGQDLTKLKsnkdwePI---RGvkIATIF 101
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEpTSGRI---LID--GEDIRDLD------PVelrRR--IGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDpmTSLDPINTIGSQITevIIKHQKKTPKEAKEMAVDY-MNKVGIPDAEKRfNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:COG1125 83 QQ--IGLFPHMTVAENIA--TVPRLLGWDKERIRARVDElLELVGLDPEEYR-DRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPY 255
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-256 |
6.08e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.75 E-value: 6.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 20 VRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE--ENGRVAQGTIDYRGQDLTKLKSNKdwepIRGvKI 97
Cdd:PRK14246 20 INDKAI--LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKIKVDGKVLYFGKDIFQIDAIK----LRK-EV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 98 ATIFQDPMTSldPINTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGI-PDAEKRFNEYPFQYSGGMRQRIVIAIALAC 176
Cdd:PRK14246 93 GMVFQQPNPF--PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQeyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYT 256
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-239 |
1.55e-27 |
|
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: 107.34 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 10 TARDIVVEFDVRDKVLtaiRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLtklksnKDW 89
Cdd:cd03226 1 RIENISFSYKKGTEIL---DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGKPI------KAK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 90 EPIRgvKIATIFQDPMTSLDpINTIGSQITEviikhQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIV 169
Cdd:cd03226 68 ERRK--SIGYVMQDVDYQLF-TDSVREELLL-----GLKELDAGNEQAETVLKDLDLYALKER---HPLSLSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 170 IAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-251 |
2.04e-27 |
|
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: 109.89 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 43 LVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKdwepiRGvkIATIFQDpmTSLDPINTIGSQITEVI 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFE----QPDSGSIMLDGEDVTNVPPHL-----RH--INMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 123 ikHQKKTPKEakEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLL 202
Cdd:TIGR01187 68 --KMRKVPRA--EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 896625925 203 KSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-251 |
4.76e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 15 VVEFDVRDK---VLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTgMLEEngrVAQGTIDYRGQDLtkLKSNKDWEP 91
Cdd:PRK09493 1 MIEFKNVSKhfgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN-KLEE---ITSGDLIVDGLKV--NDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 92 IRgVKIATIFQD----P-MTSLD-----PINTIGSqiteviikhqkkTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYS 161
Cdd:PRK09493 75 IR-QEAGMVFQQfylfPhLTALEnvmfgPLRVRGA------------SKEEAEKQARELLAKVGL---AERAHHYPSELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEY 241
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
250
....*....|
gi 896625925 242 GTVEEVFYDP 251
Cdd:PRK09493 218 GDPQVLIKNP 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-246 |
4.98e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.77 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKVLtaiRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLkSNKD 88
Cdd:COG4988 337 IELEDVSFSYPGGRPAL---DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL----PPYSGSILINGVDLSDL-DPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WepiRGvKIATIFQDPmtsldpinTI--GSqITEVIIKHQKKTPKEAKEMAVDymnKVGIPDaekrF-NEYPFQY----- 160
Cdd:COG4988 409 W---RR-QIAWVPQNP--------YLfaGT-IRENLRLGRPDASDEELEAALE---AAGLDE----FvAALPDGLdtplg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 ------SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVAsIADKVAVMY 234
Cdd:COG4988 469 eggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLD 545
|
250
....*....|..
gi 896625925 235 AGEIVEYGTVEE 246
Cdd:COG4988 546 DGRIVEQGTHEE 557
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-239 |
9.13e-27 |
|
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: 104.05 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEF-DVRdkvltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQdltklksnk 87
Cdd:cd03216 1 LELRGITKRFgGVK-----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS----GEILVDGK--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwepirgvkiatifqdpmtsldpintigsqiteviiKHQKKTPKEAKEMavdymnkvGIpdaekrfnEYPFQYSGGMRQR 167
Cdd:cd03216 63 ------------------------------------EVSFASPRDARRA--------GI--------AMVYQLSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-263 |
1.63e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 106.33 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEE-NGRVAQGTIDYRGQDLTKLKSNKDWEPirgvKIATIFQDP 104
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYRYSGDVLLGGRSIFNYRDVLEFRR----RVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 mtslDPIN-TIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEK-RFNEYPFQYSGGMRQRIVIAIALACRPDILI 182
Cdd:PRK14271 111 ----NPFPmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQeyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLSS 262
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
.
gi 896625925 263 L 263
Cdd:PRK14271 265 L 265
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-248 |
1.81e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFDvRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTklkS 85
Cdd:PRK13642 2 NKILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE----FEGKVKIDGELLT---A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 86 NKDWEPIRgvKIATIFQDPMTSLdpintIGSQITEVII--KHQKKTPKEAKEMAVD-YMNKVGIPDAEKRfneYPFQYSG 162
Cdd:PRK13642 74 ENVWNLRR--KIGMVFQNPDNQF-----VGATVEDDVAfgMENQGIPREEMIKRVDeALLAVNMLDFKTR---EPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASiADKVAVMYAGEIVEYG 242
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
....*.
gi 896625925 243 TVEEVF 248
Cdd:PRK13642 223 APSELF 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-253 |
1.87e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 105.24 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleenGRVAQGTIDYRGQDLTklksnkdwEPirGVKIATIFQDpmTS 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL----AQPTSGGVILEGKQIT--------EP--GPDRMVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LDPINTIGSQITEVIIKHQKKTPKEAKEMAVD-YMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILICDEP 186
Cdd:TIGR01184 65 LLPWLTVRENIALAVDRVLPDLSKSERRAIVEeHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 187 TTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV-FYDPRH 253
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-246 |
2.14e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVaqgTIDyrGQDLTKLksnkDWEPIRGvKIATIFQDP- 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDpTSGRI---LID--GVDIRDL----TLESLRR-QIGVVPQDTf 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLdpinTIGSQIT---------EVIikhqkktpkEAKEMAvdymnkvgipDAEKRFNEYPFQY-----------SGGM 164
Cdd:COG1132 425 LFSG----TIRENIRygrpdatdeEVE---------EAAKAA----------QAHEFIEALPDGYdtvvgergvnlSGGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 165 RQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEIVEYGTV 244
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTH 558
|
..
gi 896625925 245 EE 246
Cdd:COG1132 559 EE 560
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-224 |
2.38e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.86 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 22 DKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleENGrvAQGTIDYRGQDLTKLKSNKDWEpIRGVKIATIF 101
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL--DDG--SSGEVSLVGQPLHQMDEEARAK-LRAKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDPMtsLDP-INTIGSQITEVIIKHQKKtpKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:PRK10584 95 QSFM--LIPtLNALENVELPALLRGESS--RQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVA 224
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-251 |
3.44e-26 |
|
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: 107.11 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLtkLKSNKD-WEPIRGVKIATIFQDPmtSLD 109
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAG-LE---RPDSGRIRLGGEVL--QDSARGiFLPPHRRRIGYVFQEA--RLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 110 PintigsqiteviikH----------QKKTPKEAKEMAVDYM-NKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRP 178
Cdd:COG4148 90 P--------------HlsvrgnllygRKRAPRAERRISFDEVvELLGIGHLLDR---RPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-251 |
3.46e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.66 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKlksnkdwEPIRGVK--IATIFQDP 104
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP----TSGSVLIRGEPITK-------ENIREVRkfVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 M-----------TSLDPINTigsQITEVIIKHQKKtpkEAKEMavdymnkVGIPDAEKRFneyPFQYSGGMRQRIVIAIA 173
Cdd:PRK13652 88 DdqifsptveqdIAFGPINL---GLDEETVAHRVS---SALHM-------LGLEELRDRV---PHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 174 LACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-250 |
3.80e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFQDPMT 106
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPT----EGKVTVGDIVVSSTSKQKEIKPVRK-KVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLdpintigsqITEVIIKHQKKTPK-------EAKEMAVDYMNKVGIpdAEKRFNEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:PRK13643 96 QL---------FEETVLKDVAFGPQnfgipkeKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-219 |
4.01e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.94 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSNkd 88
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA----PSSGEITLDGVPVTGPGAD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wepiRGVkiatIFQD----P-MTSLDPInTIGSQIteviikhQKKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQYSGG 163
Cdd:COG4525 78 ----RGV----VFQKdallPwLNVLDNV-AFGLRL-------RGVPKAERRARAEELLALVGLADFARRR---IWQLSGG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHD 219
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-246 |
2.08e-25 |
|
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: 107.16 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLkSNKD 88
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDL-DEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WepiRGVkIATIFQDP---MTSL-------DPintigsQITEviikhqkktpkeakEMAVDYMNKVGIPDAEKRFN---- 154
Cdd:COG4987 407 L---RRR-IAVVPQRPhlfDTTLrenlrlaRP------DATD--------------EELWAALERVGLGDWLAALPdgld 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 155 ----EYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLgVVASIADKV 230
Cdd:COG4987 463 twlgEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRL-AGLERMDRI 539
|
250
....*....|....*.
gi 896625925 231 AVMYAGEIVEYGTVEE 246
Cdd:COG4987 540 LVLEDGRIVEQGTHEE 555
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-233 |
2.93e-25 |
|
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: 101.74 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 23 KVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKtftgMLEENGRVAQGTIDYRGQDltklksnkdwepiRGVKIATIfq 102
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLK----CIYGNYLPDSGSILVRHDG-------------GWVDLAQA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 DPMTSLDpI--NTIG--SQITEVI------------IKHQKKTPKEAKEMAVDYMNKVGIPdaEKRFNEYPFQYSGGMRQ 166
Cdd:COG4778 83 SPREILA-LrrRTIGyvSQFLRVIprvsaldvvaepLLERGVDREEARARARELLARLNLP--ERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIF-ITHDLGVVASIADKVAVM 233
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARG--TAIIgIFHDEEVREAVADRVVDV 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
26-248 |
3.98e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.86 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDlTKLKSNKdWEpIRGvKIATIFQDPm 105
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE----GKVYVDGLD-TSDEENL-WD-IRN-KAGMVFQNP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tslDpiNTIGSQITEVIIKHQKKT----PKEAKEMAVDYMNKVGIPDAEKrfnEYPFQYSGGMRQRIVIAIALACRPDIL 181
Cdd:PRK13633 95 ---D--NQIVATIVEEDVAFGPENlgipPEEIRERVDESLKKVGMYEYRR---HAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 182 ICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-246 |
6.52e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 100.66 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 21 RDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLtklksNKDWEPIRGvKIATI 100
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS----GTAYINGYSI-----RTDRKAARQ-SLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 101 FQ-----DPMTSLDPINTIGsqitevIIKHqkKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALA 175
Cdd:cd03263 81 PQfdalfDELTVREHLRFYA------RLKG--LPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-250 |
6.92e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGT--IDYRGQDLTKLKSNkdwepirgvkIATIFQD 103
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLRES----------VGMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PMTSLdpintIGSQITEVI---IKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:PRK13636 91 PDNQL-----FSASVYQDVsfgAVNLKLPEDEVRKRVDNALKRTGI---EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
30-239 |
7.23e-25 |
|
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: 100.48 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 30 GVSLDLIEGEVLALVGESGSGKSVLTkTFTGMLEengRVAQGTIDYRGQDLTKLkSNKDWEPIRGvKIATIFQ--DPMTS 107
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLL-TLIGGLR---SVQEGSLKVLGQELHGA-SKKQLVQLRR-RIGYIFQahNLLGF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LdpinTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPT 187
Cdd:TIGR02982 97 L----TARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 896625925 188 TALDVTIQAQIIDLLKSLQQEYEFTTIFITHDlGVVASIADKVAVMYAGEIV 239
Cdd:TIGR02982 170 AALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-238 |
8.26e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 100.17 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNKdwEPIRGVKIATIFQDpm 105
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP----TSGTIRVNGQDVSDLRGRA--IPYLRRKIGVVFQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDPINTIGSQIT---EVIikhqKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIALACRPDILI 182
Cdd:cd03292 87 FRLLPDRNVYENVAfalEVT----GVPPREIRKRVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFI-THDLGVVASIADKVAVMYAGEI 238
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAG--TTVVVaTHAKELVDTTRHRVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
26-248 |
1.02e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNKdwepiRGVKIATIFQDPM 105
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP----QSGTVFLGDKPISMLSSRQ-----LARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLdpintiGSQITEVI-------IKHQKKTPKEAKEMAVDYMNKVGIPD-AEKRFNEYpfqySGGMRQRIVIAIALACR 177
Cdd:PRK11231 87 TPE------GITVRELVaygrspwLSLWGRLSAEDNARVNQAMEQTRINHlADRRLTDL----SGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-247 |
2.10e-24 |
|
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: 103.73 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 24 VLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYR-GQDLTKLKSNKDWEPIRGVK-IATIF 101
Cdd:TIGR03269 296 VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEP----TSGEVNVRvGDEWVDMTKPGPDGRGRAKRyIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDpmTSLDPINTIGSQITEVIikhQKKTPKE-AKEMAVDYMNKVGIPD--AEKRFNEYPFQYSGGMRQRIVIAIALACRP 178
Cdd:TIGR03269 372 QE--YDLYPHRTVLDNLTEAI---GLELPDElARMKAVITLKMVGFDEekAEEILDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
27-242 |
2.36e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.80 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGeVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNkdwepIRGVkIATIFQDP-- 104
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS----GTIRIDGQDVLKQPQK-----LRRR-IGYLPQEFgv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 ---MTSLDPINTIGsqitevIIK--HQKKTPKEAKEMavdyMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:cd03264 84 ypnFTVREFLDYIA------WLKgiPSKEVKARVDEV----LELVNLGDRAKK---KIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
38-254 |
2.44e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.44 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 38 GEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNKdwepiRGVKIatIFQD----PMTS------ 107
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPP----DSGRILWNGQDLTALPPAE-----RPVSM--LFQEnnlfPHLTvaqnig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 --LDPintiGSQITEViikhQKKTPKEAKEmavdymnKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:COG3840 94 lgLRP----GLKLTAE----QRAQVEQALE-------RVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHP 254
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-251 |
3.81e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.73 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRV-AQGTIDYRGQDLTKLKSNKDwePIRGvKIATIFQDPmt 106
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrVEGRVEFFNQNIYERRVNLN--RLRR-QVSMVHPKP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPINTIGSQITEVIIKHQKktPKeakeMAVDYMNKVGIPDAE------KRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:PRK14258 98 NLFPMSVYDNVAYGVKIVGWR--PK----LEIDDIVESALKDADlwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYA-----GEIVEYGTVEEVFYDP 251
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-246 |
4.19e-24 |
|
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: 98.84 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLksnkDWEPIRGvKIATIFQDpmTS 107
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD----VSSGSILIDGQDIREV----TLDSLRR-AIGVVPQD--TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LdpIN-TIGSQIteviikhQKKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQY-----------SGGMRQRIVIAIALA 175
Cdd:cd03253 86 L--FNdTIGYNI-------RYGRPDATDEEVIEAAKAAQIHDKIMRF---PDGYdtivgerglklSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 176 CRPDILICDEPTTALDVT----IQAQIIDLLKSLqqeyefTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEE 246
Cdd:cd03253 154 KNPPILLLDEATSALDTHtereIQAALRDVSKGR------TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-220 |
6.28e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.35 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 23 KVLT-AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKDWEpIRGVKIATIF 101
Cdd:PRK11629 19 SVQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS----GDVIFNGQPMSKLSSAAKAE-LRNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QdpMTSLDP-INTIGSQITEVIIKHQKktPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:PRK11629 94 Q--FHHLLPdFTALENVAMPLLIGKKK--PAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDL 220
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-251 |
6.55e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 2 TQEKNVILTARDIVVEFDvrDKvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLT 81
Cdd:PRK09452 8 PSSLSPLVELRGISKSFD--GK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FET---PDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 82 KLKSNKdwepiRGVKiaTIFQD----P-MTSLDPInTIGSQIteviikhqKKTPK-EAKEMAVDYMNKVGIPD-AEKRfn 154
Cdd:PRK09452 80 HVPAEN-----RHVN--TVFQSyalfPhMTVFENV-AFGLRM--------QKTPAaEITPRVMEALRMVQLEEfAQRK-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 155 eyPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMY 234
Cdd:PRK09452 142 --PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMR 219
|
250
....*....|....*..
