|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-328 |
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: 505.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeITRGEVIFKGRDLLALPPEA 87
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQRV 167
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 248 DRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPPLSARPVGCAFHPRCDRATDICHRAEPPDTAGPAGRRWRCHHPLPEA 327
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEEA 319
|
.
gi 1208293942 328 A 328
Cdd:COG0444 320 P 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-291 |
1.34e-134 |
|
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: 392.90 E-value: 1.34e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRDLLALPP 85
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQ 165
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1208293942 246 VLDRPRHPYTRGLLNSVPgdtaRGERLRQIEGTAPPLSARPVGCAF 291
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEP----RGDPRPVPPDAPPLLEARDLKVWF 285
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-326 |
9.67e-122 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 352.88 E-value: 9.67e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRAPVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITrGEVIFKGRDL 80
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG-GSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALPPEAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFS 160
Cdd:PRK09473 84 LNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 241 GATDDVLDRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPPLSARPVGCAFHPRCDRATDICHRAePPDTAGPAGRRWRC 320
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSA-PPLEEFGPGRLRAC 322
|
....*.
gi 1208293942 321 HHPLPE 326
Cdd:PRK09473 323 FKPVEE 328
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-329 |
2.36e-117 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 341.71 E-value: 2.36e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 4 DRAPVLEVRNLQTVFHDLRGAWP-------ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFK 76
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE----EPTSGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 77 GRDLLALPPEAQRRLRgSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItSPETrLSQYP 156
Cdd:COG4608 79 GQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGL-RPEH-ADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGD 236
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 237 IVEIGATDDVLDRPRHPYTRGLLNSVP--GDTARGERLRqIEGTAP-PLSaRPVGCAFHPRCDRATDICHRAEPPDTAGP 313
Cdd:COG4608 236 IVEIAPRDELYARPLHPYTQALLSAVPvpDPERRRERIV-LEGDVPsPLN-PPSGCRFHTRCPYAQDRCATEEPPLREVG 313
|
330
....*....|....*.
gi 1208293942 314 AGRRWRCHHPLPEAAA 329
Cdd:COG4608 314 PGHQVACHLAEEGSGV 329
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-327 |
2.87e-112 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 328.62 E-value: 2.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRDLLALPPEA 87
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQRV 167
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 248 DRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPPLSARPVGCAFHPRCDRATDICHRAEpPDTAGPAGRRWRCHHPLPEA 327
Cdd:PRK11022 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEE-PALNMLAGRQSKCHYPLDDA 321
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-241 |
3.15e-111 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 322.15 E-value: 3.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvdrpGEITRGEVIFKGRDLLALPpEA 87
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL----LKPTSGSIIFDGKDLLKLS-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIdSLRRVGITSPETRLSQYPHEFSGGMRQRV 167
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-264 |
7.50e-104 |
|
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: 313.76 E-value: 7.50e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRAPVLEVRNLQTVFHDLRGAW-PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRD 79
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL----RPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 80 LLALPPEAQRRLRGSaLAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEF 159
Cdd:COG1123 329 LTKLSRRSLRELRRR-VQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGL--PPDLADRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
250 260
....*....|....*....|....*
gi 1208293942 240 IGATDDVLDRPRHPYTRGLLNSVPG 264
Cdd:COG1123 486 DGPTEEVFANPQHPYTRALLAAVPS 510
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-294 |
5.13e-97 |
|
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: 296.04 E-value: 5.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITrGEVIFKGRDLLALPP 85
Cdd:COG1123 2 TPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 eaqrRLRGSALAMIFQDPLTTLNPVlTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQ 165
Cdd:COG1123 79 ----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEA-LENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1208293942 246 VLDRPRhpytrgLLNSVPGDTARGERLRQIEGTAPP-LSARPVGCAFHPR 294
Cdd:COG1123 230 ILAAPQ------ALAAVPRLGAARGRAAPAAAAAEPlLEVRNLSKRYPVR 273
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-263 |
9.91e-95 |
|
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: 290.82 E-value: 9.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 4 DRAPVLEVRNLQTVFHDLRGAW-------PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeiTRGEVIFK 76
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 77 GRDLLALPPEAQRRLRgSALAMIFQDPLTTLNPVLTIGEQMAEAILEHAR-VAPAEVRRRCIDSLRRVGItSPETRlSQY 155
Cdd:COG4172 346 GQDLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGL-DPAAR-HRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 156 PHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:COG4172 423 PHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
250 260
....*....|....*....|....*...
gi 1208293942 236 DIVEIGATDDVLDRPRHPYTRGLLNSVP 263
Cdd:COG4172 503 KVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-307 |
4.00e-94 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 282.75 E-value: 4.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRAPVLEVRNLQTVFhDLRG--AWP--------ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITR 70
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHF-DIKDgkQWFwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 71 GEVIFKGRDLLALPPEAQRRLRgSALAMIFQDPLTTLNPVLTIGEQMAEAILE-HARVAPAEVRRRCIDSLRRVGITspE 149
Cdd:PRK15079 76 GEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLL--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 150 TRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRI 229
Cdd:PRK15079 153 NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 230 AVMYAGDIVEIGATDDVLDRPRHPYTRGLLNSVPGDTARGERLRQI---EGTAPPLSARPVGCAFHPRCDRATDICHRAE 306
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIqllEGELPSPINPPSGCVFRTRCPIAGPECAKTR 312
|
.
gi 1208293942 307 P 307
Cdd:PRK15079 313 P 313
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-324 |
2.74e-91 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 275.63 E-value: 2.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRDLLALPPE 86
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEH-------ARvaPAEVRRRCIDSLRRVGITSPETRLSQYPHEF 159
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWtfkgkwwQR--FKWRKKRAIELLHRVGIKDHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 240 IGATDDVLDRPRHPYTRGLLNSVP---GDTARGERLRQIEGTAPPLSARPVGCAFHPRCDRATDIChrAEPPDTAGPAGR 316
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPdfrQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKC--VETPRLRKIKGH 317
|
....*...
gi 1208293942 317 RWRCHHPL 324
Cdd:COG4170 318 EFACHFPL 325
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-322 |
3.98e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 274.92 E-value: 3.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRGAWP------ALNGLSLTLHAGEVLGLVGESGSGKSVAGfSILGLVDRPgeiTRGEVIFKGRD 79
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIETP---TGGELYYQGQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 80 LLALPPEAQRRLRgSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItSPEtRLSQYPHEF 159
Cdd:PRK11308 79 LLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPE-HYDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 240 IGATDDVLDRPRHPYTRGLLNSVPG--DTARGERLRqIEGTAP-PLSArPVGCAFHPRCDRATDIChRAEPPDTAGPAGR 316
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLSATPRlnPDDRRERIK-LTGELPsPLNP-PPGCAFNARCPRAFGRC-RQEQPQLRDYDGR 312
|
....*.
gi 1208293942 317 RWRCHH 322
Cdd:PRK11308 313 LVACFA 318
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-291 |
3.10e-83 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 261.18 E-value: 3.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPG-EITRGEVIFKGRDLLALPP 85
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPvVYPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQ 165
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1208293942 246 VLDRPRHPYTRGLLNSVPgdtaRGERLRQIEGTAPPLSARPVGCAF 291
Cdd:PRK15134 244 LFSAPTHPYTQKLLNSEP----SGDPVPLPEPASPLLDVEQLQVAF 285
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-264 |
1.71e-81 |
|
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: 247.41 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLE-RP---WSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgsALAMIFQDPLTTLNPVLTIGEQMAEAILEHARvapAEVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMRQRVA 168
Cdd:COG1124 78 RR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGL---PDREERIAELLEQVGL--PPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*.