gi 896625925 235 AGEIVEYGTVEEVFYDP 251
Cdd:PRK09452 220 DGRIEQDGTPREIYEEP 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-273 |
7.91e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 7.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 5 KNVILTARDivVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGML--EENgrvAQGTIDYRGqdlTK 82
Cdd:PRK13640 2 KDNIVEFKH--VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpDDN---PNSKITVDG---IT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 83 LKSNKDWEpIRGvKIATIFQDPMTSLdpintIGSQITEVI---IKHQKKTPKEAKEMAVDYMNKVGIPDAEKrfnEYPFQ 159
Cdd:PRK13640 74 LTAKTVWD-IRE-KVGIVFQNPDNQF-----VGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGMLDYID---SEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGvVASIADKVAVMYAGEIV 239
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 896625925 240 EYGTVEEVFYDPRH--------PYTWSLLS-------SLPQLADDKGEL 273
Cdd:PRK13640 223 AQGSPVEIFSKVEMlkeigldiPFVYKLKNklkekgiSVPQEINTEEKL 271
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-247 |
8.02e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFD-VRdkvltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTkLK 84
Cdd:COG1129 2 EPLLEMRGISKSFGgVK-----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS----GEILLDGEPVR-FR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 85 SNKDwepIRGVKIATIFQDP-----MTSLDPInTIGSQITE-VIIKHqkktpKEAKEMAVDYMNKVGI---PDAEKRfne 155
Cdd:COG1129 72 SPRD---AQAAGIAIIHQELnlvpnLSVAENI-FLGREPRRgGLIDW-----RAMRRRARELLARLGLdidPDTPVG--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 156 ypfQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYA 235
Cdd:COG1129 140 ---DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRD 215
|
250
....*....|..
gi 896625925 236 GEIVEYGTVEEV 247
Cdd:COG1129 216 GRLVGTGPVAEL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-250 |
2.56e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.23 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDK-VLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNK 87
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPD----TGTIEWIFKDEKNKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEP--------------IRGVK-----IATIFQDPMTSLdpintIGSQITEVII---KHQKKTPKEAKEMAVDYMNKVG 145
Cdd:PRK13651 79 EKEKvleklviqktrfkkIKKIKeirrrVGVVFQFAEYQL-----FEQTIEKDIIfgpVSMGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 146 IPdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVAS 225
Cdd:PRK13651 154 LD--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLE 230
|
250 260
....*....|....*....|....*
gi 896625925 226 IADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-263 |
5.41e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLksnk 87
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLSHV---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwePIRGVKIATIFQDpmTSLDPINTIGSQITEVIikHQKKTPK-EAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQ 166
Cdd:PRK11607 87 ---PPYQRPINMMFQS--YALFPHMTVEQNIAFGL--KQDKLPKaEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTI----QAQIIDLLKSLQqeyeFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250 260
....*....|....*....|.
gi 896625925 243 TVEEVFYDPRHPYTWSLLSSL 263
Cdd:PRK11607 233 EPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-247 |
6.28e-23 |
|
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: 95.63 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGM-LEENGRVA-----QGTID---YRGQDLTKLKSN 86
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLvdghdLALADpawLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 kdwepirgVKIATIFQDPMTSLDPintiGSQITEVIikhqkktpkEAKEMAvdymnkvgipDAEKRFNEYPFQY------ 160
Cdd:cd03252 86 --------VLFNRSIRDNIALADP----GMSMERVI---------EAAKLA----------GAHDFISELPEGYdtivge 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 -----SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYA 235
Cdd:cd03252 135 qgaglSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEK 211
|
250
....*....|..
gi 896625925 236 GEIVEYGTVEEV 247
Cdd:cd03252 212 GRIVEQGSHDEL 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-250 |
6.60e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.36 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTklksNKDWEPIRGvKIATIFQDPMTSLdp 110
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK----SGEIFYNNQAIT----DDNFEKLRK-HIGIVFQNPDNQF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 111 intIGSQITEVI---IKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPT 187
Cdd:PRK13648 97 ---VGSIVKYDVafgLENHAVPYDEMHRRVSEALKQVDMLE---RADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 188 TALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLgVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
26-242 |
6.83e-23 |
|
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: 94.59 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSnkDWEPIrGVKI-ATIFQDP 104
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSYQKNIE--ALRRI-GALIeAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLDPINTIGSQItevIIKHqkktpKEAKEMavdyMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRPDILICD 184
Cdd:cd03268 87 LTARENLRLLARLL---GIRK-----KRIDEV----LDVVGLKDSAKKKVK---GFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 185 EPTTALDVTIQAQIIDLLKSLQQEYefTTIFI-THDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQG--ITVLIsSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-247 |
9.09e-23 |
|
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: 94.81 E-value: 9.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKdwepI--RGvkIA---- 98
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL----PPRSGSIRFDGRDITGLPPHE----RarAG--IGyvpe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 99 --TIFQDpMTSLDPInTIGSQIteviikHQKKTPKEAKEMAVDYMnkvgiPDAEKRFNEYPFQYSGGMRQRIVIAIALAC 176
Cdd:cd03224 83 grRIFPE-LTVEENL-LLGAYA------RRRAKRKARLERVYELF-----PRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-238 |
1.05e-22 |
|
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: 93.43 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNkdwepIRGVKIATIFQDpmts 107
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL----RPTSGRVRLDGADISQWDPN-----ELGDHVGYLPQD---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 ldpINTIGSQITEVIIkhqkktpkeakemavdymnkvgipdaekrfneypfqySGGMRQRIVIAIALACRPDILICDEPT 187
Cdd:cd03246 85 ---DELFSGSIAENIL-------------------------------------SGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 896625925 188 TALDVTIQAQIIDLLKSLqQEYEFTTIFITHDLGVVASiADKVAVMYAGEI 238
Cdd:cd03246 125 SHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
27-256 |
3.28e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.46 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGM--LEENGRVaQGTIDYRGQDLtklkSNKDWEPIR-GVKIATIFQD 103
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRV-EGKVTFHGKNL----YAPDVDPVEvRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PmtsldpiNTIGSQITEVI-----IKHQKKTPKEAKEMAvdyMNKVGIPDAEK-RFNEYPFQYSGGMRQRIVIAIALACR 177
Cdd:PRK14243 100 P-------NPFPKSIYDNIaygarINGYKGDMDELVERS---LRQAALWDEVKdKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYA---------GEIVEYGTVEEVF 248
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIF 247
|
....*...
gi 896625925 249 YDPRHPYT 256
Cdd:PRK14243 248 NSPQQQAT 255
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-246 |
7.27e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 92.68 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDYRGQDLTKLKSnkdwepirg 94
Cdd:cd03251 6 VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASLRR--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 95 vKIATIFQDPMTSLDpinTIGSQIT---------EVIikhqkktpkEAKEMA--VDYMNKvgIPDA-EKRFNEYPFQYSG 162
Cdd:cd03251 77 -QIGLVSQDVFLFND---TVAENIAygrpgatreEVE---------EAARAAnaHEFIME--LPEGyDTVIGERGVKLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEIVEYG 242
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
....
gi 896625925 243 TVEE 246
Cdd:cd03251 219 THEE 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-255 |
1.08e-21 |
|
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: 94.41 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSV-------LTKTFTGMLEENGRVAQGTidYRGQDLtklksnkdwePIRGVKIATIFQD 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTlirliagLTRPDEGEIVLNGRTLFDS--RKGIFL----------PPEKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 pmTSLDPINTIGSQI----TEVIIKHQKKTPKEAKEMavdymnkVGIPDAEKRfneYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:TIGR02142 84 --ARLFPHLSVRGNLrygmKRARPSERRISFERVIEL-------LGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPY 255
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-246 |
1.16e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 92.22 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLE-----ENGRVaqgTIDyrGQDLTKLksNKDWepIRGvKIATIFQ 102
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLErfydpTSGEI---LLD--GVDIRDL--NLRW--LRS-QIGLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 DPMTsLDpiNTIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDA-EKRFNEYPFQYSGGMRQRIVIAIALACRPDIL 181
Cdd:cd03249 85 EPVL-FD--GTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGyDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 182 ICDEPTTALDV----TIQAQIIDLLKSlqqeyeFTTIFITHDLgvvASI--ADKVAVMYAGEIVEYGTVEE 246
Cdd:cd03249 162 LLDEATSALDAesekLVQEALDRAMKG------RTTIVIAHRL---STIrnADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-239 |
1.45e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.47 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleenGRVAQGTIDYRGQDLTKLKSNKdwEPIRGVKIATIFQDPMT 106
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI----ERPSAGKIWFSGHDITRLKNRE--VPFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPINTIGSQITEVIIKHQKKTPKEAKEMAVDymnKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDILICDEP 186
Cdd:PRK10908 91 LMDRTVYDNVAIPLIIAGASGDDIRRRVSAALD---KVGLLDKAKNF---PIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 896625925 187 TTALDVTIQAQIIDLLKSLQQeYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-242 |
1.67e-21 |
|
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: 91.28 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVAqgTIDyrGQDLTKlksnk 87
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--TVD--GFDVVK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwEPiRGVKIATIFQDPMTSLDPINTIGSQITEVIIKHQKKtPKEAKEMAVDYMNKVGIPD-AEKRFNEYpfqySGGMRQ 166
Cdd:cd03266 72 --EP-AEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLK-GDELTARLEELADRLGMEElLDRRVGGF----STGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-245 |
1.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLtktftgMLEENG--RVAQGTIDYRGQDLTKlkSNKDWepIRGvKIATIFQDP 104
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTL------LLHLNGiyLPQRGRVKVMGREVNA--ENEKW--VRS-KVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 ------MTSLD-----PINtigsqiteviikhQKKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIA 173
Cdd:PRK13647 89 ddqvfsSTVWDdvafgPVN-------------MGLDKDEVERRVEEALKAVRMWDFRDK---PPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 174 LACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVE 245
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-247 |
2.76e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDvrDKvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNK 87
Cdd:COG4152 1 MLELKGLTKRFG--DK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD----SGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwepI------RGvkiatifqdpmtsLDPINTIGSQIT---EviIKHQKKtpKEAKEMAVDYMNKVGIPDAEKRFNEypf 158
Cdd:COG4152 73 ----IgylpeeRG-------------LYPKMKVGEQLVylaR--LKGLSK--AEAKRRADEWLERLGLGDRANKKVE--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 159 QYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
....*....
gi 896625925 239 VEYGTVEEV 247
Cdd:COG4152 208 VLSGSVDEI 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-248 |
3.02e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKsnkdwepiRGV-----KIATIFQ 102
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGKPLDYSK--------RGLlalrqQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 DPMTSLdpintIGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEkRFNEYPFQ-YSGGMRQRIVIAIALACRPDIL 181
Cdd:PRK13638 85 DPEQQI-----FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 182 ICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIfITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-248 |
3.17e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGML-EENGRVAQGtiDYR-GQDLTKLKSNKDWEPirgvKIATIFQDP 104
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIVG--DYAiPANLKKIKEVKRLRK----EIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLDPiNTIGSQITEVIIkHQKKTPKEAKEMAVDYMNKVGIP-DAEKRfneYPFQYSGGMRQRIVIAIALACRPDILIC 183
Cdd:PRK13645 100 EYQLFQ-ETIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPeDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 184 DEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-245 |
4.34e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.94 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTkLKSNKDwePIR-GvkIATIFQ- 102
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDS----GEILIDGKPVR-IRSPRD--AIAlG--IGMVHQh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 ----DPMTsldpintigsqITEVII------KHQKKTPKEAKEMAVDYMNKVGI---PDAekrfneYPFQYSGGMRQRIV 169
Cdd:COG3845 89 fmlvPNLT-----------VAENIVlgleptKGGRLDRKAARARIRELSERYGLdvdPDA------KVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 170 IAIALACRPDILICDEPTTALdvTIQ--AQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVeyGTVE 245
Cdd:COG3845 152 ILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV--GTVD 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-247 |
4.78e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 21 RDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGqdltklksnkdwepirgvKIA-- 98
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT----SGRVEVNG------------------RVSal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 99 ----TIFQDPMTSLDPINTIGSqitevIIKHQKKTPKEAKEMAVDYmnkvgipdAE-KRFNEYPFQ-YSGGMRQRIVIAI 172
Cdd:COG1134 93 lelgAGFHPELTGRENIYLNGR-----LLGLSRKEIDEKFDEIVEF--------AElGDFIDQPVKtYSSGMRARLAFAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 173 ALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
27-239 |
5.44e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSNkdwepiRGVkiatIFQD--- 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP----YQHGSITLDGKPVEGPGAE------RGV----VFQNegl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 -PMTSLDPINTIGSQITEViikhqkktPKEAKE-MAVDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDIL 181
Cdd:PRK11248 82 lPWRNVQDNVAFGLQLAGV--------EKMQRLeIAHQMLKKVGLEGAEKRY---IWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 182 ICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLgvvasiadKVAVMYAGEIV 239
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI--------EEAVFMATELV 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-242 |
6.70e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.90 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 17 EFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKsnkdwepirgvk 96
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD----SGTVTVRGRVSSLLG------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 97 IATIFQDPMTSLDPINTIGSqitevIIKHQKKTPKEAKEMAVDYmnkvgipdAE-KRFNEYPF-QYSGGMRQRIVIAIAL 174
Cdd:cd03220 91 LGGGFNPELTGRENIYLNGR-----LLGLSRKEIDEKIDEIIEF--------SElGDFIDLPVkTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
27-252 |
6.83e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 90.04 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKdwepirgvkIAT------- 99
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL----PPRSGSIRFDGEDITGLPPHR---------IARlgigyvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 100 ----IFQDpMTSLDpiN-TIGSQIteviiKHQKKTPKEAKEMAVDYMnkvgiPDAEKRFNEYPFQYSGGMRQRIVIAIAL 174
Cdd:COG0410 85 egrrIFPS-LTVEE--NlLLGAYA-----RRDRAEVRADLERVYELF-----PRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFIT-HDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPR 252
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREG--VTILLVeQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-238 |
8.46e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 89.15 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 32 SLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNKdwEPIrgvkiATIFQDpmTSLDPI 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP----ASGSIKVNDQSHTGLAPYQ--RPV-----SMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 112 NTIGSQITeVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDILICDEPTTALD 191
Cdd:TIGR01277 85 LTVRQNIG-LGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896625925 192 VTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-246 |
1.24e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.10 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLEengRV---AQGTIDYRGQDltklksnkdwepIRGVK------- 96
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLQ---RVfdpQSGRILIDGTD------------IRTVTraslrrn 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 97 IATIFQDPMTsldpIN-TIGSQITeviIKHQKKTPKEAKE-----MAVDYMNKvgipdAEKRFN----EYPFQYSGGMRQ 166
Cdd:PRK13657 411 IAVVFQDAGL----FNrSIEDNIR---VGRPDATDEEMRAaaeraQAHDFIER-----KPDGYDtvvgERGRQLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-252 |
1.24e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEF-DVrdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNK 87
Cdd:PRK09536 4 IDVSDLSVEFgDT-----TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwepiRGVKIATIFQDpmTSLDpINTIGSQITEViikhqKKTPK--------EAKEMAVDY-MNKVGIpdaeKRFNEYPF 158
Cdd:PRK09536 75 -----ASRRVASVPQD--TSLS-FEFDVRQVVEM-----GRTPHrsrfdtwtETDRAAVERaMERTGV----AQFADRPV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 159 -QYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:PRK09536 138 tSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGR 216
|
250
....*....|....*
gi 896625925 238 IVEYGTVEEVFYDPR 252
Cdd:PRK09536 217 VRAAGPPADVLTADT 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-219 |
1.38e-20 |
|
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: 88.30 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDvrDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLtklksNKD 88
Cdd:COG4133 3 LEAENLSCRRG--ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL----PPSAGEVLWNGEPI-----RDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEPIRGvKIATIFQDP-----MTSLDPINTIGSQiteviikHQKKTPKEAKEMAVDymnKVGIPDAEkrfNEYPFQYSGG 163
Cdd:COG4133 70 REDYRR-RLAYLGHADglkpeLTVRENLRFWAAL-------YGLRADREAIDEALE---AVGLAGLA---DLPVRQLSAG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHD 219
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-246 |
1.61e-20 |
|
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: 92.47 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDYRGQDLTKLKSnkdwepirg 94
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEpDSGQILLDGHDLADYTLASLRR--------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 95 vKIATIFQDPMTSLDPI-NTIGSQITEVIIKHQKKtpkEAKEMA--VDYMNKvgIPDA-EKRFNEYPFQYSGGMRQRIVI 170
Cdd:TIGR02203 407 -QVALVSQDVVLFNDTIaNNIAYGRTEQADRAEIE---RALAAAyaQDFVDK--LPLGlDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 171 AIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEE 246
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
26-242 |
1.81e-20 |
|
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: 88.11 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKdwepI------RGvkiat 99
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD----SGEVLFDGKPLDIAARNR----IgylpeeRG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 100 IFQDpMTSLDPINTIGSqiteviIKHQKKtpKEAKEMAVDYMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRPD 179
Cdd:cd03269 81 LYPK-MKVIDQLVYLAQ------LKGLKK--EEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
237-323 |
1.95e-20 |
|
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: 84.34 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 237 EIVEYGTVEEVFYDPRHPYTWSLLSSLPQLADDKGELYSIPGTPPSLYSQLQGDAFALRSDYAMEIDFEEKPPQIYVTDT 316
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 896625925 317 HWAKTWL 323
Cdd:TIGR01727 81 HRVACHL 87
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-243 |
3.11e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 87.93 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLksnkDWEPIRGvKIATIFQDPMT 106
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKI----GLHDLRS-RISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 -------SLDPINTIG-SQITEVIIKHQKKTPKEAKEMAVDYMNKVGipdaekrfneyPFQYSGGMRQRIVIAIALACRP 178
Cdd:cd03244 90 fsgtirsNLDPFGEYSdEELWQALERVGLKEFVESLPGGLDTVVEEG-----------GENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSlqqeyEF---TTIFITHDLGVVASiADKVAVMYAGEIVEYGT 243
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIRE-----AFkdcTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-242 |
3.13e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 87.55 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 19 DVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGM-LEENGRVaqgTIDyrGQDLTKLksnkdwePIRGVKI 97
Cdd:cd03298 5 KIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFeTPQSGRV---LIN--GVDVTAA-------PPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 98 ATIFQDpmTSLDPINTIGSQITEVIIKHQKKTPKEAKEMAVdYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACR 177
Cdd:cd03298 73 SMLFQE--NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEV-ALARVGLAGLEKRL---PGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
26-254 |
3.43e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleENGRVAQGTIDyrGQDLTKlksnkdwEPIRGVKIATIFQDpm 105
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL--EKPTEGQIFID--GEDVTH-------RSIQQRDICMVFQS-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDPINTIGSQItEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRPDILICDE 185
Cdd:PRK11432 87 YALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 186 PTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFydpRHP 254
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQP 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-239 |
4.06e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKdwepiRGVKIATIFQDPM 105
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSL----PPDSGSILIDGKDVTKLPEYK-----RAKYIGRVFQDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tsldpINTIGS-QITEVII----KHQKKT-----PKEAKEMAVDYMNKVGIpDAEKRFNEYPFQYSGGMRQRIVIAIALA 175
Cdd:COG1101 91 -----MGTAPSmTIEENLAlayrRGKRRGlrrglTKKRRELFRELLATLGL-GLENRLDTKVGLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
27-268 |
4.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDyrGQDLTKLKSnkdwepIRGVkIATIFQDPM 105
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSGID--TGDFSKLQG------IRKL-VGIVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLdpintIGSQITEVIIKHQKK---TPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILI 182
Cdd:PRK13644 88 TQF-----VGRTVEEDLAFGPENlclPPIEIRKRVDRALAEIGL---EKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVaSIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLSS 262
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPS 237
|
....*.
gi 896625925 263 LPQLAD 268
Cdd:PRK13644 238 LIELAE 243
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-245 |
5.27e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.82 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEfdVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmlEENGRVAQGTIDYRGQDLTklksnkD 88
Cdd:COG0396 1 LEIKNLHVS--VEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKYEVTSGSILLDGEDIL------E 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEP----IRGVKIAtiFQDP-----MTSLDPINTIGSQITEviikhQKKTPKEAKEMAVDYMNKVGIPD--AEKRFNEyp 157
Cdd:COG0396 69 LSPderaRAGIFLA--FQYPveipgVSVSNFLRTALNARRG-----EELSAREFLKLLKEKMKELGLDEdfLDRYVNE-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 158 fQYSGGMRQRIVIAIALACRPDILICDEPTTALDV-TIQAqIIDLLKSLQQEyEFTTIFITHDLGVVASI-ADKVAVMYA 235
Cdd:COG0396 140 -GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLVD 216
|
250
....*....|
gi 896625925 236 GEIVEYGTVE 245
Cdd:COG0396 217 GRIVKSGGKE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-238 |
8.66e-20 |
|
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: 85.56 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEfdvrdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTkLKSN 86
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR----PPASGEITLDGKPVT-RRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KDWepiRGVKIATIfqdpmtsldpintigsqiteviikhqkktPKEAKEMAVdymnkvgIPDAEKRFN-EYPFQYSGGMR 165
Cdd:cd03215 70 RDA---IRAGIAYV-----------------------------PEDRKREGL-------VLDLSVAENiALSSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 166 QRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-252 |
1.34e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKdwepIRGVKIATIFQD- 103
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG----GTILLRGQHIEGLPGHQ----IARMGVVRTFQHv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 ----PMTSLDpiNTIGSQiteviikHQK----------KTP------KEAKEMAVDYMNKVGIPDAEkrfNEYPFQYSGG 163
Cdd:PRK11300 90 rlfrEMTVIE--NLLVAQ-------HQQlktglfsgllKTPafrraeSEALDRAATWLERVGLLEHA---NRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGT 243
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
....*....
gi 896625925 244 VEEVFYDPR 252
Cdd:PRK11300 238 PEEIRNNPD 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-233 |
1.48e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGqdltklksnkdwepirGVKIATIFQdpM 105
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL----RPTSGTVRRAG----------------GARVAYVPQ--R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLD---PIN-----TIGsqiteviiKHQKKTP-----KEAKEMAVDYMNKVGIPDAEKRfneyPFQ-YSGGMRQRIVIA 171
Cdd:NF040873 64 SEVPdslPLTvrdlvAMG--------RWARRGLwrrltRDDRAAVDDALERVGLADLAGR----QLGeLSGGQRQRALLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 172 IALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASiADKVAVM 233
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
26-238 |
2.46e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEE--NGRVAQGTidyrgqdlTKLKSNKDwepirgvKIATIFQD 103
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETpsAGELLAGT--------APLAEARE-------DTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 ----PMTSLdpINTIGSQITeviikhqkktpKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:PRK11247 90 arllPWKKV--IDNVGLGLK-----------GQWRDAALQALAAVGLAD---RANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-247 |
2.66e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVefdVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSN 86
Cdd:COG3845 256 VVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLR----PPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KdwepIRGVKIATIFQDPM-----TSLDpintigsqITE-VIIKHQKKTP---------KEAKEMAVDYMNKVGI----P 147
Cdd:COG3845 329 E----RRRLGVAYIPEDRLgrglvPDMS--------VAEnLILGRYRRPPfsrggfldrKAIRAFAEELIEEFDVrtpgP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 148 DAEKRfneypfQYSGGMRQRIVIAIALACRPDILICDEPTTALDV----TIQAQIIDLLKSlqqeyEFTTIFITHDLGVV 223
Cdd:COG3845 397 DTPAR------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLELRDA-----GAAVLLISEDLDEI 465
|
250 260
....*....|....*....|....
gi 896625925 224 ASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG3845 466 LALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-233 |
4.80e-19 |
|
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: 88.11 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 2 TQEKNVILTARDIVVEFD---VRDKVLT-AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRG 77
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSgvsVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 78 QDLTKLKSnKDWepirGVKIATIFQDP-MTSldpintiGSqITEVIIKHQKKTPKEAKEMAVDymnKVGIPDA------- 149
Cdd:TIGR02857 384 VPLADADA-DSW----RDQIAWVPQHPfLFA-------GT-IAENIRLARPDASDAEIREALE---RAGLDEFvaalpqg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 150 -EKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiAD 228
Cdd:TIGR02857 448 lDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-AD 524
|
....*
gi 896625925 229 KVAVM 233
Cdd:TIGR02857 525 RIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-239 |
6.52e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 84.18 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDYRGQDLTKLKSNkdwepirgvkIATIFQDPM 105
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRN----------IGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 ----TSLDPInTIGSQI--TEVIIkhqkktpkEAKEMAV--DYMNKVgiPDA-EKRFNEYPFQYSGGMRQRIVIAIALAC 176
Cdd:cd03245 89 lfygTLRDNI-TLGAPLadDERIL--------RAAELAGvtDFVNKH--PNGlDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVaSIADKVAVMYAGEIV 239
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-237 |
8.19e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVrdkvLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrVAQGTIDYRGQDLtKLKSNK 87
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG--TYEGEIIFEGEEL-QASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEPiRGvkIATIFQD-----PMTSLDPInTIGSQITEVIIKHQKKTPKEAKEMavdyMNKVGIP-DAEKRFNEypfqYS 161
Cdd:PRK13549 78 DTER-AG--IAIIHQElalvkELSVLENI-FLGNEITPGGIMDYDAMYLRAQKL----LAQLKLDiNPATPVGN----LG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGE 237
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-239 |
1.25e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.47 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 22 DKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRvAQGTIDYRGQDLTKLKsnkdwepirgvkiatiF 101
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT-TSGQILFNGQPRKPDQ----------------F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDPMTSLDPINTIGSQIT-------EVIIKHQKKTPKEAKEM--AVDYMNKVGIPDAEkrfNEYPFQYSGGMRQRIVIAI 172
Cdd:cd03234 80 QKCVAYVRQDDILLPGLTvretltyTAILRLPRKSSDAIRKKrvEDVLLRDLALTRIG---GNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 173 ALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyefttifithDLGVVASIA----------DKVAVMYAGEIV 239
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR----------NRIVILTIHqprsdlfrlfDRILLLSSGEIV 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-247 |
1.26e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.78 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDvrDKVltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleENGRVAQGTIDYR------------ 76
Cdd:TIGR03269 1 IEVKNLTKKFD--GKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPTSGRIIYHvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 77 -----------GQDLTKLKSNKdWEPIRGV------KIATIFQDPMtSLDPINTIGSQITEVIikHQKKTP-KEAKEMAV 138
Cdd:TIGR03269 75 pskvgepcpvcGGTLEPEEVDF-WNLSDKLrrrirkRIAIMLQRTF-ALYGDDTVLDNVLEAL--EEIGYEgKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 139 DYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITH 218
Cdd:TIGR03269 151 DLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
250 260
....*....|....*....|....*....
gi 896625925 219 DLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-239 |
1.90e-18 |
|
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: 83.15 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 23 KVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENG---RVAqGTIDYRGQDltKLKSnkdwepirgvKIAT 99
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSgevRVA-GLVPWKRRK--KFLR----------RIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 100 IFQDPMT---SLDPINT--IGSQITEVIIKHQKKTPKEAKEMavdyMNKVGIPDAEKRfneypfQYSGGMRQRIVIAIAL 174
Cdd:cd03267 99 VFGQKTQlwwDLPVIDSfyLLAAIYDLPPARFKKRLDELSEL----LDLEELLDTPVR------QLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-246 |
3.25e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.84 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 1 MTQEKN----VILTAR-DIV---VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGT 72
Cdd:PRK11176 324 LEQEKDegkrVIERAKgDIEfrnVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD----IDEGE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 73 IDYRGQDLT--KLKSNKDwepirgvKIATIFQDPMTSLDPI-NTIGSQITEviiKHQKKTPKEAKEMA--VDYMNKVgip 147
Cdd:PRK11176 400 ILLDGHDLRdyTLASLRN-------QVALVSQNVHLFNDTIaNNIAYARTE---QYSREQIEEAARMAyaMDFINKM--- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 148 daEKRFN----EYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVV 223
Cdd:PRK11176 467 --DNGLDtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTI 542
|
250 260
....*....|....*....|...