gi 1208293942 249 RPRHPYTRGLLNSVPG 264
Cdd:COG1124 229 GPKHPYTRELLAASLA 244
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-259 |
1.36e-79 |
|
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: 241.89 E-value: 1.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 30 GLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRDLLALppeaqrRLRGSALAMIFQDPLTTLNP 109
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 110 VLTIGEQMAEAILEHARVApAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTAL 189
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLS-KQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 190 DVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLL 259
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLL 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-281 |
3.47e-76 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 245.15 E-value: 3.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 4 DRAPVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPG-EITRGEVIFKGR---- 78
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLRRRsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 79 -DLLALPPEAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPH 157
Cdd:PRK10261 88 iELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1208293942 238 VEIGATDDVLDRPRHPYTRGLLNSVPgdtargeRLRQIEGTAPP 281
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVP-------QLGAMKGLDYP 284
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-262 |
1.55e-73 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 227.77 E-value: 1.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRAPVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGR-- 78
Cdd:COG4107 1 MTNEEQPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPTSGSVYYRDRdg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 79 ---DLLALPPEAQRRLRGSALAMIFQDPLTTLNPVLT----IGEQMAEAILEHArvapAEVRRRCIDSLRRVGItsPETR 151
Cdd:COG4107 77 gprDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSaggnIAERLMAAGERHY----GDIRARALEWLERVEI--PLER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 152 LSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAV 231
Cdd:COG4107 151 IDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMV 230
|
250 260 270
....*....|....*....|....*....|.
gi 1208293942 232 MYAGDIVEIGATDDVLDRPRHPYTRGLLNSV 262
Cdd:COG4107 231 MKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-324 |
4.65e-73 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 228.92 E-value: 4.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRDLLALPPE 86
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVR-----RRCIDSLRRVGITSPETRLSQYPHEFSG 161
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRfgwrkRRAIELLHRVGIKDHKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 242 ATDDVLDRPRHPYTRGLLNSVPgDTARG----ERLRQIEGTAPPLSARPVGCAFHPRCDRATDIChrAEPPDTAGPAGRR 317
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIP-DFGSAmphkSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQREC--IETPRLTGAKNHL 318
|
....*..
gi 1208293942 318 WRCHHPL 324
Cdd:PRK15093 319 YACHFPL 325
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-261 |
4.20e-64 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 203.53 E-value: 4.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDlRGAWP------ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDL 80
Cdd:COG4167 3 ALLEVRNLSKTFKY-RTGLFrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGII----EPTSGEILINGHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LalPPEAQRRLRgsALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItSPEtRLSQYPHEFS 160
Cdd:COG4167 78 E--YGDYKYRCK--HIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGL-LPE-HANFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250 260
....*....|....*....|.
gi 1208293942 241 GATDDVLDRPRHPYTRGLLNS 261
Cdd:COG4167 232 GKTAEVFANPQHEVTKRLIES 252
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-239 |
2.24e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 195.26 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPP 85
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL-LNILGGLDRP---TSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGSALAMIFQDPltTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQ 165
Cdd:COG1136 78 RELARLRRRHIGFVFQFF--NLLPELTALENVALP-LLLAGVSRKERRERARELLERVGL---GDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLgVVAELADRIAVMYAGDIVE 239
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-237 |
1.49e-60 |
|
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: 192.70 E-value: 1.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDRP---TSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGSALAMIFQDPltTLNPVLTIGEQmAEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVA 168
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTALEN-VELPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLgVVAELADRIAVMYAGDI 237
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-259 |
1.50e-60 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 201.86 E-value: 1.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRAPVLEVRNLQTVFHDLRGAWP-------ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeiTRGEV 73
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-----SQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 74 IFKGRDLLALPPEAQRRLRgSALAMIFQDPLTTLNPVLTIGEQMAEAI-LEHARVAPAEVRRRCIDSLRRVGItSPETRl 152
Cdd:PRK15134 343 WFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGL-DPETR- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 153 SQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVM 232
Cdd:PRK15134 420 HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
250 260
....*....|....*....|....*..
gi 1208293942 233 YAGDIVEIGATDDVLDRPRHPYTRGLL 259
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-263 |
1.68e-59 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 201.24 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhDLRGAW--------PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeitrGEVIFKGR 78
Cdd:PRK10261 312 PILQVRNLVTRF-PLRSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 79 DLLALPPEAQRRLRGSaLAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItSPETRLsQYPHE 158
Cdd:PRK10261 387 RIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAW-RYPHE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
250 260
....*....|....*....|....*
gi 1208293942 239 EIGATDDVLDRPRHPYTRGLLNSVP 263
Cdd:PRK10261 544 EIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-259 |
2.17e-54 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 178.35 E-value: 2.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQtvfhdLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRdllalpPEA 87
Cdd:PRK10418 4 QIELRNIA-----LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGK------PVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCidsLRRVGITSPETRLSQYPHEFSGGMRQRV 167
Cdd:PRK10418 73 PCALRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAA---LEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|..
gi 1208293942 248 DRPRHPYTRGLL 259
Cdd:PRK10418 230 NAPKHAVTRSLV 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-262 |
6.51e-54 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 177.04 E-value: 6.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRGawpaLNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGR-----DL 80
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLAPDAGEVHYRMRdgqlrDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALPPEAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFS 160
Cdd:PRK11701 76 YALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEI--DAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|..
gi 1208293942 241 GATDDVLDRPRHPYTRGLLNSV 262
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSSV 255
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-254 |
2.16e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 178.75 E-value: 2.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 5 RAPVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRD 79
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTtllrmIAGF------ETP---DSGRILLDGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 80 LLALPPEaQRRLrgsalAMIFQDPLttLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEF 159
Cdd:COG3842 69 VTGLPPE-KRNV-----GMVFQDYA--LFPHLTVAENVAFG-LRMRGVPKAEIRARVAELLELVGLEGLADR---YPHQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
250
....*....|....*
gi 1208293942 240 IGATDDVLDRPRHPY 254
Cdd:COG3842 217 VGTPEEIYERPATRF 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-281 |
1.15e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLV---DRPgeiTRGEVIFKGRDLLALPP 85
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCInllERP---TSGSVLVDGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGSaLAMIFQDPlttlNpvL----TIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSG 161
Cdd:COG1135 75 RELRAARRK-IGMIFQHF----N--LlssrTVAENVALP-LEIAGVPKAEIRKRVAELLELVGLSD---KADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1208293942 242 ATDDVLDRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPP 281
Cdd:COG1135 224 PVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGG 263
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-256 |
1.26e-51 |
|
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: 170.55 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 4 DRAPVLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLAL 83
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL-RP---DSGEILVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEAQRRLR--------GSALamiFQDplttlnpvLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItsPETRlSQY 155
Cdd:COG1127 73 SEKELYELRrrigmlfqGGAL---FDS--------LTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL--PGAA-DKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 156 PHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250 260
....*....|....*....|.
gi 1208293942 236 DIVEIGATDDVLDRPrHPYTR 256
Cdd:COG1127 219 KIIAEGTPEELLASD-DPWVR 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-251 |
1.42e-51 |
|
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: 170.45 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEA 87
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLERP---TSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRgSALAMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRV 167
Cdd:cd03258 77 LRKAR-RRIGMIFQH--FNLLSSRTVFENVALP-LEIAGVPKAEIEERVLELLELVGL---EDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
....
gi 1208293942 248 DRPR 251
Cdd:cd03258 230 ANPQ 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-241 |
7.09e-51 |
|
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: 167.70 E-value: 7.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRDLLAL 83
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTtllrlIAGL------ERP---DSGEILIDGRDVTGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEaQRRLrgsalAMIFQDPltTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGM 163
Cdd:cd03259 68 PPE-RRNI-----GMVFQDY--ALFPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-256 |
8.44e-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: 165.75 E-value: 8.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL-RP---DSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRgSALAMIFQDPltTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVA 168
Cdd:cd03261 73 YRLR-RRMGMLFQSG--ALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL---RGAEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*...