gi 896625925 224 ASiADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK11176 543 EK-ADEILVVEDGEIVERGTHAE 564
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-239 |
3.67e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.55 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFtGMLEengRVAQGTIDYRGQDLTKLkS 85
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLD---KPTSGTYRVAGQDVATL-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 86 NKDWEPIRGVKIATIFQ--DPMTSLDpintiGSQITEVIIKHQKKTPKEAKEMAVDYMNKVGIPDaekRFNEYPFQYSGG 163
Cdd:PRK10535 77 ADALAQLRREHFGFIFQryHLLSHLT-----AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDlGVVASIADKVAVMYAGEIV 239
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-248 |
4.48e-18 |
|
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: 81.89 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSNKDWEpirgvKIATIFQDPM- 105
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD----PQKGQILIDGIDIRDISRKSLRS-----MIGVVLQDTFl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 ---TSLDPI--NTIGSQITEVIIkhqkktpkEAKEMAVDYMnkvgIPDAEKRFNEYPFQ----YSGGMRQRIVIAIALAC 176
Cdd:cd03254 89 fsgTIMENIrlGRPNATDEEVIE--------AAKEAGAHDF----IMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEVF 248
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-257 |
4.77e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 81.82 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 33 LDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKSNKDWEPIRGvKIATIFqdpmtSLDPIN 112
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLI----PPAKGTVKVAGASPGKGWRHIGYVPQRH-EFAWDF-----PISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 113 TIGSQITEVIIKHQKktPKEAKEMAV-DYMNKVGIPDAEKRfneyPF-QYSGGMRQRIVIAIALACRPDILICDEPTTAL 190
Cdd:TIGR03771 71 TVMSGRTGHIGWLRR--PCVADFAAVrDALRRVGLTELADR----PVgELSGGQRQRVLVARALATRPSVLLLDEPFTGL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 191 DVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVaVMYAGEIVEYGTVEEVfydpRHPYTW 257
Cdd:TIGR03771 145 DMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL----QDPAPW 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-242 |
5.58e-18 |
|
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: 80.43 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDivVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNkd 88
Cdd:cd03247 1 LSINN--VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ----QGEITLDGVPVSDLEKA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wepiRGVKIATIFQDPM---TSLdpintigsqiteviikhqkktpkeakemavdyMNKVGIpdaekrfneypfQYSGGMR 165
Cdd:cd03247 73 ----LSSLISVLNQRPYlfdTTL--------------------------------RNNLGR------------RFSGGER 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 166 QRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLksLQQEYEFTTIFITHDLGVVASiADKVAVMYAGEIVEYG 242
Cdd:cd03247 105 QRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-252 |
9.14e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKsvlTKTF---TGMLeengRVAQGTIDYRGQDLTKLk 84
Cdd:COG1137 3 TLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGK---TTTFymiVGLV----KPDSGRIFLDGEDITHL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 85 snkdwePI-----RGvkI------ATIFQDpMTSLDPIntigsqitEVIIKHQKKTPKEAKEMAVDYMNKVGIpdaEKRF 153
Cdd:COG1137 71 ------PMhkrarLG--IgylpqeASIFRK-LTVEDNI--------LAVLELRKLSKKEREERLEELLEEFGI---THLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 154 NEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALD---VT-IQaQIIDLLKSLQqeyefTTIFIT-HD----LGVVa 224
Cdd:COG1137 131 KSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQ-KIIRHLKERG-----IGVLITdHNvretLGIC- 203
|
250 260
....*....|....*....|....*...
gi 896625925 225 siaDKVAVMYAGEIVEYGTVEEVFYDPR 252
Cdd:COG1137 204 ---DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-247 |
9.32e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 80.26 E-value: 9.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEfdVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmlEENGRVAQGTIDYRGQDLTKLKSNkd 88
Cdd:cd03217 1 LEIKDLHVS--VGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKYEVTEGEILFKGEDITDLPPE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wEPIR-GVKIAtiFQDPMtsldpintigsQITEVIIKhqkktpkeakemavDYMNKVgipdaekrfNEypfQYSGGMRQR 167
Cdd:cd03217 73 -ERARlGIFLA--FQYPP-----------EIPGVKNA--------------DFLRYV---------NE---GFSGGEKKR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASI-ADKVAVMYAGEIVEYGTVEE 246
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKEL 191
|
.
gi 896625925 247 V 247
Cdd:cd03217 192 A 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-251 |
1.33e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.00 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLEENGRVAQGTIDYRGQDLTKLksnkDWEPIRgVKIATIFQDPMTs 107
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPLVQY----DHHYLH-RQVALVGQEPVL- 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 ldpintIGSQITEVIIKHQKKTPKE-----AK---------EMAVDYMNKVGipdaekrfnEYPFQYSGGMRQRIVIAIA 173
Cdd:TIGR00958 567 ------FSGSVRENIAYGLTDTPDEeimaaAKaanahdfimEFPNGYDTEVG---------EKGSQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 174 LACRPDILICDEPTTALDVTIQAqiidLLKSLQQEYEFTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-251 |
1.46e-17 |
|
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: 80.66 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLksnkd 88
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDITKL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wePI-----RGV----KIATIFQDpMTSLDPIntigsqitEVIIKHQKKTPKEAKEMAVDYMNKVGIpdaEKRFNEYPFQ 159
Cdd:cd03218 68 --PMhkrarLGIgylpQEASIFRK-LTVEENI--------LAVLEIRGLSKKEREEKLEELLEEFHI---THLRKSKASS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALD-VTIQ--AQIIDLLKSLQqeyefTTIFIT-HDLGVVASIADKVAVMYA 235
Cdd:cd03218 134 LSGGERRRVEIARALATNPKFLLLDEPFAGVDpIAVQdiQKIIKILKDRG-----IGVLITdHNVRETLSITDRAYIIYE 208
|
250
....*....|....*.
gi 896625925 236 GEIVEYGTVEEVFYDP 251
Cdd:cd03218 209 GKVLAEGTPEEIAANE 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-248 |
1.82e-17 |
|
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: 83.26 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTklksnkDWEPIR-GVKIATIFQDP-- 104
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW----PPTAGSVRLDGADLS------QWDREElGRHIGYLPQDVel 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 -----------MTSLDPintigsqiTEVIikhqkktpkEAKEMAvdymnkvGIPDAEKRFneyPFQY-----------SG 162
Cdd:COG4618 418 fdgtiaeniarFGDADP--------EKVV---------AAAKLA-------GVHEMILRL---PDGYdtrigeggarlSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVAsIADKVAVMYAGEIVEYG 242
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFG 548
|
....*.
gi 896625925 243 TVEEVF 248
Cdd:COG4618 549 PRDEVL 554
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-220 |
1.98e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.18 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRDKVLtaiRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTKLKSNKD 88
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVL---DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL----QGEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 WEPIRGVKiatifQDPmtsldpiNTIGSQITE-VIIKHQKKTPKEAKEMavdyMNKVGIPD--------AEKRFNEYPFQ 159
Cdd:TIGR02868 408 RRRVSVCA-----QDA-------HLFDTTVREnLRLARPDATDEELWAA----LERVGLADwlralpdgLDTVLGEGGAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLksLQQEYEFTTIFITHDL 220
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-243 |
2.47e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 79.38 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDYRGQDLTKLKSnkdwepirgvKIATIFQDPM 105
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDLRS----------SLTIIPQDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 -------TSLDPINTIGS-QITEVIikhqkktpkeakemavdymnkvgipdaekRFNEYPFQYSGGMRQRIVIAIALACR 177
Cdd:cd03369 93 lfsgtirSNLDPFDEYSDeEIYGAL-----------------------------RVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 178 PDILICDEPTTALDVTIQAQIidlLKSLQQEYEFTTIF-ITHDLGVVASIaDKVAVMYAGEIVEYGT 243
Cdd:cd03369 144 PRVLVLDEATASIDYATDALI---QKTIREEFTNSTILtIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-243 |
1.07e-16 |
|
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: 81.32 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLtklkSNKDWEPIRGVkIATIFQDPMt 106
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR----SGEILLNGFSL----KDIDRHTLRQF-INYLPQEPY- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 sldpINTiGSQITEVIIKHQKKTPKEAKEMAVDYmnkVGI-PDAEK-------RFNEYPFQYSGGMRQRIVIAIALACRP 178
Cdd:TIGR01193 559 ----IFS-GSILENLLLGAKENVSQDEIWAACEI---AEIkDDIENmplgyqtELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEyefTTIFITHDLGvVASIADKVAVMYAGEIVEYGT 243
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGS 691
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-219 |
1.15e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.52 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRvAQGTIDYRGQDLTKLksnkdwePIRGVKIATIFQDPMts 107
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFS-ASGEVLLNGRRLTAL-------PAEQRRIGILFQDDL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LDPINTIGSQI----TEVIIKHQKKtpkeakEMAVDYMNKVGIPDaekRFNEYPFQYSGGMRQRIVIAIALACRPDILIC 183
Cdd:COG4136 87 LFPHLSVGENLafalPPTIGRAQRR------ARVEQALEEAGLAG---FADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 896625925 184 DEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHD 219
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
28-247 |
1.26e-16 |
|
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: 80.85 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLtklksnKDWEPIR-GVKIATIFQDpmT 106
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP----TSGSVRLDGADL------KQWDRETfGKHIGYLPQD--V 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPiNTIGSQITEViikHQKKTPKEAKEMAVdymnkvgIPDAEKRFNEYPFQY-----------SGGMRQRIVIAIALA 175
Cdd:TIGR01842 402 ELFP-GTVAENIARF---GENADPEKIIEAAK-------LAGVHELILRLPDGYdtvigpggatlSGGQRQRIALARALY 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEV 247
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGC-VDKILVLQDGRIARFGERDEV 540
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-248 |
2.66e-16 |
|
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: 77.43 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFDvrDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmleENGRVAQGTIDYRGQDLTKLks 85
Cdd:COG1119 1 DPLLELRNVTVRRG--GKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITG---DLPPTYGNDVRLFGERRGGE-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 86 nkDWEPIRGvKI----ATIFQDPMTSLDPINTIGSQITEVIIKHQKKTPkEAKEMAVDYMNKVGIPD-AEKRFNeypfQY 160
Cdd:COG1119 72 --DVWELRK-RIglvsPALQLRFPRDETVLDVVLSGFFDSIGLYREPTD-EQRERARELLELLGLAHlADRPFG----TL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLG-VVASIaDKVAVMYAGEIV 239
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKDGRVV 222
|
....*....
gi 896625925 240 EYGTVEEVF 248
Cdd:COG1119 223 AAGPKEEVL 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-243 |
3.33e-16 |
|
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: 79.86 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 29 RGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVaqgTIDyrGQDLTKLKSnkdwEPIRGVkIATIFQDpmTS 107
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDvTSGRI---LID--GQDIRDVTQ----ASLRAA-IGIVPQD--TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 L--DpinTIGSQI---------TEVIikhqkktpkEAKEMA-----VDymnkvGIPDA-EKRFNEYPFQYSGGMRQRIVI 170
Cdd:COG5265 443 LfnD---TIAYNIaygrpdaseEEVE---------AAARAAqihdfIE-----SLPDGyDTRVGERGLKLSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 171 AIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEIVEYGT 243
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-239 |
4.89e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEfdvrdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLtKLKSN 86
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD----PADSGEIRLDGKPV-RIRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KDwePIR-GV-------KIATIFQDpmtsldpiNTIGSQITEVIIKHQKK----TPKEAKEMAVDYMNKVGI--PDAEKR 152
Cdd:COG1129 322 RD--AIRaGIayvpedrKGEGLVLD--------LSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRIktPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 153 FNeypfQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAV 232
Cdd:COG1129 392 VG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILV 466
|
....*..
gi 896625925 233 MYAGEIV 239
Cdd:COG1129 467 MREGRIV 473
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-247 |
5.05e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNkdwEPIRgvKIATIFQDPM 105
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP----AHGHVWLDGEHIQHYASK---EVAR--RIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDPinTIGSQITEVIIKHQ---KKTPKEAKEMAVDYMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRPDILI 182
Cdd:PRK10253 92 TPGDI--TVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVD---TLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-238 |
5.79e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 29 RGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKDWEpiRGvkIATIFQDPMTS- 107
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG----GRIMLNGKEINALSTAQRLA--RG--LVYLPEDRQSSg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 --LD-PI--NTIGsqiteviIKHQKKT--PKEAKEMAV--DYMNKVGIpdaekRFNEyPFQ----YSGGMRQRIVIAIAL 174
Cdd:PRK15439 352 lyLDaPLawNVCA-------LTHNRRGfwIKPARENAVleRYRRALNI-----KFNH-AEQaartLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-239 |
7.00e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.71 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVrdkvLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrVAQGTIDYRGQDLtKLKSNK 87
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG--TWDGEIYWSGSPL-KASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 DWEpirGVKIATIFQD-----PMTSLDPInTIGSQIT-EVIIKHQKKTPKEAKEMavdyMNKVGIPDAEkrfNEYPF-QY 160
Cdd:TIGR02633 74 DTE---RAGIVIIHQEltlvpELSVAENI-FLGNEITlPGGRMAYNAMYLRAKNL----LRELQLDADN---VTRPVgDY 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQeYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-248 |
8.45e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTK-LKSNKdwepirgvkIATIFQDP 104
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPTRQaLQKNL---------VAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLD-PIntigsQITEVIIKHQ-------KKTPKEAKEMAVDYMNKVGIPDAEKRfneYPFQYSGGMRQRIVIAIALAC 176
Cdd:PRK15056 88 EVDWSfPV-----LVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHR---QIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADkVAVMYAGEIVEYGTVEEVF 248
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-242 |
1.37e-15 |
|
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: 74.22 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGRVaQGTIDYRGQDLTKLKSN 86
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV-EGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KDWEPI----RGVKIATIfqdpmtsldpintigsqiteviikhqkkTPKEAKEMAvdymnkvgipdAEKRFNEYPFQYSG 162
Cdd:cd03233 81 YPGEIIyvseEDVHFPTL----------------------------TVRETLDFA-----------LRCKGNEFVRGISG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVA-SIADKVAVMYAGEIVEY 241
Cdd:cd03233 122 GERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQIYY 201
|
.
gi 896625925 242 G 242
Cdd:cd03233 202 G 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-242 |
1.37e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.12 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVEFDVRD--KVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvAQGTIDYRGQDLTKLK 84
Cdd:cd03213 2 VTLSFRNLTVTVKSSPskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEVLINGRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 85 SNKdwepirgvKIATIFQDpmtsldpintigsqitEVIIKHQkkTPKEAKEMAvdymnkvgipdAEKRfneypfQYSGGM 164
Cdd:cd03213 80 FRK--------IIGYVPQD----------------DILHPTL--TVRETLMFA-----------AKLR------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 165 RQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDL-GVVASIADKVAVMYAGEIVEYG 242
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
26-247 |
1.46e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLeenGRVA---QGTIDYRGQDLTKLKSNKdwepiRGVKIATIFQ 102
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKS----TLLSMI---SRLLppdSGEVLVDGLDVATTPSRE-----LAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 DpmtsldpiNTIGSQITeviIK----------HQKKTPKEAKEM---AVDYMNkvgIPDAEKRFNEypfQYSGGMRQRIV 169
Cdd:COG4604 83 E--------NHINSRLT---VRelvafgrfpySKGRLTAEDREIideAIAYLD---LEDLADRYLD---ELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 170 IAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-246 |
2.88e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 23 KVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENG--RVAqGTIDYRgqDLTKLKSNkdwepirgvkIAT 99
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVpTSGevRVL-GYVPFK--RRKEFARR----------IGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 100 IF-Q------D--PMTSLDpINtigsqiteviikhqkktpkeaKEMavdYmnkvGIPDAE--KRFNEY-------PF--- 158
Cdd:COG4586 100 VFgQrsqlwwDlpAIDSFR-LL---------------------KAI---Y----RIPDAEykKRLDELvelldlgELldt 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 159 ---QYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFIT-HDLGVVASIADKVAVMY 234
Cdd:COG4586 151 pvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERG-TTILLTsHDMDDIEALCDRVIVID 229
|
250
....*....|..
gi 896625925 235 AGEIVEYGTVEE 246
Cdd:COG4586 230 HGRIIYDGSLEE 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-240 |
3.80e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEF-DVRdkvltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmleengrVA-----QGTIDYRGQdLT 81
Cdd:NF040905 1 ILEMRGITKTFpGVK-----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-------VYphgsyEGEILFDGE-VC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 82 KLKSNKDWEPiRGvkIATIFQD----PMTSldpintigsqITEVI----------IKHQKKTPKEAKEMavdyMNKVGIp 147
Cdd:NF040905 68 RFKDIRDSEA-LG--IVIIHQElaliPYLS----------IAENIflgnerakrgVIDWNETNRRAREL----LAKVGL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 148 daekrfNEYPFQYSG----GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVV 223
Cdd:NF040905 130 ------DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEI 202
|
250
....*....|....*..
gi 896625925 224 ASIADKVAVMYAGEIVE 240
Cdd:NF040905 203 RRVADSITVLRDGRTIE 219
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
239-302 |
4.41e-15 |
|
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: 68.97 E-value: 4.41e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 239 VEYGTVEEVFYDPRHPYTWSLLSSLPQLADDKGELYSIPGTPPSLYSQLQGDAFALRSDYAMEI 302
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEE 64
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-247 |
4.44e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKtftgMLEENGRVAQGTIDYRGQDLTKLKSNkdwepIRGV 95
Cdd:PRK10575 17 VSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLK----MLGRHQPPSEGEILLDAQPLESWSSK-----AFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 96 KIATIFQ-----DPMTSLDPInTIGSQITEVIIKHQKKTPKEAKEMAVDYmnkVGIPDAEKRFNEypfQYSGGMRQRIVI 170
Cdd:PRK10575 86 KVAYLPQqlpaaEGMTVRELV-AIGRYPWHGALGRFGAADREKVEEAISL---VGLKPLAHRLVD---SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 171 AIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-246 |
6.02e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 6 NVILTARDIVVEFDvrDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTidyrgqdltklk 84
Cdd:COG0488 313 KKVLELEGLSKSYG--DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTVKLGE------------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 85 snkdwepirGVKIATIFQDpMTSLDPINTIgsqITEVIIKHQKKTPKEAKEMAvdymnkvgipdaeKRFN---EYPFQY- 160
Cdd:COG0488 377 ---------TVKIGYFDQH-QEELDPDKTV---LDELRDGAPGGTEQEVRGYL-------------GRFLfsgDDAFKPv 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 ---SGGMRQRIVIAIALACRPDILICDEPTTALDV-TIQAqIIDLLkslqQEYEFTTIFITHDLGVVASIADKVAVMYAG 236
Cdd:COG0488 431 gvlSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEAL----DDFPGTVLLVSHDRYFLDRVATRILEFEDG 505
|
250
....*....|.
gi 896625925 237 EIVEY-GTVEE 246
Cdd:COG0488 506 GVREYpGGYDD 516
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-241 |
1.03e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 22 DKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRgqdltklksnkdwepiRGVKIATIF 101
Cdd:COG0488 10 GRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS----GEVSIP----------------KGLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDP------------MTSLDPINTIGSQITEVIIKHQKkTPKEAKEMAV-----------DY-------MNKVGIP--DA 149
Cdd:COG0488 68 QEPpldddltvldtvLDGDAELRALEAELEELEAKLAE-PDEDLERLAElqeefealggwEAearaeeiLSGLGFPeeDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 150 EKRFNEYpfqySGGMRQRIVIAIALACRPDILICDEPTTALDvtIQAqiIDLLKSLQQEYEFTTIFITHDLGVVASIADK 229
Cdd:COG0488 147 DRPVSEL----SGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES--IEWLEEFLKNYPGTVLVVSHDRYFLDRVATR 218
|
250
....*....|..
gi 896625925 230 VAVMYAGEIVEY 241
Cdd:COG0488 219 ILELDRGKLTLY 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-246 |
1.62e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 32 SLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSNKdwepiRGVKIatIFQDpmTSLDPI 111
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLT----PASGSLTLNGQDHTTTPPSR-----RPVSM--LFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 112 NTIGSQITEVIIKHQKKTPKEAKEMAvDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDILICDEPTTALD 191
Cdd:PRK10771 86 LTVAQNIGLGLNPGLKLNAAQREKLH-AIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 192 VTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-246 |
2.52e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 3 QEKNVILTARDIVVeFDVRDKVLTAirGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrvAQGTIDYRGQDLTK 82
Cdd:PRK11174 344 SNDPVTIEAEDLEI-LSPDGKTLAG--PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----YQGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 83 LkSNKDWepiRGvKIATIFQDPM----TSLDPINTIGSQITEVIIKH--QKKTPKE---AKEMAVDYMnkvgIPDAEKRF 153
Cdd:PRK11174 416 L-DPESW---RK-HLSWVGQNPQlphgTLRDNVLLGNPDASDEQLQQalENAWVSEflpLLPQGLDTP----IGDQAAGL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 154 neypfqySGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIaDKVAVM 233
Cdd:PRK11174 487 -------SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVM 556
|
250
....*....|...
gi 896625925 234 YAGEIVEYGTVEE 246
Cdd:PRK11174 557 QDGQIVQQGDYAE 569
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
27-251 |
2.81e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEengRVAQGTIDYRGQDLTKLksnkdwEPI-RGvkIATIFQD-- 103
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LE---RITSGEIWIGGRVVNEL------EPAdRD--IAMVFQNya 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 --P-MTSLDPInTIGSQIteviikhqKKTPKEAKEMAVDymNKVGIPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:PRK11650 87 lyPhMSVRENM-AYGLKI--------RGMPKAEIEERVA--EAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 181 LICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDlGVVA-SIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-QVEAmTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-247 |
3.40e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.39 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTklksnkdwepirgVKIATIFQDPMT 106
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN----KGTVDIKGSAAL-------------IAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPINTIGsqiteVIIKHQKKTPKEAKEMAVDYmnkvgiPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEP 186
Cdd:PRK13545 102 GIENIELKG-----LMMGLTKEKIKEIIPEIIEF------ADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 187 TTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-247 |
3.58e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 24 VLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNKDWEpirgVKIATIFQD 103
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINNINYNKLDHKLAAQ----LGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 pmtsLDPINTIGSQITEVIIKHQKKTP--------KEAKEMAVDYMNKVGIpdaEKRFNEYPFQYSGGMRQRIVIAIALA 175
Cdd:PRK09700 89 ----LSVIDELTVLENLYIGRHLTKKVcgvniidwREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-238 |
4.00e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 70.96 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLEENGRVAQGTIDYRGQDLTKLKSNKDWEpirgvKIATIFQDPMTS 107
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS-----KVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 ldpintiGSQITEVI-IKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFN----EYPFQYSGGMRQRIVIAIALACRPDILI 182
Cdd:cd03248 101 -------ARSLQDNIaYGLQSCSFECVKEAAQKAHAHSFISELASGYDtevgEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASiADKVAVMYAGEI 238
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-247 |
1.55e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 11 ARDIVVEFDV--RDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmlEENGRVAQGTIDYrgqdltklksnkd 88
Cdd:COG2401 27 VAIVLEAFGVelRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCVDV------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wepirgvkiatifqdpmtsldPINTIGSQITevIIKH--QKKTPKEAKEmavdYMNKVGIPDA---EKRFNEYpfqySGG 163
Cdd:COG2401 92 ---------------------PDNQFGREAS--LIDAigRKGDFKDAVE----LLNAVGLSDAvlwLRRFKEL----STG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 164 MRQRIVIAIALACRPDILICDEPTTALDVTiQAQIIDL-LKSLQQEYEFTTIFITHDLGVVASIADKVAVmyageIVEYG 242
Cdd:COG2401 141 QKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLI-----FVGYG 214
|
....*
gi 896625925 243 TVEEV 247
Cdd:COG2401 215 GVPEE 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-263 |
2.01e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.01 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 3 QEKNVILTARDivVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLEENGRVAQGTIDYRGQDLTk 82
Cdd:PRK11160 333 AADQVSLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIA- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 83 lksnkDWepirgvkiatifqdPMTSLDPINTIGSQITEVI-------IKHQKKTPKEAKEMAVdyMNKVGIP---DAEKR 152
Cdd:PRK11160 406 -----DY--------------SEAALRQAISVVSQRVHLFsatlrdnLLLAAPNASDEALIEV--LQQVGLEkllEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 153 FN----EYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIaD 228
Cdd:PRK11160 465 LNawlgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-D 541
|
250 260 270
....*....|....*....|....*....|....*
gi 896625925 229 KVAVMYAGEIVEYGTVEEVFydPRHPYTWSLLSSL 263
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELL--AQQGRYYQLKQRL 574
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-246 |
2.98e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSvltkTFTGMLEENGRVAQGTIDYRGQDLTKLKSNkDWepiRGvKIATIFQDPM 105
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLD-SW---RS-RLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDpinTIGSQITeviIKHQKKTPKEAKEMA-------------VDYMNKVGipdaekrfnEYPFQYSGGMRQRIVIAI 172
Cdd:PRK10789 400 LFSD---TVANNIA---LGRPDATQQEIEHVArlasvhddilrlpQGYDTEVG---------ERGVMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 173 ALACRPDILICDEPTTALDVTIQAQIidlLKSLQQEYEFTTIFIT-HDLGVVASiADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISaHRLSALTE-ASEILVMQHGHIAQRGNHDQ 535
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
133-251 |
3.25e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 133 AKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFT 212
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
90 100 110
....*....|....*....|....*....|....*....
gi 896625925 213 TIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-233 |
5.38e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.55 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDvrDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYrgqdltklksnkd 88
Cdd:cd03221 1 IELENLSKTYG--GKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD----EGIVTW------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wepIRGVKIAtifqdpmtsldpintigsqiteviikhqkktpkeakemavdYMNkvgipdaekrfneypfQYSGGMRQRI 168
Cdd:cd03221 60 ---GSTVKIG-----------------------------------------YFE----------------QLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 169 VIAIALACRPDILICDEPTTALDVTIQAQIIDLLKslqqEYEFTTIFITHDLGVVASIADKVAVM 233
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-247 |
9.75e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEE----NGRVAQGTIDYRGQDLTKLKSNKdWEPIRGV-----KIA 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggapRGARVTGDVTLNGEPLAAIDAPR-LARLRAVlpqaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 99 TIFqdpmtSLDPINTIG----SQITEVIIKHQKKTPKEAKEMAvdymnkvgipDAEKRFNEYPFQYSGGMRQRIVIAIAL 174
Cdd:PRK13547 96 FAF-----SAREIVLLGryphARRAGALTHRDGEIAWQALALA----------GATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 175 A---------CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVE 245
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
..
gi 896625925 246 EV 247
Cdd:PRK13547 241 DV 242
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
27-250 |
1.03e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgRVAQGTIDYRGQdlTKLKSNKDWEPIRGVKIAT--IFQdp 104
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-KSAGSHIELLGR--TVQREGRLARDIRKSRANTgyIFQ-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 mtSLDPINTIgSQITEVIIKHQKKTP----------KEAKEMAVDYMNKVGIPD-AEKRFNeypfQYSGGMRQRIVIAIA 173
Cdd:PRK09984 94 --QFNLVNRL-SVLENVLIGALGSTPfwrtcfswftREQKQRALQALTRVGMVHfAHQRVS----TLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 174 LACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGeiveygtveEVFYD 250
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG---------HVFYD 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
31-252 |
1.41e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKDWEPIRgvKIATIFQDP--MTSL 108
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH----GEILFDGENIPAMSRSRLYTVRK--RMSMLFQSGalFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 109 DPINTIGSQITEviikHQKKTPKEAKEMAVDYMNKVGIPDAEKRFneyPFQYSGGMRQRIVIAIALACRPDILICDEPTT 188
Cdd:PRK11831 100 NVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 189 ALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFY--DPR 252
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPR 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-252 |
1.59e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 29 RGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEEngrVAQGTIDYRGQDLTKLKSNKdwepiRGVKIatIFQD----P 104
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LED---ITSGDLFIGEKRMNDVPPAE-----RGVGM--VFQSyalyP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLdpintigsqiteviikhqkktpkeAKEMAVDY-MNKVGIPDAEKRFNEY-------------PFQYSGGMRQRIVI 170
Cdd:PRK11000 89 HLSV------------------------AENMSFGLkLAGAKKEEINQRVNQVaevlqlahlldrkPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 171 AIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHY 224
|
..