gi 1208293942 249 RPrHPYTR 256
Cdd:cd03261 227 SD-DPLVR 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-257 |
3.49e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 164.88 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTrDRAPVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIF 75
Cdd:COG1116 1 MS-AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKStllrlIAGL------EKP---TSGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 76 KGRDLLALPPEaqrrlrgsaLAMIFQDPltTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqY 155
Cdd:COG1116 71 DGKPVTGPGPD---------RGVVFQEP--ALLPWLTVLDNVALG-LELRGVPKAERRERARELLELVGLAGFEDA---Y 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 156 PHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVtiqgQIIAEMQ----ALQRETGTAMIWITHDlgvVAE---LADR 228
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDA----LTRERLQdellRLWQETGKTVLFVTHD---VDEavfLADR 208
|
250 260 270
....*....|....*....|....*....|
gi 1208293942 229 IAVMyAGDIVEIGATDDV-LDRPRHPYTRG 257
Cdd:COG1116 209 VVVL-SARPGRIVEEIDVdLPRPRDRELRT 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-263 |
4.54e-49 |
|
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: 165.12 E-value: 4.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQD 102
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:cd03294 111 --FALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLLNSV 262
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
.
gi 1208293942 263 P 263
Cdd:cd03294 265 D 265
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-262 |
7.67e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 163.24 E-value: 7.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLAlPPEA 87
Cdd:COG1126 1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKS----TLLRCINLLEEPDSGTITVDGEDLTD-SKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRgSALAMIFQDPltTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRV 167
Cdd:COG1126 72 INKLR-RKVGMVFQQF--NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
250
....*....|....*
gi 1208293942 248 DRPRHPYTRGLLNSV 262
Cdd:COG1126 225 ENPQHERTRAFLSKV 239
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-262 |
1.02e-48 |
|
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: 163.46 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILG-LVDRPGEITRGEVIFKGRDLLALP 84
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMR 164
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEI--DPTRIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATD 244
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
250
....*....|....*...
gi 1208293942 245 DVLDRPRHPYTRGLLNSV 262
Cdd:TIGR02323 235 QVLDDPQHPYTQLLVSSI 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-285 |
2.92e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.25 E-value: 2.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPPEAq 88
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLED----PTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 rrlRGsaLAMIFQDPltTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVA 168
Cdd:COG3839 75 ---RN--IAMVFQSY--ALYPHMTVYENIAFP-LKLRKVPKAEIDRRVREAAELLGLED---LLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLgvvAE---LADRIAVMYAGDIVEIGATDD 245
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ---VEamtLADRIAVMNDGRIQQVGTPEE 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1208293942 246 VLDRPRHPYTRGLL-----NSVPGdTARGERLRqIEGTAPPLSAR 285
Cdd:COG3839 221 LYDRPANLFVAGFIgsppmNLLPG-TVEGGGVR-LGGVRLPLPAA 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-262 |
1.09e-47 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 161.39 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 19 HDLRGAWPA---LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIFKGRDLLALPPEAQRRLRGSa 95
Cdd:PRK10419 16 GGLSGKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESP---SQGNVSWRGEPLAKLNRAQRKAFRRD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 96 LAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMRQRVAIAIALLN 175
Cdd:PRK10419 91 IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDL--DDSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 176 SPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDvLDRPRHPYT 255
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD-KLTFSSPAG 247
|
....*..
gi 1208293942 256 RGLLNSV 262
Cdd:PRK10419 248 RVLQNAV 254
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-251 |
1.38e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.81 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfSIL----GLVdRPgeiTRGEVIFKGRDLLALP 84
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKS----TLLrllnGLL-KP---TSGEVLVDGKDITKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLRGsalaMIFQDPLTTL-NPvlTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGM 163
Cdd:COG1122 70 LRELRRKVG----LVFQNPDDQLfAP--TVEEDVAFG-PENLGLPREEIRERVEEALELVGL---EHLADRPPHELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGAT 243
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
....*...
gi 1208293942 244 DDVLDRPR 251
Cdd:COG1122 219 REVFSDYE 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-232 |
2.92e-47 |
|
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: 158.79 E-value: 2.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRDLLAL 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKStllriIAGL------ERP---TSGEVLVDGEPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPeaqrrlrgsALAMIFQDPltTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGM 163
Cdd:cd03293 72 GP---------DRGYVFQQD--ALLPWLTVLDNVALG-LELQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGM 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVM 232
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
8-274 |
4.46e-47 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 159.96 E-value: 4.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHdLRGAW------PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLl 81
Cdd:PRK15112 4 LLEVRNLSKTFR-YRTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMI----EPTSGELLIDDHPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 alpPEAQRRLRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITsPEtRLSQYPHEFSG 161
Cdd:PRK15112 78 ---HFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLL-PD-HASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
250 260 270
....*....|....*....|....*....|...
gi 1208293942 242 ATDDVLDRPRHPYTRGLLNSVPGDTARGERLRQ 274
Cdd:PRK15112 233 STADVLASPLHELTKRLIAGHFGEALTADAWRK 265
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-249 |
5.90e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 5.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL-RP---TSGEVRVLGEDVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLrgsalAMIFQDPltTLNPVLTiGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVA 168
Cdd:COG1131 73 RRI-----GYVPQEP--ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 1208293942 249 R 249
Cdd:COG1131 221 R 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-235 |
7.24e-46 |
|
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: 7.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 10 EVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQR 89
Cdd:cd03225 1 ELKNLSFSYPD--GARPALDDISLTIKKGEFVLIVGPNGSGKS----TLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 90 RLRGsalaMIFQDP----LTTlnpvlTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQ 165
Cdd:cd03225 75 RKVG----LVFQNPddqfFGP-----TVEEEVAFG-LENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-239 |
1.34e-45 |
|
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: 154.43 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEA 87
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTL-LHLLGGLDNP---TSGEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQdpLTTLNPVLTIGEQMAEAILEhARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRV 167
Cdd:TIGR02211 77 RAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGvVAELADRIAVMYAGDIVE 239
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQLFN 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-250 |
1.51e-45 |
|
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: 154.70 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSilglvdrpgEITRGEVIFKGRDLLAL 83
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTtllrlIAGFE---------TPTSGEILLDGKDITNL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPeAQRRLRgsalaMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGM 163
Cdd:cd03300 68 PP-HKRPVN-----TVFQN--YALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGAT 243
Cdd:cd03300 136 QQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
....*..
gi 1208293942 244 DDVLDRP 250
Cdd:cd03300 216 EEIYEEP 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-259 |
1.45e-44 |
|
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: 152.45 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSVAgfsiLGLVDRPGEITRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINRLIEPTSGEIFIDGEDIREQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGSALAMIfqdpltTLNPVLTIGEQMAeAILEHARVAPAEVRRRCIDSLRRVGItSPETRLSQYPHEFSGGMRQRVA 168
Cdd:cd03295 74 RRKIGYVIQQI------GLFPHMTVEENIA-LVPKLLKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
250
....*....|.
gi 1208293942 249 RPRHPYTRGLL 259
Cdd:cd03295 226 SPANDFVAEFV 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-285 |
9.73e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.03 E-value: 9.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 10 EVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQR 89
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS----TLIRCINLLERPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 90 RLRGSaLAMIFQDplttLNpVL---TIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQR 166
Cdd:PRK11153 79 KARRQ-IGMIFQH----FN-LLssrTVFDNVALP-LELAGTPKAEIKARVTELLELVGLSD---KADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 167 VAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDV 246
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 1208293942 247 LDRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPPLSAR 285
Cdd:PRK11153 229 FSHPKHPLTREFIQSTLHLDLPEDYLARLQAEPTTGSGP 267
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-290 |
4.10e-43 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 151.84 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRDLLA- 82
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTtllriIAGL------ETP---DSGRIVLNGRDLFTn 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 LPPEaQRRLrgsalAMIFQDPLttLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGG 162
Cdd:COG1118 70 LPPR-ERRV-----GFVFQHYA--LFPHMTVAENIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1208293942 243 TDDVLDRPRHPYTRGLL--NSVPGDTARGERLRQIEGTAPPLSARPVGCA 290
Cdd:COG1118 218 PDEVYDRPATPFVARFLgcVNVLRGRVIGGQLEADGLTLPVAEPLPDGPA 267
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
27-275 |
6.82e-43 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 151.54 E-value: 6.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDplTT 106
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKS----TTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQ--FA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNPVLTIgEQMAEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPT 186
Cdd:TIGR01186 82 LFPHMTI-LQNTSLGPELLGWPEQERKEKALELLKLVGL---EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 187 TALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLLnsvpgdt 266
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI------- 230
|
....*....
gi 1208293942 267 aRGERLRQI 275
Cdd:TIGR01186 231 -GKVDLSQV 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-244 |
5.51e-42 |
|
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: 145.27 E-value: 5.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRAPVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLV---DRPgeiTRGEVIFKG 77
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLaglDRP---TSGTVRLAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 78 RDLLALPPEAQRRLRGSALAMIFQD----P-LTTLNPVLTIgeqmaeaiLEHARVAPAevRRRCIDSLRRVGITSpetRL 152
Cdd:COG4181 74 QDLFALDEDARARLRARHVGFVFQSfqllPtLTALENVMLP--------LELAGRRDA--RARARALLERVGLGH---RL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 153 SQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGvVAELADRIAVM 232
Cdd:COG4181 141 DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRL 219
|
250
....*....|..
gi 1208293942 233 YAGDIVEIGATD 244
Cdd:COG4181 220 RAGRLVEDTAAT 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-246 |
1.86e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.43 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPE 86
Cdd:COG3638 1 PMLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKS----TLLRCLNGLVEPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRGSaLAMIFQDP-----LTTLNPVLT--IGEQ-MAEAILehaRVAPAEVRRRCIDSLRRVGITSpetRLSQYPHE 158
Cdd:COG3638 74 ALRRLRRR-IGMIFQQFnlvprLSVLTNVLAgrLGRTsTWRSLL---GLFPPEDRERALEALERVGLAD---KAYQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
....*...
gi 1208293942 239 EIGATDDV 246
Cdd:COG3638 227 FDGPPAEL 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-241 |
3.20e-41 |
|
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: 142.78 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAq 88
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE----EPTSGRIYIGGRDVTDLPPKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 rrlRGsaLAMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVA 168
Cdd:cd03301 72 ---RD--IAMVFQN--YALYPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-237 |
3.57e-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: 142.67 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLAlPPEAQ 88
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRCINLLEEPDSGTIIIDGLKLTD-DKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRgSALAMIFQDplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVA 168
Cdd:cd03262 72 NELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-242 |
4.58e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLV---DRPgeiTRGEVIFKGRDLLALPPEAQRRLRGSaLAMIFQD 102
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLygeERP---TSGQVLVNGQDLSRLKRREIPYLRRR-IGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:COG2884 88 --FRLLPDRTVYENVALP-LRVTGKSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 183 DEPTTALDVTIQGQIiaeMQALQR--ETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:COG2884 162 DEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-235 |
4.68e-41 |
|
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: 141.17 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALppEAQ 88
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLTDL--EDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGSALAMIFQDPltTLNPVLTIGEQMAEAIleharvapaevrrrcidslrrvgitspetrlsqyphefSGGMRQRVA 168
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-249 |
2.27e-40 |
|
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: 141.55 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKS----TLLRCLNGLVEPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRgSALAMIFQDplttLNpvlTIGEQMA-EAILeHARVA------------PAEVRRRCIDSLRRVGItspETRLSQY 155
Cdd:cd03256 74 RQLR-RQIGMIFQQ----FN---LIERLSVlENVL-SGRLGrrstwrslfglfPKEEKQRALAALERVGL---LDKAYQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 156 PHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
250
....*....|....*...
gi 1208293942 236 DIVEIGA----TDDVLDR 249
Cdd:cd03256 222 RIVFDGPpaelTDEVLDE 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-250 |
3.40e-40 |
|
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: 140.93 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpaLNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI----KPDSGKILLNGKDITNLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RrlrgsaLAMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVA 168
Cdd:cd03299 72 D------ISYVPQN--YALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
..
gi 1208293942 249 RP 250
Cdd:cd03299 220 KP 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-298 |
1.77e-39 |
|
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: 142.10 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIFKGRDLLALPP 85
Cdd:TIGR03265 2 SPYLSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-ERQ---TAGTIYQGGRDITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 eaQRRLRGsalaMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQ 165
Cdd:TIGR03265 74 --QKRDYG----IVFQS--YALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:TIGR03265 142 RVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 246 VLDRPRHPYTR---GLLNSVPGDTARGERLR------------QIEGTAPPLSARPVGCAFHPRCDRA 298
Cdd:TIGR03265 222 IYRHPATPFVAdfvGEVNWLPGTRGGGSRARvggltlacapglAQPGASVRLAVRPEDIRVSPAGNAA 289
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-256 |
9.33e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 141.01 E-value: 9.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQd 102
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKS----TLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQ- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plttlN----PVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPEtrlSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:COG4175 113 -----HfallPHRTVLENVAFG-LEIQGVPKAERRERAREALELVGLAGWE---DSYPDELSGGMQQRVGLARALATDPD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 179 LIIADEPTTALDVTIQgqiiAEMQ----ALQRETGTAMIWITHDLgvvAE---LADRIAVMYAGDIVEIGATDDVLDRPR 251
Cdd:COG4175 184 ILLMDEAFSALDPLIR----REMQdellELQAKLKKTIVFITHDL---DEalrLGDRIAIMKDGRIVQIGTPEEILTNPA 256
|
....*
gi 1208293942 252 HPYTR 256
Cdd:COG4175 257 NDYVA 261
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-237 |
1.36e-38 |
|
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: 134.83 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL-KP---DSGEIKVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLrgsalAMIFQDPltTLNPVLTIGEQMaeaileharvapaevrrrcidslrrvgitspetrlsqyphEFSGGMRQRVA 168
Cdd:cd03230 73 RRI-----GYLPEEP--SLYENLTVRENL----------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-259 |
7.66e-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: 134.77 E-value: 7.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIFKGRDLLALPPeaQ 88
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERP---DSGTILFGGEDATDVPV--Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGsalaMIFQDplTTLNPVLTIGEQMAEAI-LEHARVAP--AEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQ 165
Cdd:cd03296 73 ERNVG----FVFQH--YALFRHMTVFDNVAFGLrVKPRSERPpeAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
250
....*....|....
gi 1208293942 246 VLDRPRHPYTRGLL 259
Cdd:cd03296 224 VYDHPASPFVYSFL 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-262 |
8.12e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 139.01 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 32 SLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDplTTLNPVL 111
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 112 TIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDV 191
Cdd:PRK10070 122 TVLDNTAFG-MELAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 192 TIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLLNSV 262
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-237 |
1.57e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.02 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGawpaLNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTL-LRALADLDPP---TSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLrgsaLAMIFQDPlttlnpVL---TIGEQMAEA-ILEHARVAPAEVRrrciDSLRRVGItsPETRLSQYPHEFSGGMR 164
Cdd:COG4619 73 RRQ----VAYVPQEP------ALwggTVRDNLPFPfQLRERKFDRERAL----ELLERLGL--PPDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-262 |
2.24e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 133.68 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLAlpPEA 87
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEITSGDLIVDGLKVND--PKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRV 167
Cdd:PRK09493 71 DERLIRQEAGMVFQQ--FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
250
....*....|....*
gi 1208293942 248 DRPRHPYTRGLLNSV 262
Cdd:PRK09493 225 KNPPSQRLQEFLQHV 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-285 |
4.57e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 133.71 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLAlpPEAQ 88
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLL-LP---TSGKVTVDGLDTLD--EENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRgSALAMIFQDPLTTLnpvltIGEQMAEAI---LEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQ 165
Cdd:TIGR04520 73 WEIR-KKVGMVFQNPDNQF-----VGATVEDDVafgLENLGVPREEMRKRVDEALKLVGMED---FRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAeLADRIAVMYAGDIVEIGATDD 245
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPRE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1208293942 246 VLdrprhpytrgllnsvpgdtARGERLRQIeGTAPPLSAR 285
Cdd:TIGR04520 223 IF-------------------SQVELLKEI-GLDVPFITE 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-187 |
3.98e-36 |
|
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: 127.38 E-value: 3.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQRRlrgsALAMIFQDPltTL 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-SP---TEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMAEAILEHArVAPAEVRRRCIDSLRRVGITS-PETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPT 186
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1208293942 187 T 187
Cdd:pfam00005 150 A 150
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-250 |
4.34e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 4.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSILglvdrpgeiTRGEVIFKGRDLL 81
Cdd:PRK09452 13 PLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTtvlrlIAGFETP---------DSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPPEaQRRLRgsalaMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVgitspetRLSQY----PH 157
Cdd:PRK09452 80 HVPAE-NRHVN-----TVFQS--YALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMV-------QLEEFaqrkPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
250
....*....|...