gi 896625925 251 PR 252
Cdd:PRK11000 225 PA 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-230 |
1.59e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFDVRdKVLTAIrgvSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQdltklksnk 87
Cdd:PRK09544 4 LVSLENVSVSFGQR-RVLSDV---SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD----EGVIKRNGK--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 88 dwepirgVKIATIFQDpmTSLDPinTIGSQITEVIIKHQKktpkeakemavdyMNKVGIPDAEKRFN-----EYPFQ-YS 161
Cdd:PRK09544 67 -------LRIGYVPQK--LYLDT--TLPLTVNRFLRLRPG-------------TKKEDILPALKRVQaghliDAPMQkLS 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 162 GGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKV 230
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-239 |
1.75e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmleeNGRVAQGTIDYRGQDLTklksnkDWEPIRgvkiatIFQDP 104
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG----DPRATSGRIVFDGKDIT------DWQTAK------IMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLDPINTIGSQIT--EVIIKHQKKTPKEAKEMAVDYMNKVgIPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDILI 182
Cdd:PRK11614 82 VAIVPEGRRVFSRMTveENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-238 |
2.32e-12 |
|
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: 67.93 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 5 KNVILTARDIVVeFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEenGRVAqGTIDYRGQDLTkLK 84
Cdd:TIGR02633 254 GDVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP--GKFE-GNVFINGKPVD-IR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 85 SNKDwePIRGvKIATIFQD-PMTSLDPINTIGSQITEVIIKhqkktpKEAKEMAVDYMNKVGIPDAE-KRFN---EYPF- 158
Cdd:TIGR02633 329 NPAQ--AIRA-GIAMVPEDrKRHGIVPILGVGKNITLSVLK------SFCFKMRIDAAAELQIIGSAiQRLKvktASPFl 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 159 ---QYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYA 235
Cdd:TIGR02633 400 pigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGE 478
|
...
gi 896625925 236 GEI 238
Cdd:TIGR02633 479 GKL 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-246 |
3.74e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 18 FDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEENGRVAQGTIDYRGQDLTKlksnkdwEPIRGVKi 97
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGVKGSGSVLLNGMPIDA-------KEMRAIS- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 98 ATIFQDPMtsLDPINTIGSQIT-EVIIKHQKKTPKEAKEMAVDYM-----------NKVGIPDAEKRFneypfqySGGMR 165
Cdd:TIGR00955 102 AYVQQDDL--FIPTLTVREHLMfQAHLRMPRRVTKKEKRERVDEVlqalglrkcanTRIGVPGRVKGL-------SGGER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 166 QRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVE 245
Cdd:TIGR00955 173 KRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPD 252
|
.
gi 896625925 246 E 246
Cdd:TIGR00955 253 Q 253
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-247 |
4.31e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 21 RDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQdltklksnkdwepIRGVKIATI 100
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSP----TVGKVDRNGE-------------VSVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 101 FQDPMTSLDPIntigsqitEVIIKHQKKTPKEAKEMavdyMNKVgIPDAEkrFNEYPFQ----YSGGMRQRIVIAIALAC 176
Cdd:PRK13546 96 LSGQLTGIENI--------EFKMLCMGFKRKEIKAM----TPKI-IEFSE--LGEFIYQpvkkYSSGMRAKLGFSINITV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 177 RPDILICDEPTTALDVTIqAQiidllKSLQQEYEF-----TTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK13546 161 NPDILVIDEALSVGDQTF-AQ-----KCLDKIYEFkeqnkTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-246 |
7.46e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 12 RDIVVEFdvRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTIDYRGQDLTKLKSNkdwe 90
Cdd:PLN03130 1241 EDVVLRY--RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKFGLMDLRKV---- 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 91 pirgvkIATIFQDPMT-------SLDPINtigsqiteviiKHQKKTPKEAKEMA----VDYMNKVGIpDAEkrFNEYPFQ 159
Cdd:PLN03130 1315 ------LGIIPQAPVLfsgtvrfNLDPFN-----------EHNDADLWESLERAhlkdVIRRNSLGL-DAE--VSEAGEN 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIidlLKSLQQEYEFTTIF-ITHDLGVVASiADKVAVMYAGEI 238
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI---QKTIREEFKSCTMLiIAHRLNTIID-CDRILVLDAGRV 1450
|
....*...
gi 896625925 239 VEYGTVEE 246
Cdd:PLN03130 1451 VEFDTPEN 1458
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-238 |
4.07e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTkLKSNKDwepirGVK--IATIFQD-- 103
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT----SGYVTLDGHEVV-TRSPQD-----GLAngIVYISEDrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 --------------PMTSLDPINTIGSQIteviiKHQkktpkeAKEMAVD---YMNKVGIPDAEKRFNEYpfqySGGMRQ 166
Cdd:PRK10762 338 rdglvlgmsvkenmSLTALRYFSRAGGSL-----KHA------DEQQAVSdfiRLFNIKTPSMEQAIGLL----SGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 167 RIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-243 |
5.66e-11 |
|
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: 62.04 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 34 DLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRV--AQGTIDYRGQDLTklksnkdwepirgVKIATIFQDPMTSLDP 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIeiELDTVSYKPQYIK-------------ADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 111 INTIGSQ-ITEViikhqkktpkeakemavdyMNKVGIPDA-EKRFNEYpfqySGGMRQRIVIAIALACRPDILICDEPTT 188
Cdd:cd03237 88 DFYTHPYfKTEI-------------------AKPLQIEQIlDREVPEL----SGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 189 ALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVmYAGEIVEYGT 243
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-FEGEPSVNGV 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-230 |
6.09e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.65 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 3 QEKNVILTARDivVEFDVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTK 82
Cdd:PRK10247 2 QENSPLLQLQN--VGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT----SGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 83 LKSnkdwEPIRGvKIATIFQDPM----TSLDPIntigsqITEVIIKHQKKTPKEakeMAVDYMnKVGIPDA--EKRFNEY 156
Cdd:PRK10247 74 LKP----EIYRQ-QVSYCAQTPTlfgdTVYDNL------IFPWQIRNQQPDPAI---FLDDLE-RFALPDTilTKNIAEL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 157 pfqySGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASiADKV 230
Cdd:PRK10247 139 ----SGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-244 |
1.17e-10 |
|
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: 61.23 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 37 EGEVLALVGESGSGKSVLTKTFTGMLEENgrvaqgtidyrgqdLTKLKSNKDWEPI----RGVKIATIFQDPMT-SLDPI 111
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPN--------------LGKFDDPPDWDEIldefRGSELQNYFTKLLEgDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 112 ntIGSQITEVIIKH---------QKKTPKEAKEMAVDYMNKVGIPDAEKRfneypfQYSGGMRQRIVIAIALACRPDILI 182
Cdd:cd03236 91 --VKPQYVDLIPKAvkgkvgellKKKDERGKLDELVDQLELRHVLDRNID------QLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYaGEIVEYGTV 244
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY-GEPGAYGVV 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-247 |
2.31e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 32 SLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSNKDWEpirgvKIATIFQD---PMTSL 108
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP----LLSGERQSQFSHITRLSFEQLQK-----LVSDEWQRnntDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 109 DPINTiGSQITEVIIKHQKKTPKEAKemavdYMNKVGIPDAEKRfneyPFQY-SGGMRQRIVIAIALACRPDILICDEPT 187
Cdd:PRK10938 94 GEDDT-GRTTAEIIQDEVKDPARCEQ-----LAQQFGITALLDR----RFKYlSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 188 TALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-246 |
3.94e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTkLKSNKDWEPirgVKIATIFQDpmt 106
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA----GSILYLGKEVT-FNGPKSSQE---AGIGIIHQE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 sldpINTIGS-QITEVIIKHQKKTPK----EAKEM---AVDYMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRP 178
Cdd:PRK10762 88 ----LNLIPQlTIAENIFLGREFVNRfgriDWKKMyaeADKLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-254 |
4.05e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvAQGTIDYRGQDLTK--LKsnkdwepirgvKIATIFQD 103
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN--FTGTILANNRKPTKqiLK-----------RTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PMtsLDPINTIGSQITEV-IIKHQKKTPKEAKEMAVD-YMNKVGIPDAEKRF--NEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:PLN03211 149 DI--LYPHLTVRETLVFCsLLRLPKSLTKQEKILVAEsVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 180 ILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGT-------VEEVFYDPR 252
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKgsdamayFESVGFSPS 306
|
..
gi 896625925 253 HP 254
Cdd:PLN03211 307 FP 308
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-248 |
5.06e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 13 DIVVEFdvRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVaqgTIDyrGQDLTKLKSNKdwep 91
Cdd:PLN03232 1239 DVHLRY--RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRI---MID--DCDVAKFGLTD---- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 92 IRGVkIATIFQDPMT-------SLDPINtigsqiteviiKHQKKTPKEAKEMA----VDYMNKVGIpDAEkrFNEYPFQY 160
Cdd:PLN03232 1308 LRRV-LSIIPQSPVLfsgtvrfNIDPFS-----------EHNDADLWEALERAhikdVIDRNPFGL-DAE--VSEGGENF 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIidlLKSLQQEYEFTTIF-ITHDLGVVASiADKVAVMYAGEIV 239
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI---QRTIREEFKSCTMLvIAHRLNTIID-CDKILVLSSGQVL 1448
|
....*....
gi 896625925 240 EYGTVEEVF 248
Cdd:PLN03232 1449 EYDSPQELL 1457
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
37-241 |
5.87e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 37 EGEVLALVGESGSGKSVLTKTFTG-MLEENGRV------------------AQGTI-DYRGQDLT----KLKSNKDwepi 92
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIiyeqdlivarlqqdpprnVEGTVyDFVAEGIEeqaeYLKRYHD---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 93 rgvkiatIFQDPMTslDPINTIGSQITEV--IIKHQKKTPKEAKEMAVdyMNKVGIpDAEKRFNEYpfqySGGMRQRIVI 170
Cdd:PRK11147 104 -------ISHLVET--DPSEKNLNELAKLqeQLDHHNLWQLENRINEV--LAQLGL-DPDAALSSL----SGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 171 AIALACRPDILICDEPTTALDVTiqaqIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEY 241
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY 234
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-242 |
8.02e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmlEENGRVAQGTIDYRGQDLTKLksnkDWEPIRGVKIATIFQDPMTS 107
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLEL----SPEDRAGEGIFMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 108 LDPINTIGSQIT-EVIIKHQKKTPKEAKEMAvDYM-NKVGI----PDAEKRFNEYPFqySGGMRQRIVIAIALACRPDIL 181
Cdd:PRK09580 91 PGVSNQFFLQTAlNAVRSYRGQEPLDRFDFQ-DLMeEKIALlkmpEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 182 ICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIA-DKVAVMYAGEIVEYG 242
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-204 |
8.68e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 57.75 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTKLKsnkd 88
Cdd:TIGR01189 1 LAARNLACSRGER----MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPLAEQR---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 89 wePIRGVKIATIFQDPmtSLDPINTIGSQITEVIIKHQkktpkEAKEMAVDYMNKVGIPDAEKRfneyPF-QYSGGMRQR 167
Cdd:TIGR01189 69 --DEPHENILYLGHLP--GLKPELSALENLHFWAAIHG-----GAQRTIEDALAAVGLTGFEDL----PAaQLSAGQQRR 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 896625925 168 IVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKS 204
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-246 |
1.03e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 8 ILTARDIVVEFD-VRdkVLtaiRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSN 86
Cdd:PRK15439 11 LLCARSISKQYSgVE--VL---KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS----GTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KDWEpirgVKIATIFQDPMtsLDPINTIGSQITEVIIKHQKKTPKEAKEMA-----VDYMNKVGIPD-AEkrfneypfqy 160
Cdd:PRK15439 82 KAHQ----LGIYLVPQEPL--LFPNLSVKENILFGLPKRQASMQKMKQLLAalgcqLDLDSSAGSLEvAD---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 sggmRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVE 240
Cdd:PRK15439 146 ----RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
....*.
gi 896625925 241 YGTVEE 246
Cdd:PRK15439 221 SGKTAD 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
25-247 |
1.56e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSG--KSVLTKTFTGmlEENGRVAQGTIDYRGQDLTKLKSNKDWEPIRGVKiatifQ 102
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G--PDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GR-----R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 DPMTSLDPINTIGSQIteviikhqKKTPKEAKEMAVDYMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRPDILI 182
Cdd:NF000106 99 ESFSGRENLYMIGR*L--------DLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 183 CDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-248 |
1.81e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.96 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRD--KVLTAIrgvSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLKSnkdwEPIR 93
Cdd:PRK10790 346 VSFAYRDdnLVLQNI---NLSVPSRGFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSH----SVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 94 GvKIATIFQDPM----TSLDPInTIGSQITEVIIKHQKKTPKEAkEMAvdymnkVGIPDA-EKRFNEYPFQYSGGMRQRI 168
Cdd:PRK10790 415 Q-GVAMVQQDPVvladTFLANV-TLGRDISEEQVWQALETVQLA-ELA------RSLPDGlYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 169 VIAIALACRPDILICDEPTTALDV-TIQAqiidLLKSLQQEYEFTT-IFITHDLGVVASiADKVAVMYAGEIVEYGTVEE 246
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSgTEQA----IQQALAAVREHTTlVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
..
gi 896625925 247 VF 248
Cdd:PRK10790 561 LL 562
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-240 |
2.50e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMleenGRVAQGTIDYRGQDLTKlKSnkdwePIRGVK--IATIFQDPM 105
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV----DKRAGGEIRLNGKDISP-RS-----PLDAVKkgMAYITESRR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 -TSLDPINTIGSQITevIIKHQKK----------TPKEAKEMAVDYMNKVGIPDAEkrFNEYPFQYSGGMRQRIVIAIAL 174
Cdd:PRK09700 349 dNGFFPNFSIAQNMA--ISRSLKDggykgamglfHEVDEQRTAENQRELLALKCHS--VNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVE 240
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-240 |
3.17e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.53 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 21 RDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDltklksnkdwEPIRG----VK 96
Cdd:PRK13536 52 GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD----AGKITVLGVP----------VPARArlarAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 97 IATIFQdpMTSLDPINTIgsqiTEVIIKHQKKTPKEAKEMAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQRIVIAIALAC 176
Cdd:PRK13536 116 IGVVPQ--FDNLDLEFTV----RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 177 RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAG-EIVE 240
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGrKIAE 253
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-247 |
3.33e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 38 GEVLALVGESGSGKSVLTKTFTGMLEENGRVAQGTIDYRGQDLTKLKSNKDWEPIRGVKIATIFqdpmtsldPINTIGSQ 117
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHF--------PHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 118 ITEVIikhQKKTPKE----------AKEMAVDYM----------NKVGipdaekrfNEYPFQYSGGMRQRIVIAIALACR 177
Cdd:TIGR00956 159 LDFAA---RCKTPQNrpdgvsreeyAKHIADVYMatyglshtrnTKVG--------NDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFIT--------HDLgvvasiADKVAVMYAGEIVEYGTVEEV 247
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILD-TTPLVAiyqcsqdaYEL------FDKVIVLYEGYQIYFGPADKA 298
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-202 |
4.20e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRG-------VSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTklksnkdwEPIRGVKI 97
Cdd:PRK13539 8 LACVRGgrvlfsgLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL----PPAAGTIKLDGGDID--------DPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 98 ATI-----FQDPMTSLDPI-------NTIGSQITEVIikhqkktpkeakemavdymNKVGIPDAEKRfneyPFQY-SGGM 164
Cdd:PRK13539 76 HYLghrnaMKPALTVAENLefwaaflGGEELDIAAAL-------------------EAVGLAPLAHL----PFGYlSAGQ 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 896625925 165 RQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLL 202
Cdd:PRK13539 133 KRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-230 |
5.11e-09 |
|
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: 55.58 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 9 LTARDIVVEFDVRdkvlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVA-QGTIDYRGQDltKLKSN 86
Cdd:cd03231 1 LEADELTCERDGR----ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGRVLlNGGPLDFQRD--SIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 87 KDW---EPirGVKIATIFQDPMTSLDPINTigsqiteviikhqkktpKEAKEMAVDYMNKVGIPDAekrfneyPFQY-SG 162
Cdd:cd03231 75 LLYlghAP--GIKTTLSVLENLRFWHADHS-----------------DEQVEEALARVGLNGFEDR-------PVAQlSA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKV 230
Cdd:cd03231 129 GQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-251 |
6.99e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 12 RDIVVEFDVRDKVlTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEN------------------------GR 67
Cdd:PTZ00265 386 KNVRFHYDTRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTegdiiindshnlkdinlkwwrskiGV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 68 VAQGTI------------------------DYRGQDLTKLKSNKDWEPIRGVKIATIFQDPMTSLDPINTIGSQITEVII 123
Cdd:PTZ00265 465 VSQDPLlfsnsiknnikyslyslkdlealsNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTI 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 124 KHQKKTPKEAKEMAVDYMNkvGIPDA-EKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLL 202
Cdd:PTZ00265 545 KDSEVVDVSKKVLIHDFVS--ALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 896625925 203 KSLQQEYEFTTIFITHDLGVVaSIADKVAVMYAGEIVEYGTVEEVFYDP 251
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-238 |
7.44e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 7 VILTARDIVVefdvRDKVLTAIR---GVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEenGRvAQGTIDYRGQdltKL 83
Cdd:PRK13549 258 VILEVRNLTA----WDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GR-WEGEIFIDGK---PV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 84 KSNKDWEPIRGvKIATIFQD-PMTSLDPINTIGSQITEVIIK---HQKKTPKEAKEMAVD-YMN--KVGIPDAEKRFNey 156
Cdd:PRK13549 328 KIRNPQQAIAQ-GIAMVPEDrKRDGIVPVMGVGKNITLAALDrftGGSRIDDAAELKTILeSIQrlKVKTASPELAIA-- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 157 pfQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAG 236
Cdd:PRK13549 405 --RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
..