gi 1208293942 238 VEIGATDDVLDRP 250
Cdd:PRK09452 224 EQDGTPREIYEEP 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-229 |
5.26e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 129.94 E-value: 5.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPE 86
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTL-LHLLGGLDTP---TSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRGSALAMIFQdpLTTLNPVLTIGEQMAEAILEhARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQR 166
Cdd:PRK11629 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 167 VAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLgvvaELADRI 229
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-249 |
5.54e-36 |
|
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: 129.98 E-value: 5.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPPEA 87
Cdd:COG4555 1 MIEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK----PDSGSILIDGEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLrgsalAMIFQDPltTLNPVLTiGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSqypHEFSGGMRQRV 167
Cdd:COG4555 73 RRQI-----GVLPDER--GLYDRLT-VRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV---GELSTGMKKKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
..
gi 1208293942 248 DR 249
Cdd:COG4555 221 EE 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-259 |
5.65e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.87 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGAWpalnglSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRDLLAL 83
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF------DLTIAAGERVAILGPSGAGKStllnlIAGF------LPP---DSGRILWNGQDLTAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPeAQRrlrgsALAMIFQDplTTLNPVLTIGEQMAEAILEHARVAPAEvRRRCIDSLRRVGITSPETRLsqyPHEFSGGM 163
Cdd:COG3840 67 PP-AER-----PVSMLFQE--NNLFPHLTVAQNIGLGLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRL---PGQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGAT 243
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
250
....*....|....*.
gi 1208293942 244 DDVLDRPRHPYTRGLL 259
Cdd:COG3840 215 AALLDGEPPPALAAYL 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-251 |
1.08e-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: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPeAQ 88
Cdd:cd03219 1 LEVRGLTKRFGGLV----ALDDVSFSVRPGEIHGLIGPNGAGKTTL-FNLISGFLRP---TSGSVLFDGEDITGLPP-HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGsaLAMIFQDP-----LTTLNPVLtIGEQMAE---AILEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFS 160
Cdd:cd03219 72 IARLG--IGRTFQIPrlfpeLTVLENVM-VAAQARTgsgLLLARARREEREARERAEELLERVGLAD---LADRPAGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|.
gi 1208293942 241 GATDDVLDRPR 251
Cdd:cd03219 225 GTPDEVRNNPR 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-235 |
1.23e-35 |
|
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: 126.59 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 10 EVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQR 89
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 90 RLrgsaLAMIFQdplttlnpvltigeqmaeaileharvapaevrrrcidslrrvgitspetrlsqypheFSGGMRQRVAI 169
Cdd:cd00267 73 RR----IGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 170 AIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-246 |
1.51e-35 |
|
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: 128.45 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDR-PGEITRGEVIFKGRDLLAL--PP 85
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLiPGAPDEGEVLLDGKDIYDLdvDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGsalaMIFQDPlttlNPV-LTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITsPETRLSQYPHEFSGGMR 164
Cdd:cd03260 77 LELRRRVG----MVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALW-DEVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtgTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATD 244
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
..
gi 1208293942 245 DV 246
Cdd:cd03260 226 QI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-248 |
1.94e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.67 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLqTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKS--VAgfSILGLVdrpgEITRGEVIFKGRdllal 83
Cdd:COG1121 4 MPAIELENL-TVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKStlLK--AILGLL----PPTSGTVRLFGK----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEAQRRLRG-----SALAMIFqdPLTTLNPVLTigeqmaeAILEHA---RVAPAEVRRRCIDSLRRVGITSPETRlsQY 155
Cdd:COG1121 69 PPRRARRRIGyvpqrAEVDWDF--PITVRDVVLM-------GRYGRRglfRRPSRADREAVDEALERVGLEDLADR--PI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 156 pHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMyAG 235
Cdd:COG1121 138 -GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NR 214
|
250
....*....|...
gi 1208293942 236 DIVEIGATDDVLD 248
Cdd:COG1121 215 GLVAHGPPEEVLT 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-249 |
2.12e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 128.57 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEA 87
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV----EPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRgSALAMIFQD-----PLTTLNPVLtigeqmaeaileHARVA------------PAEVRRRCIDSLRRVGItspET 150
Cdd:TIGR02315 74 LRKLR-RRIGMIFQHynlieRLTVLENVL------------HGRLGykptwrsllgrfSEEDKERALSALERVGL---AD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 151 RLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIA 230
Cdd:TIGR02315 138 KAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIV 217
|
250 260
....*....|....*....|...
gi 1208293942 231 VMYAGDIVEIGA----TDDVLDR 249
Cdd:TIGR02315 218 GLKAGEIVFDGApselDDEVLRH 240
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
23-262 |
3.82e-35 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 127.61 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIFKGRDLLALPPeaQRRLRGsalaMIFQD 102
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL-EQP---DSGRIRLNGQDATRVHA--RDRKIG----FVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:TIGR00968 81 --YALFKHLTVRDNIAFG-LEIRKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLLNSV 262
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-241 |
8.84e-35 |
|
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: 126.08 E-value: 8.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSIL-GLVdrpgEITRGEVIFKGRDLLALPPEA 87
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtGEL----RPTSGTAYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLrgsalAMIFQDplTTLNPVLTIgeqmAEAILEHAR---VAPAEVRRRCIDSLRRVGITSPETRLSqypHEFSGGMR 164
Cdd:cd03263 74 RQSL-----GYCPQF--DALFDELTV----REHLRFYARlkgLPKSEIKEEVELLLRVLGLTDKANKRA---RTLSGGMK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIiaeMQALQRE-TGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI---WDLILEVrKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-253 |
1.60e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.62 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 16 TVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPGE---ITRGEVIFKGRD---LLALPPEAQR 89
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTF-LRCINFLEKPSEgsiVVNGQTINLVRDkdgQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 90 RLRGSALAMIFQDplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITspETRLSQYPHEFSGGMRQRVAI 169
Cdd:PRK10619 88 RLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGID--ERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 170 AIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
....
gi 1208293942 250 PRHP 253
Cdd:PRK10619 243 PQSP 246
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-229 |
4.61e-34 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 123.88 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 11 VRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPGeitRGEVIFKGRDLLALPPEAQRR 90
Cdd:TIGR03608 1 LKNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTL-LNIIGLLEKFD---SGQVYLNGQETPPLNSKKASK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 91 LRGSALAMIFQDPLTTLNpvLTIGEQMaEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIA 170
Cdd:TIGR03608 73 FRREKLGYLFQNFALIEN--ETVEENL-DLGLKYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 171 IALLNSPDLIIADEPTTALDvTIQGQIIAEMQALQRETGTAMIWITHDLgVVAELADRI 229
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLD-PKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-248 |
4.72e-34 |
|
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: 125.16 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLqTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEA 87
Cdd:COG1120 1 MLEAENL-SVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKS----TLLRALAGLLKPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLrgsaLAMIFQDPLTTLNpvLTIGEqmaeaILEHARVA--------PAEVRRRCIDSLRRVGITSPETRLSqypHEF 159
Cdd:COG1120 73 LARR----IAYVPQEPPAPFG--LTVRE-----LVALGRYPhlglfgrpSAEDREAVEEALERTGLEHLADRPV---DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
....*....
gi 1208293942 240 IGATDDVLD 248
Cdd:COG1120 219 QGPPEEVLT 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-260 |
5.84e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.86 E-value: 5.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSIlGLVDRP--GEITRGEVIFKGRDLLALPPE 86
Cdd:PRK11264 4 IEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPeaGTIRVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRgSALAMIFQDplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQR 166
Cdd:PRK11264 79 LIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS---YPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 167 VAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTaMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDV 246
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
250
....*....|....
gi 1208293942 247 LDRPRHPYTRGLLN 260
Cdd:PRK11264 232 FADPQQPRTRQFLE 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-250 |
1.17e-33 |
|
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: 126.75 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 32 SLTLHAGEVLGLVGESGSGKSvagfSILGLV---DRP--GEIT-RGEVIFKGRDLLALPPEaQRRLrgsalAMIFQDPLt 105
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKT----TLLRAIaglERPdsGRIRlGGEVLQDSARGIFLPPH-RRRI-----GYVFQEAR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tLNPVLTIGEQMAEAilehARVAPAEVRRRCIDSL-RRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADE 184
Cdd:COG4148 88 -LFPHLSVRGNLLYG----RKRAPRAERRISFDEVvELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 185 PTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
23-250 |
3.42e-33 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 125.88 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeiTRGEVIFKGRDLLALPPEAQrrlrgsALAMIFQD 102
Cdd:TIGR03258 16 GANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG--LTGRIAIADRDLTHAPPHKR------GLALLFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:TIGR03258 88 --YALFPHLKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQRE-TGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:TIGR03258 162 DEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAP 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-245 |
3.60e-33 |
|
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: 122.09 E-value: 3.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03265 1 IEVENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTT-IKMLTTLLKP---TSGRATVAGHDVVREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLrgsalAMIFQDPltTLNPVLTIGEQMaeaiLEHARVA--PAEVRRRCIDS-LRRVGITSPETRLSQYpheFSGGMRQ 165
Cdd:cd03265 73 RRI-----GIVFQDL--SVDDELTGWENL----YIHARLYgvPGAERRERIDElLDFVGLLEAADRLVKT---YSGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-277 |
1.02e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 123.28 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRR-----LRGSALa 97
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKT----TTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRrigyvIQQIGL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 98 miFqdplttlnPVLTIGEQMAeAILEHARVAPAEVRRRCIDSLRRVGItSPETRLSQYPHEFSGGMRQRVAIAIALLNSP 177
Cdd:COG1125 88 --F--------PHMTVAENIA-TVPRLLGWDKERIRARVDELLELVGL-DPEEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 178 DLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRG 257
Cdd:COG1125 156 PILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAD 235
|
250 260
....*....|....*....|
gi 1208293942 258 LLNSvpGDTARGERLRQIEG 277
Cdd:COG1125 236 FVGA--DRGLRRLSLLRVED 253
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
1.37e-32 |
|
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: 126.80 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 2 TRDRAPVLEVRNLqTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLL 81
Cdd:COG4988 330 PAAGPPSIELEDV-SFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL-PP---YSGSILINGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPPEAQRRLrgsaLAMIFQdplttlNPVL---TIgeqmAEAILEHARVAPAEvrrRCIDSLRRVGITS--------PET 150
Cdd:COG4988 403 DLDPASWRRQ----IAWVPQ------NPYLfagTI----RENLRLGRPDASDE---ELEAALEAAGLDEfvaalpdgLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 151 RLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLGVVAElADRIA 230
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRIL 542
|
250
....*....|....*..
gi 1208293942 231 VMYAGDIVEIGATDDVL 247
Cdd:COG4988 543 VLDDGRIVEQGTHEELL 559
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
8-238 |
3.30e-32 |
|
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: 119.35 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPGEitrGEVIFKGRDLLALPPEA 87
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTL-LTLIGGLRSVQE---GSLKVLGQELHGASKKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSaLAMIFQ-----DPLTTLNPVltigeQMAeaiLE-HARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSG 161
Cdd:TIGR02982 77 LVQLRRR-IGYIFQahnllGFLTARQNV-----QMA---LElQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHD---LGVvaelADRIAVMYAGDIV 238
Cdd:TIGR02982 145 GQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDnriLDV----ADRILQMEDGKLL 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-262 |
4.61e-32 |
|
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: 121.83 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 43 LVGESGSGKSVAGFSILGLvDRPGEitrGEVIFKGRDLLALPPEaqrrLRGsaLAMIFQDplTTLNPVLTIGEQMAEAiL 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDS---GSIMLDGEDVTNVPPH----LRH--INMVFQS--YALFPHMTVEENVAFG-L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 123 EHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQ 202
Cdd:TIGR01187 68 KMRKVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 203 ALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLLNSV 262
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-262 |
1.08e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.87 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHdlrgAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRDLL 81
Cdd:PRK11607 18 PLLEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKStllrmLAGF------EQP---TAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPPeAQRrlrgsALAMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSG 161
Cdd:PRK11607 85 HVPP-YQR-----PINMMFQS--YALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250 260
....*....|....*....|.
gi 1208293942 242 ATDDVLDRPRHPYTRGLLNSV 262
Cdd:PRK11607 233 EPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-241 |
2.67e-31 |
|
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: 116.00 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 10 EVRNLqTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQR 89
Cdd:cd03214 1 EVENL-SVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----KPSSGEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 90 RLRgsalamifqdplttlnpvltigeqmaeAILEHArvapaevrrrcidsLRRVGITSPETRLSqypHEFSGGMRQRVAI 169
Cdd:cd03214 73 RKI---------------------------AYVPQA--------------LELLGLAHLADRPF---NELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 170 AIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-246 |
2.75e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLqtVFHDLRGAwPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvdRPgeITRGEVIFKGRDLLALPP 85
Cdd:COG3845 255 EVVLEVENL--SVRDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL--RP--PASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 eAQRRLRGsaLAMIFQDPLTT-LNPVLTIGEQMaeaILEHARVAP---------AEVRRRCIDSLRRVGI--TSPETRLS 153
Cdd:COG3845 328 -RERRRLG--VAYIPEDRLGRgLVPDMSVAENL---ILGRYRRPPfsrggfldrKAIRAFAEELIEEFDVrtPGPDTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 154 QypheFSGGMRQRVAIAIALLNSPDLIIADEPTTALDV----TIQGQIIAemqalQRETGTAMIWITHDLGVVAELADRI 229
Cdd:COG3845 402 S----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRI 472
|
250
....*....|....*..
gi 1208293942 230 AVMYAGDIVEIGATDDV 246
Cdd:COG3845 473 AVMYEGRIVGEVPAAEA 489
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-237 |
9.69e-31 |
|
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: 115.58 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSaLAMIFQDPLt 105
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQDFR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:cd03292 89 -LLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 186 TTALDVTIQGQIIAEMQALQReTGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-254 |
1.21e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 118.68 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 31 LSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRP--GEIT-RGEVIFKGRDLLALPPEaQRRLrgsalAMIFQDplTTL 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT-RPdeGEIVlNGRTLFDSRKGIFLPPE-KRRI-----GYVFQE--ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQ----MAEAILEHARVAPAEVrrrcidsLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIAD 183
Cdd:TIGR02142 87 FPHLSVRGNlrygMKRARPSERRISFERV-------IELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 184 EPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPY 254
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-256 |
1.74e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.90 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 1 MTRDRA---PVLEVRNLqTVFHdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVagF--SILGLVDR-PGEITRGEVI 74
Cdd:COG1117 1 MTAPAStlePKIEVRNL-NVYY---GDKQALKDINLDIPENKVTALIGPSGCGKST--LlrCLNRMNDLiPGARVEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 75 FKGRDLLA--LPPEAQRRLRGsalaMIFQDPlttlNPV-LTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSpET- 150
Cdd:COG1117 75 LDGEDIYDpdVDVVELRRRVG----MVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWD-EVk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 151 -RLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtgTAMIWITHDLGVVAELADRI 229
Cdd:COG1117 146 dRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYT 223
|
250 260
....*....|....*....|....*..