gi 896625925 237 EI 238
Cdd:PRK13549 482 KL 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-247 |
1.07e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQD-----LTKLKSnkdwe 90
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE----VCGGEIRVNGREigaygLRELRR----- 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 91 pirgvKIATIFQDPM-------TSLDPIntigsqiteviikhQKKTPKE---AKEMaVDYMNKV-----GIpdaEKRFNE 155
Cdd:PTZ00243 1385 -----QFSMIPQDPVlfdgtvrQNVDPF--------------LEASSAEvwaALEL-VGLRERVaseseGI---DSRVLE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 156 YPFQYSGGMRQRIVIAIALACRPDILIC-DEPTT----ALDVTIQAQIIDLLKSlqqeyeFTTIFITHDLGVVASIaDKV 230
Cdd:PTZ00243 1442 GGSNYSVGQRQLMCMARALLKKGSGFILmDEATAnidpALDRQIQATVMSAFSA------YTVITIAHRLHTVAQY-DKI 1514
|
250
....*....|....*..
gi 896625925 231 AVMYAGEIVEYGTVEEV 247
Cdd:PTZ00243 1515 IVMDHGAVAEMGSPREL 1531
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-248 |
1.16e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 30 GVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrvAQGTIDYRGQDLtklksnKDWEP-----IRG--------VK 96
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-----GQGEILLNGRPL------SDWSAaelarHRAylsqqqspPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 97 IATIFQdpmtsldpintigsqiteVIIKHQ-KKTPKEAKEMAVDYM-NKVGIPDAEKRfneyPF-QYSGGMRQRIVIAIA 173
Cdd:COG4138 83 AMPVFQ------------------YLALHQpAGASSEAVEQLLAQLaEALGLEDKLSR----PLtQLSGGEWQRVRLAAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 174 L-----ACRPD--ILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEE 246
Cdd:COG4138 141 LlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
..
gi 896625925 247 VF 248
Cdd:COG4138 220 VM 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-238 |
1.31e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 24 VLTAIRgvsLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDyrgqdLTKlksnkdwepirGVKIATIFQD 103
Cdd:PRK10636 327 ILDSIK---LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP----VSGEIG-----LAK-----------GIKLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PMTSLDPintigsqiTEVIIKHQKK-TPKEAKEMAVDYMNKVG-----IPDAEKRFneypfqySGGMRQRIVIAIALACR 177
Cdd:PRK10636 384 QLEFLRA--------DESPLQHLARlAPQELEQKLRDYLGGFGfqgdkVTEETRRF-------SGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 178 PDILICDEPTTALDVTIQAQIIDLLKslqqEYEFTTIFITHDLGVVASIADKVAVMYAGEI 238
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
160-241 |
1.53e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTiqaQIIDLLKSLQQeYEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKS-YQGTLILISHDRDFLDPIVDKIIHIEQQSLF 225
|
..
gi 896625925 240 EY 241
Cdd:PRK10636 226 EY 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-247 |
1.80e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEengrvAQGTIDYRGQDL-----TKLKSNKDW--EPIRGVKIATIFQd 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-----GSGSIQFAGQPLeawsaAELARHRAYlsQQQTPPFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 pMTSLdpintigsqiteviikHQ-KKTPKEAKEMAVDYM-NKVGIPDAEKRfneyPF-QYSGGMRQRIVIAIA-LACRPD 179
Cdd:PRK03695 89 -YLTL----------------HQpDKTRTEAVASALNEVaEALGLDDKLGR----SVnQLSGGEWQRVRLAAVvLQVWPD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 180 I------LICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEV 247
Cdd:PRK03695 148 InpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-257 |
2.12e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 2 TQEKNVILTARDIVVEFDVRDkvltAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrVAQGTIDYRGQDLT 81
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK--ILEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 82 KLksnkdwEPI----RGVKIAtiFQDPM-----TSLDPINTIGSQITeviiKHQKKTPKEAKEMAVDYMNKVGIPDAEKR 152
Cdd:CHL00131 75 DL------EPEerahLGIFLA--FQYPIeipgvSNADFLRLAYNSKR----KFQGLPELDPLEFLEIINEKLKLVGMDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 153 F-----NEypfQYSGGMRQRIVIAIALACRPDILICDEPTTALDV---TIQAQIIDLLKSLQQEYefttIFITHDLGVVA 224
Cdd:CHL00131 143 FlsrnvNE---GFSGGEKKRNEILQMALLDSELAILDETDSGLDIdalKIIAEGINKLMTSENSI----ILITHYQRLLD 215
|
250 260 270
....*....|....*....|....*....|....
gi 896625925 225 SIA-DKVAVMYAGEIVEYGTVEEVFYDPRHPYTW 257
Cdd:CHL00131 216 YIKpDYVHVMQNGKIIKTGDAELAKELEKKGYDW 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-250 |
4.01e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 26 TAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKdwEPIRGV----KIATIF 101
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----GNIIIDDEDISLLPLHA--RARRGIgylpQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 102 QDpMTSLDPINTIgSQITEVIIKHQKKtpkeakEMAVDYMNKVGIPDAEKRFNEypfQYSGGMRQRIVIAIALACRPDIL 181
Cdd:PRK10895 91 RR-LSVYDNLMAV-LQIRDDLSAEQRE------DRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 182 ICDEPTTALDvtiQAQIIDLLKSLQ--QEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYD 250
Cdd:PRK10895 160 LLDEPFAGVD---PISVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-227 |
8.07e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 38 GEVLALVGESGSGKSVLTKTFTGMLEENGRvaqgtidyrgqdltklksnkdwepirGVKIATifqdpmtsldpintigsq 117
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG--------------------------GVIYID------------------ 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 118 iteviikhqkktpkeakemAVDYMNKVGIPDAEKRFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQ 197
Cdd:smart00382 38 -------------------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*
gi 896625925 198 IIDL-----LKSLQQEYEFTTIFITHDLGVVASIA 227
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-246 |
8.36e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 3 QEK---NVILTARDIVVEFDvrDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEN-GRVA---QGTIDY 75
Cdd:PRK15064 311 QDKklhRNALEVENLTKGFD--NGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDsGTVKwseNANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 76 RGQDltklkSNKDwepirgvkiatiFQDPMTSLDPIntigsqiteviikHQKKTPKEAKEMAVDYMNKV--GIPDAEKRF 153
Cdd:PRK15064 387 YAQD-----HAYD------------FENDLTLFDWM-------------SQWRQEGDDEQAVRGTLGRLlfSQDDIKKSV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 154 NeypfQYSGGMRQRIVIAIALACRPDILICDEPTTALDVtiqaQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVM 233
Cdd:PRK15064 437 K----VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEI 508
|
250
....*....|....
gi 896625925 234 YAGEIVEY-GTVEE 246
Cdd:PRK15064 509 TPDGVVDFsGTYEE 522
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-219 |
9.98e-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: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEE-NG--RVAQG-TIDYRGQDlTKLKSNKD-WE-------PIRGV 95
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDfNGeaRPQPGiKVGYLPQE-PQLDPTKTvREnveegvaEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 96 -----KIATIFQDPMTSLDPINTIGSQITEvIIKHQKKTPKEAK-EMAVDYMNkvgIPDAEKRFNEYpfqySGGMRQRIV 169
Cdd:TIGR03719 100 ldrfnEISAKYAEPDADFDKLAAEQAELQE-IIDAADAWDLDSQlEIAMDALR---CPPWDADVTKL----SGGERRRVA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 896625925 170 IAIALACRPDILICDEPTTALDvtiqAQIIDLLKSLQQEYEFTTIFITHD 219
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-218 |
1.45e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmLEENGrvaQGTIDY-RGQDLtklksnkdwepirgvkiatIF--QDP 104
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYG---SGRIARpAGARV-------------------LFlpQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTsldPINTIGSQITeviikhqkkTPKEAKEM----AVDYMNKVGIPDAEKRFN-EYPFQY--SGGMRQRIVIAIALACR 177
Cdd:COG4178 436 YL---PLGTLREALL---------YPATAEAFsdaeLREALEAVGLGHLAERLDeEADWDQvlSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896625925 178 PDILICDEPTTALDVTIQAQiidLLKSLQQEYEFTT-IFITH 218
Cdd:COG4178 504 PDWLFLDEATSALDEENEAA---LYQLLREELPGTTvISVGH 542
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
161-291 |
1.46e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.50 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVE 240
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIA 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 241 YGTVEEVF-----------YDPRHPYTWSLLSSLPQLADDKGE-LYSIPGTPPSLYSQLQGDA 291
Cdd:PRK13537 219 EGAPHALIeseigcdvieiYGPDPVALRDELAPLAERTEISGEtLFCYVRDPEPLHARLKGRA 281
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-219 |
1.54e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 16 VEFDVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQGTidyrgqdltKLKsnkdwepirg 94
Cdd:PRK11147 325 VNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQaDSGRIHCGT---------KLE---------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 95 vkIAtIFQDPMTSLDPINTI------GSQitEVIIKHQKK-----------TPKEAkemavdyMNKVGipdaekrfneyp 157
Cdd:PRK11147 384 --VA-YFDQHRAELDPEKTVmdnlaeGKQ--EVMVNGRPRhvlgylqdflfHPKRA-------MTPVK------------ 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 158 fQYSGGMRQRIVIAiALACRP-DILICDEPTTALDVtiqaQIIDLLKSLQQEYEFTTIFITHD 219
Cdd:PRK11147 440 -ALSGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-232 |
2.35e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 37 EGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQG-TIDYRGQdltKLKSNKDwepirgvkiatifqdpMTSLDPINTI 114
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKpDEGEVDPElKISYKPQ---YIKPDYD----------------GTVEDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 115 GSQITEVIIKHqkktpkeakemavDYMNKVGIPDA-EKRFNEYpfqySGGMRQRIVIAIALACRPDILICDEPTTALDVT 193
Cdd:PRK13409 425 TDDLGSSYYKS-------------EIIKPLQLERLlDKNVKDL----SGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190
....*....|....*....|....*....|....*....
gi 896625925 194 IQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAV 232
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-243 |
2.56e-07 |
|
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: 52.71 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaQGTIDYRGQDLTklksnkdwepirgvkiatifqdpmT 106
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT----SGTVLVGGKDIE------------------------T 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 107 SLDPI-NTIGSQITEVIIKH--------------QKKTPKEAKEMAVDYMNKVGIpdAEKRfNEYPFQYSGGMRQRIVIA 171
Cdd:TIGR01257 997 NLDAVrQSLGMCPQHNILFHhltvaehilfyaqlKGRSWEEAQLEMEAMLEDTGL--HHKR-NEEAQDLSGGMQRKLSVA 1073
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896625925 172 IALACRPDILICDEPTTALDVTIQAQIIDLLksLQQEYEFTTIFITHDLGVVASIADKVAVMYAGEIVEYGT 243
Cdd:TIGR01257 1074 IAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-239 |
2.72e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGMleenGRVAQGTIDYRGQDLtKLKSNKDwePIR-GV-------KIATIFq 102
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGA----TRRTAGQVYLDGKPI-DIRSPRD--AIRaGImlcpedrKAEGII- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 103 dPMTSL-DPINtIGSQiteviiKHQKK-----TPKEAKEMAVDYMNKVGI--PDAEKRFNeypfQYSGGMRQRIVIAIAL 174
Cdd:PRK11288 344 -PVHSVaDNIN-ISAR------RHHLRagcliNNRWEAENADRFIRSLNIktPSREQLIM----NLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 175 ACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
156-218 |
4.26e-07 |
|
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: 49.07 E-value: 4.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 156 YPFQ--YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKslqqEYEFTTIFITH 218
Cdd:cd03223 86 YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-244 |
5.48e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 37 EGEVLALVGESGSGKSVLTKTFTGMLEEN-GRV-AQGTID-----YRG---QD-LTKLKSNKdwepIRgvkiatifqdpm 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlGDYdEEPSWDevlkrFRGtelQDyFKKLANGE----IK------------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 TSLDPintigsQITEVIIKHQKKTPKEA------KEMAVDYMNKVGI-PDAEKRFNEYpfqySGGMRQRIVIAIALACRP 178
Cdd:COG1245 162 VAHKP------QYVDLIPKVFKGTVRELlekvdeRGKLDELAEKLGLeNILDRDISEL----SGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYaGEIVEYGTV 244
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDLAILDYLADYVHILY-GEPGVYGVV 295
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-232 |
6.15e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 37 EGEVLALVGESGSGKSVLTKTFTGMLE-ENGRVAQG-TIDYRGQdltKLKSNKDwEPIRGVkIATIFQDPMTSldpinti 114
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKpDEGEVDEDlKISYKPQ---YISPDYD-GTVEEF-LRSANTDDFGS------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 115 gSQITEVIIKHqkktpkeakeMAVDYMnkvgipdAEKRFNEYpfqySGGMRQRIVIAIALACRPDILICDEPTTALDVTI 194
Cdd:COG1245 433 -SYYKTEIIKP----------LGLEKL-------LDKNVKDL----SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 896625925 195 QAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAV 232
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-245 |
7.01e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEENGrvaqGTIDYRGQDLTKLKSNKD--------WEPIRGVKIA 98
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA----GTITLHGKKINNHNANEAinhgfalvTEERRSTGIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 99 TIFQDPMTSLdpINTIGSQITEVIIKHQKKTpKEAKEMAVDYMNkVGIPDAEKRFNeypfQYSGGMRQRIVIAIALACRP 178
Cdd:PRK10982 339 AYLDIGFNSL--ISNIRNYKNKVGLLDNSRM-KSDTQWVIDSMR-VKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896625925 179 DILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIVeyGTVE 245
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA--GIVD 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-244 |
9.15e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 35 LIEGEVLALVGESGSGKSVLTKTFTGMLEENgrvaqgtidyrgqdLTKLKSNKDWEPI----RGVKIATIFQDpmtsldp 110
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN--------------LGDYEEEPSWDEVlkrfRGTELQNYFKK------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 111 inTIGSQITeVIIKHQ--KKTPKEAKEMAVDYMNKVgipDAEKRFNEY------------PFQY-SGGMRQRIVIAIALA 175
Cdd:PRK13409 155 --LYNGEIK-VVHKPQyvDLIPKVFKGKVRELLKKV---DERGKLDEVverlglenildrDISElSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 176 CRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYefTTIFITHDLGVVASIADKVAVMYaGEIVEYGTV 244
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY-GEPGAYGVV 294
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
161-243 |
9.25e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASIADKVAVMYaGEIVE 240
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEPGV 151
|
...