gi 1208293942 230 AVMYAGDIVEIGATDDVLDRPRHPYTR 256
Cdd:COG1117 224 AFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-246 |
1.80e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsilglVDRPGEitrGEVIFKGRDL 80
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKStlmkiLSG------VYQPDS---GEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALPP-EAQRrlRGsaLAMIFQDPltTLNPVLTIGEQ--MAEAILEHARVAPAEVRRRCIDSLRRVGIT-SPETRLSqyp 156
Cdd:COG1129 69 RFRSPrDAQA--AG--IAIIHQEL--NLVPNLSVAENifLGREPRRGGLIDWRAMRRRARELLARLGLDiDPDTPVG--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 hEFSGGMRQRVAIAIALLNSPDLIIADEPTTAL---DVTIQGQIIAEMqalqRETGTAMIWITHDLGVVAELADRIAVMY 233
Cdd:COG1129 140 -DLSVAQQQLVEIARALSRDARVLILDEPTASLterEVERLFRIIRRL----KAQGVAIIYISHRLDEVFEIADRVTVLR 214
|
250
....*....|...
gi 1208293942 234 AGDIVEIGATDDV 246
Cdd:COG1129 215 DGRLVGTGPVAEL 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-254 |
2.05e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 121.48 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLqtVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQ 88
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY----EPTSGRILIDGIDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgsALAMIFQDPlttlnpVL---TIGEQMAeaiLEHARVAPAEVRRRCidslRRVGITS-----P---ETRLSQYPH 157
Cdd:COG2274 548 RR----QIGVVLQDV------FLfsgTIRENIT---LGDPDATDEEIIEAA----RLAGLHDfiealPmgyDTVVGEGGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLGVVAeLADRIAVMYAGDI 237
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRI 687
|
250
....*....|....*..
gi 1208293942 238 VEIGATDDVLDRPRHPY 254
Cdd:COG2274 688 VEDGTHEELLARKGLYA 704
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-238 |
2.39e-30 |
|
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: 114.28 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRDLlalppeAQRRLRGSAlAMIFQDPLTTL 107
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGKPI------KAKERRKSI-GYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 npvltIGEQMAEAILEHARVAPAEVRR-RCIdsLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIADEPT 186
Cdd:cd03226 85 -----FTDSVREELLLGLKELDAGNEQaETV--LKDLDLYALKER---HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 187 TALDvTIQGQIIAE-MQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:cd03226 155 SGLD-YKNMERVGElIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-238 |
2.65e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.98 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPP 85
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLDKP---TSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGSALAMIFQDplTTLNPVLTiGEQMAEAILEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQ 165
Cdd:PRK10535 78 DALAQLRREHFGFIFQR--YHLLSHLT-AAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAElADRIAVMYAGDIV 238
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-241 |
4.35e-30 |
|
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: 113.54 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 38 GEVLGLVGESGSGKSVAGFSILGLvDRP--GEIT-RGEVIFKGRDLLALPPEaQRRLrgsalAMIFQDplTTLNPVLTIG 114
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGL-EKPdgGTIVlNGTVLFDSRKKINLPPQ-QRKI-----GLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 115 EQMAEAIlehARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQ 194
Cdd:cd03297 94 ENLAFGL---KRKRNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1208293942 195 GQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
23-235 |
5.20e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 113.50 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLV---DRPgeiTRGEVIFKGRDLLALPPEAQRRLRGSaLAMI 99
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLygaLTP---SRGQVRIAGEDVNRLRGRQLPLLRRR-IGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 100 FQDPLttLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:TIGR02673 85 FQDFR--LLPDRTVYENVALP-LEVRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-247 |
5.60e-30 |
|
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: 119.14 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDL-RGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPP 85
Cdd:TIGR03269 278 PIIKVRNVSKRYISVdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVL----EPTSGEVNVRVGDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRGSA---LAMIFQDplTTLNPVLTIGEQMAEAI-LEharvAPAEV-RRRCIDSLRRVGITSPETR--LSQYPHE 158
Cdd:TIGR03269 354 KPGPDGRGRAkryIGILHQE--YDLYPHRTVLDNLTEAIgLE----LPDELaRMKAVITLKMVGFDEEKAEeiLDKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
....*....
gi 1208293942 239 EIGATDDVL 247
Cdd:TIGR03269 508 KIGDPEEIV 516
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-241 |
1.12e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.34 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRP--GEITRGEvifkgrdlLALP 84
Cdd:PRK13635 4 EIIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL-LPeaGTITVGG--------MVLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLRgSALAMIFQDPLTTLnpvltIGEQMAEAI---LEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSG 161
Cdd:PRK13635 73 EETVWDVR-RQVGMVFQNPDNQF-----VGATVQDDVafgLENIGVPREEMVERVDQALRQVGMED---FLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAElADRIAVMYAGDIVEIG 241
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-232 |
1.50e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 112.24 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRdllalPPEAQRRL------RGSALami 99
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP----TSGSIRVFGK-----PLEKERKRigyvpqRRSID--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 100 FQDPLTTLNPVLTIGEQMAEAIlehaRVAPAEVRRRCIDSLRRVGITSPETR-LSqyphEFSGGMRQRVAIAIALLNSPD 178
Cdd:cd03235 81 RDFPISVRDVVLMGLYGHKGLF----RRLSKADKAKVDEALERVGLSELADRqIG----ELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVM 232
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-255 |
2.82e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDR-----PGEITRGEVIFKGRDLLA 82
Cdd:PRK14247 3 KIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKS----TLLRVFNRlielyPEARVSGEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 LP-PEAQRRLRgsalaMIFQDPlttlNPV--LTIGEQMAEAI-LEHARVAPAEVRRRCIDSLRRVGI-TSPETRLSQYPH 157
Cdd:PRK14247 75 MDvIELRRRVQ-----MVFQIP----NPIpnLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwDEVKDRLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETgtAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*...
gi 1208293942 238 VEIGATDDVLDRPRHPYT 255
Cdd:PRK14247 224 VEWGPTREVFTNPRHELT 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-249 |
4.26e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLlalPPEA 87
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILA----PDSGEVLWDGEPL---DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRL------RGsalamifqdplttLNPVLTIGEQmaeaILEHAR---VAPAEVRRRCIDSLRRVGITSPETRLSQyphE 158
Cdd:COG4152 70 RRRIgylpeeRG-------------LYPKMKVGEQ----LVYLARlkgLSKAEAKRRADEWLERLGLGDRANKKVE---E 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
250
....*....|.
gi 1208293942 239 EIGATDDVLDR 249
Cdd:COG4152 209 LSGSVDEIRRQ 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-232 |
4.89e-29 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 111.37 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVF--HDLRGA-WPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGR----D 79
Cdd:COG4778 3 TLLEVENLSKTFtlHLQGGKrLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNYLPDSGSILVRHDggwvD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 80 LLALPPEAQRRLRGSALAMIFQDpLTTLNPVLTIgEQMAEAILEHArVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEF 159
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQF-LRVIPRVSAL-DVVAEPLLERG-VDREEARARARELLARLNL--PERLWDLPPATF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVM 232
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-241 |
5.06e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAqrrLRgSALAMIFQDplt 105
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LR-RQIGVVPQD--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlnPVL---TIGEQMA--------EAILEHARVAPAEVRrrcIDSLrrvgitsPE---TRLSQYPHEFSGGMRQRVAIAI 171
Cdd:COG1132 423 ---TFLfsgTIRENIRygrpdatdEEVEEAAKAAQAHEF---IEAL-------PDgydTVVGERGVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 172 ALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLGVVAElADRIAVMYAGDIVEIG 241
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-244 |
5.32e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRP--GEITRGEVIFkgrDLLALPPEAQRRLRGSALAMIF 100
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMPrsGTLNIAGNHF---DFSKTPSDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 101 QDplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:PRK11124 89 QQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATD 244
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-248 |
6.07e-29 |
|
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: 110.99 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPPEaQ 88
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPH-E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGSALA----MIFqdplttlnPVLTIGE--QMAEAILEHARVApaevrrrciDSLRRVGITSP--ETRLSQYPHEFS 160
Cdd:cd03224 72 RARAGIGYVpegrRIF--------PELTVEEnlLLGAYARRRAKRK---------ARLERVYELFPrlKERRKQLAGTLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
....*...