gi 896625925 241 YGT 243
Cdd:cd03222 152 YGI 154
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-248 |
1.08e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 31 VSLDLIEGEVLALVGESGSGKSVLTKTFTGML---EENGRVAQGTIDYRGQDL----TKLKSN----KDWEPIRGVKI-- 97
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELshaETSSVVIRGSVAYVPQVSwifnATVRENilfgSDFESERYWRAid 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 98 ATIFQDPMTSLDpintiGSQITEViikhqkktpkeakemavdymnkvgipdAEKRFNeypfqYSGGMRQRIVIAIALACR 177
Cdd:PLN03232 716 VTALQHDLDLLP-----GRDLTEI---------------------------GERGVN-----ISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 178 PDILICDEPTTALDVTIQAQIID--LLKSLQQEyefTTIFITHDLGVVASIaDKVAVMYAGEIVEYGTVEEVF 248
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDscMKDELKGK---TRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
161-246 |
1.08e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDllKSLQQEYEFTT-IFITHDLGVVASIaDKVAVMYAGEIV 239
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELRGKTrVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
....*..
gi 896625925 240 EYGTVEE 246
Cdd:PLN03130 819 EEGTYEE 825
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
158-234 |
1.14e-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: 47.74 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 158 FQYSGGMRQRIVIAIALA---CRPDILIC-DEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGvVASIADKVAVM 233
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPE-LAELADKLIHI 153
|
.
gi 896625925 234 Y 234
Cdd:cd03227 154 K 154
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-247 |
1.58e-06 |
|
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: 50.29 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 24 VLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQdlTKLKSNKDWEPIRGVKIATIFQd 103
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP----SEGKIKHSGR--ISFSPQTSWIMPGTIKDNIIFG- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 pmTSLDPIntigsQITEVIikhqkKTPKEAKEMAVdYMNKVGIPdaekrFNEYPFQYSGGMRQRIVIAIALACRPDILIC 183
Cdd:TIGR01271 511 --LSYDEY-----RYTSVI-----KACQLEEDIAL-FPEKDKTV-----LGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896625925 184 DEPTTALDVTIQAQIID--LLKSLQQEyefTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEV 247
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
38-256 |
1.98e-06 |
|
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: 48.37 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 38 GEVLALVGESGSGKSVLTKTFTGMLEengrVAQGTIDYRGQDLTKLksnkdwePIRGVK--IATIFQDPMT-------SL 108
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKL-------PLHTLRsrLSIILQDPILfsgsirfNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 109 DPINT-IGSQITEVIIKHQKKTPKEAKEMAVDYMnkvgipdaekrFNEYPFQYSGGMRQRIVIAIALACRPDILICDEPT 187
Cdd:cd03288 116 DPECKcTDDRLWEALEIAQLKNMVKSLPGGLDAV-----------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 188 TALDVTIQAQiidLLKSLQQEY-EFTTIFITHDLGVVASiADKVAVMYAGEIVEYGTVEEVFYDPRHPYT 256
Cdd:cd03288 185 ASIDMATENI---LQKVVMTAFaDRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-247 |
2.35e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.31 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQdlTKLKSNKDW---EPIRGVKIATIFQDP 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEP----SEGKIKHSGR--ISFSSQFSWimpGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 105 MTSLDPINtiGSQITEVIIKHQKKtpkeakemavDYmnkvgIPDAEKRFNeypfqYSGGMRQRIVIAIALACRPDILICD 184
Cdd:cd03291 127 YRYKSVVK--ACQLEEDITKFPEK----------DN-----TVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 185 EPTTALDVTIQAQIID--LLKSLQQEyefTTIFITHDLGVVaSIADKVAVMYAGEIVEYGTVEEV 247
Cdd:cd03291 185 SPFGYLDVFTEKEIFEscVCKLMANK---TRILVTSKMEHL-KKADKILILHEGSSYFYGTFSEL 245
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-248 |
2.46e-06 |
|
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: 49.56 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEE-NGRVA-QGTIDYRGQDltklksnkdwepirgvkiATIFQDpm 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKvEGHVHmKGSVAYVPQQ------------------AWIQND-- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 tSLDPINTIGSQITEviiKHQKKTPKEAKEMAVDYMnkvgIPDAEK-RFNEYPFQYSGGMRQRIVIAIALACRPDILICD 184
Cdd:TIGR00957 714 -SLRENILFGKALNE---KYYQQVLEACALLPDLEI----LPSGDRtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 185 EPTTALDVTIQAQIID-------LLKSLqqeyefTTIFITHDLGVVASIaDKVAVMYAGEIVEYGTVEEVF 248
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEhvigpegVLKNK------TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-247 |
2.48e-06 |
|
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: 49.56 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 28 IRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEEngrvAQGTIDYRGQDLTKLKSNKdwepIRgVKIATIFQDPM-- 105
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES----AEGEIIIDGLNIAKIGLHD----LR-FKITIIPQDPVlf 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 106 -----TSLDPINTIGSQitEVIIkhqkktpkeAKEMAVDYMNKVGIPDA-EKRFNEYPFQYSGGMRQRIVIAIALACRPD 179
Cdd:TIGR00957 1373 sgslrMNLDPFSQYSDE--EVWW---------ALELAHLKTFVSALPDKlDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 180 ILICDEPTTALDVTIQaqiiDLLKS-LQQEYEFTTIF-ITHDLGVVASIAdKVAVMYAGEIVEYGTVEEV 247
Cdd:TIGR00957 1442 ILVLDEATAAVDLETD----NLIQStIRTQFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-240 |
4.66e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 27 AIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGmleeNGRVAQGTIDYRGQDLtKLKSNKDwepIRGVKIATIFQD--- 103
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSG----NYQPDAGSILIDGQEM-RFASTTA---ALAAGVAIIYQElhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 -P-MTSLDPI------NTIGsqiteVIIKhqkktpKEAKEMAVDYMNKVGI---PDAekrfneyPFQY-SGGMRQRIVIA 171
Cdd:PRK11288 91 vPeMTVAENLylgqlpHKGG-----IVNR------RLLNYEAREQLEHLGVdidPDT-------PLKYlSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 172 IALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASIADKVAVMYAGEIVE 240
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-248 |
6.32e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEFTTIFITHDlgvVASI--ADKVAVM----Y 234
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR---IASIkrSDKIVVFnnpdR 1436
|
90
....*....|....*
gi 896625925 235 AGEIVE-YGTVEEVF 248
Cdd:PTZ00265 1437 TGSFVQaHGTHEELL 1451
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
161-237 |
7.73e-06 |
|
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: 46.31 E-value: 7.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIID--LLKSLQQEYefTTIFITHDLGVVaSIADKVAVMYAGE 237
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
161-230 |
1.21e-05 |
|
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: 45.68 E-value: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 161 SGGmrQRIVIAIALAC--------RPDILICDEPTTALDV-TIQAQIIDLLKSLQQEYEFTTIFITHDLGVVASiADKV 230
Cdd:cd03240 117 SGG--EKVLASLIIRLalaetfgsNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA-ADHI 192
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
160-249 |
1.28e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 160 YSGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyEFTTIFITHDLGVVASIADKVAVMYAGEIV 239
Cdd:TIGR01257 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
90
....*....|
gi 896625925 240 EYGTVEEVFY 249
Cdd:TIGR01257 2150 CLGTIQHLKS 2159
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-236 |
1.59e-05 |
|
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: 45.40 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 25 LTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLEE-NGRVaqgtidYRGQDLTKLKSNKDWEPIRGVKIATIFQD 103
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlEGKV------HWSNKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 104 PM---TSLDPINTIGSQITeviiKHQKKTPKEAKEMAVDyMNKVGIPDaEKRFNEYPFQYSGGMRQRIVIAIALACRPDI 180
Cdd:cd03290 88 PWllnATVEENITFGSPFN----KQRYKAVTDACSLQPD-IDLLPFGD-QTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 896625925 181 LICDEPTTALDVTIQAQIID--LLKSLQQEYEfTTIFITHDLGVVASiADKVAVMYAG 236
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
165-205 |
3.60e-05 |
|
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: 44.16 E-value: 3.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 896625925 165 RQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSL 205
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-219 |
4.36e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 43 LVGESGSGKSVLTKTFTGMLE-ENGRVAQgtidyrgqdltklksnkdwEPirGVKIATIFQDP-----MTSLDpintigs 116
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEpSAGNVSL-------------------DP--NERLGKLRQDQfafeeFTVLD------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 117 qitEVIIKHQK----KTPKEA----KEMA-VDYMnKVGipDAEKRFNEY------------------PF-QYSGGMRQ-- 166
Cdd:PRK15064 84 ---TVIMGHTElwevKQERDRiyalPEMSeEDGM-KVA--DLEVKFAEMdgytaearagelllgvgiPEeQHYGLMSEva 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896625925 167 -----RIVIAIALACRPDILICDEPTTALDvtiqaqiIDLLKSLQQ---EYEFTTIFITHD 219
Cdd:PRK15064 158 pgwklRVLLAQALFSNPDILLLDEPTNNLD-------INTIRWLEDvlnERNSTMIIISHD 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
163-246 |
5.12e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 163 GMRQRIVIAIALACRPDILICDEPTT-----ALDVTIQaQIIDLlkSLQQEyefTTIFI-THDLGvVASIADKVAVMYAG 236
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSgvdpvARDMFWR-LLIEL--SREDG---VTIFIsTHFMN-EAERCDRISLMHAG 473
|
90
....*....|
gi 896625925 237 EIVEYGTVEE 246
Cdd:NF033858 474 RVLASDTPAA 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
161-219 |
5.36e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 5.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896625925 161 SGGMRQRIviaiALaCR-----PDILICDEPTTALDvtiqAQIIDLLKSLQQEYEFTTIFITHD 219
Cdd:PRK11819 165 SGGERRRV----AL-CRlllekPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
161-247 |
1.23e-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: 43.85 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACR---PDILICDEPTTAL---DVtiqAQIIDLLKSLQQEYEfTTIFITHDLGVVASiADKVAVM- 233
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVIKT-ADYIIDLg 905
|
90
....*....|....*....
gi 896625925 234 -----YAGEIVEYGTVEEV 247
Cdd:TIGR00630 906 peggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
161-242 |
1.72e-04 |
|
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: 41.92 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPD--ILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVASiADKVAVM----- 233
Cdd:cd03238 89 SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSS-ADWIIDFgpgsg 166
|
90
....*....|
gi 896625925 234 -YAGEIVEYG 242
Cdd:cd03238 167 kSGGKVVFSG 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
159-192 |
1.84e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.84e-04
10 20 30
....*....|....*....|....*....|....
gi 896625925 159 QYSGGMRQRIVIAIALACRPDILICDEPTTALDV 192
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
161-247 |
5.45e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDVTIQAQIIDLLKSLQQEyefttifiTHDLGVVASIA--------DKVAV 232
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE--------RPGMSVLVATAymeeaerfDWLVA 209
|
90
....*....|....*
gi 896625925 233 MYAGEIVEYGTVEEV 247
Cdd:NF033858 210 MDAGRVLATGTPAEL 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
161-239 |
6.55e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 161 SGGMRQRIVIAIALACRPDILICDEPTTALDV-------TIQAQIIDLLKSLqqeyefttIFITHDLGVVASIADKVAVM 233
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyeiyTIINELAAEGKGV--------IVISSELPELLGMCDRIYVM 477
|
....*.
gi 896625925 234 YAGEIV 239
Cdd:NF040905 478 NEGRIT 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-205 |
9.09e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 12 RDIVVEFDVRDKVLTAIRGVSLDLIEGEVLALVGESGSGKSVLTKTF-----TGMLEE-----NGRVAQGT----IDY-R 76
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVITGgdrlvNGRPLDSSfqrsIGYvQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896625925 77 GQDLTKLKSNkdwepirgVKIATIFQDPMtsldpintigsqiteviiKHQKKTPKEAKEMAVDYMNK-----------VG 145
Cdd:TIGR00956 843 QQDLHLPTST--------VRESLRFSAYL------------------RQPKSVSKSEKMEYVEEVIKllemesyadavVG 896
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896625925 146 IP----DAEKRfneypfqysggmrQRIVIAIALACRPDILI-CDEPTTALDVTIQAQIIDLLKSL 205
Cdd:TIGR00956 897 VPgeglNVEQR-------------KRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-82 |
1.99e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.78 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896625925 14 IVVEFDVRDKVLtaIRGVSLDLIEGEVLALVGESGSGKSVLTKTFTGMLeengRVAQGTIDYRGQDLTK 82
Cdd:PRK13540 5 IELDFDYHDQPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL----NPEKGEILFERQSIKK 67
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
161-230 |
3.99e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 3.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896625925 161 SGGMRQRIVIAIALAC---RPDILICDEPTTALDVTIQAQIIDLLKSLQQEYEfTTIFITHDLGVVaSIADKV 230
Cdd:PRK00635 811 SGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVV-KVADYV 881
|
|
| |