gi 1208293942 241 GATDDVLD 248
Cdd:cd03224 214 GTAAELLA 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-232 |
7.96e-29 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 109.01 E-value: 7.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPPEAQRRlrgsALAMIFQDPlt 105
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLDLESLRK----NIAYVPQDP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlnpVL---TIgeqmAEAILeharvapaevrrrcidslrrvgitspetrlsqyphefSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:cd03228 86 ----FLfsgTI----RENIL-------------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQRETGTAMiwITHDLGVVaELADRIAVM 232
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIV--IAHRLSTI-RDADRIIVL 167
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-252 |
1.27e-28 |
|
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: 110.25 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEaqrRLrgsalaMIFQDplTTL 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGLAQPTSGGVILEGKQITEPGPD---RM------VVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMAEAILEHARVAPAEVRRRCID-SLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIADEPT 186
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKSERRAIVEeHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 187 TALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDV-LDRPRH 252
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-241 |
2.06e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.10 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRP--GEITRGEVIFkgrDLLALPPEAQRRLRGSALAMIF 100
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSL-LRVLNLLETPdsGQLNIAGHQF---DFSQKPSEKAIRLLRQKVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 101 QDplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:COG4161 89 QQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-254 |
2.20e-28 |
|
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: 114.86 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 4 DRAPVLEVRNLqtVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLAL 83
Cdd:COG4987 329 PGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEAQRRLrgsaLAMIFQDP---LTTL--NpvLTIG------EQMAEAileharvapaevrrrcidsLRRVGI-----TS 147
Cdd:COG4987 403 DEDDLRRR----IAVVPQRPhlfDTTLreN--LRLArpdatdEELWAA-------------------LERVGLgdwlaAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 148 PE---TRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLgVVAE 224
Cdd:COG4987 458 PDgldTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLE 534
|
250 260 270
....*....|....*....|....*....|
gi 1208293942 225 LADRIAVMYAGDIVEIGATDDVLDRPRHPY 254
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
26-238 |
2.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.95 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALppEAQRRLRGSAlAMIFQDPLT 105
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL-IP---SEGKVYVDGLDTSDE--ENLWDIRNKA-GMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLnpVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGitspetrLSQY----PHEFSGGMRQRVAIAIALLNSPDLII 181
Cdd:PRK13633 97 QI--VATIVEEDVAFGPENLGIPPEEIRERVDESLKKVG-------MYEYrrhaPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 182 ADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAElADRIAVMYAGDIV 238
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-239 |
6.53e-28 |
|
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: 107.69 E-value: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI-KP---DSGEITFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RrlrgsaLAMIFQDPltTLNPVLTiGEqmaEAILEHARVApaEVRRRCIDS-LRRVGitspetrLSQYPHE----FSGGM 163
Cdd:cd03268 73 R------IGALIEAP--GFYPNLT-AR---ENLRLLARLL--GIRKKRIDEvLDVVG-------LKDSAKKkvkgFSLGM 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVtiQGqiIAEMQAL---QRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:cd03268 132 KQRLGIALALLGNPDLLILDEPTNGLDP--DG--IKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-237 |
9.69e-28 |
|
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: 106.36 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTvfhdlrgaWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvdRPgeITRGEVIFKGRDLLALPP 85
Cdd:cd03215 2 EPVLEVRGLSV--------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL--RP--PASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRgsaLAMIFQDPLTT-LNPVLTIGEQMAeaileharvapaevrrrcidslrrvgitspetrLSQYpheFSGGMR 164
Cdd:cd03215 70 RDAIRAG---IAYVPEDRKREgLVLDLSVAENIA---------------------------------LSSL---LSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-241 |
3.50e-27 |
|
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: 105.83 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRdllALPPEAQ 88
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII----LPDSGEVLFDGK---PLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRL------RGsalamifqdplttLNPVLTIGEQMaeaiLEHAR---VAPAEVRRRCIDSLRRVGItspETRLSQYPHEF 159
Cdd:cd03269 70 NRIgylpeeRG-------------LYPKMKVIDQL----VYLAQlkgLKKEEARRRIDEWLERLEL---SEYANKRVEEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:cd03269 130 SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
..
gi 1208293942 240 IG 241
Cdd:cd03269 209 YG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-238 |
6.77e-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: 103.66 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSIL-GLVdrpgEITRGEVIFKGRDLLALPPEA 87
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTL-MKILsGLY----KPDSGEILVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRgsaLAMIFQdplttlnpvltigeqmaeaileharvapaevrrrcidslrrvgitspetrlsqypheFSGGMRQRV 167
Cdd:cd03216 72 ARRAG---IAMVYQ---------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-255 |
9.61e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEIT-RGEVIFKGRDLLAlPP 85
Cdd:PRK14239 4 PILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTiTGSIVYNGHNIYS-PR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRgSALAMIFQDPlttlNPV-LTIGEQMA----------EAILEHArvapaeVRRrcidSLRRVGI-TSPETRLS 153
Cdd:PRK14239 79 TDTVDLR-KEIGMVFQQP----NPFpMSIYENVVyglrlkgikdKQVLDEA------VEK----SLKGASIwDEVKDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 154 QYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtgTAMIWITHDLGVVAELADRIAVMY 233
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|..
gi 1208293942 234 AGDIVEIGATDDVLDRPRHPYT 255
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKET 243
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-239 |
9.87e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.10 E-value: 9.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSilglvdrpgEITRGEVIFKGRDLL 81
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTtllnlIAGFL---------APSSGEITLDGVPVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 AlpPEAQRrlrgsalAMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSG 161
Cdd:COG4525 73 G--PGADR-------GVVFQK--DALLPWLNVLDNVAFG-LRLRGVPKAERRARAEELLALVGLADFARR---RIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQiiaeMQAL----QRETGTAMIWITHDlgvVAE---LADRIAVM-- 232
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQ----MQELlldvWQRTGKGVFLITHS---VEEalfLATRLVVMsp 210
|
....*..
gi 1208293942 233 YAGDIVE 239
Cdd:COG4525 211 GPGRIVE 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-232 |
1.05e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 110.07 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 2 TRDRAPVLEVRNLQTVFhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLL 81
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS----TLLNLLLGFVDPTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPPEAQRRLrgsaLAMIFQdplttlNPVLTIGeQMAEAILEHARVA-PAEVRRrcidSLRRVGITS--------PETRL 152
Cdd:TIGR02857 388 DADADSWRDQ----IAWVPQ------HPFLFAG-TIAENIRLARPDAsDAEIRE----ALERAGLDEfvaalpqgLDTPI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 153 SQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLgVVAELADRIAVM 232
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-247 |
1.36e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.84 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 2 TRDRAPVLEVRNLqtVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVagFS-ILGLVDRPgeiTRGEVIFKGrdl 80
Cdd:PRK13632 1 IKNKSVMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKST--ISkILTGLLKP---QSGEIKIDG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALPPEAQRRLRGSaLAMIFQDPLTTLnpvltIGEQMAEAI---LEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPH 157
Cdd:PRK13632 71 ITISKENLKEIRKK-IGIIFQNPDNQF-----IGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAeLADRIAVMYAGDI 237
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
250
....*....|
gi 1208293942 238 VEIGATDDVL 247
Cdd:PRK13632 221 IAQGKPKEIL 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-250 |
1.38e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.62 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSilglvdrpgEITRGEVIFKGRDLLALPPeaqrRLRGsaLA 97
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKStllrmVAGLE---------RITSGEIWIGGRVVNELEP----ADRD--IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 98 MIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSP 177
Cdd:PRK11650 80 MVFQN--YALYPHMSVRENMAYG-LKIRGMPKAEIEERVAEAARILEL---EPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 178 DLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-245 |
1.40e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTvfhdLRGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSIlglvdrPGEITRGEVIFKGRDLLAL 83
Cdd:COG4136 2 LSLENLTI----TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKStllaaIAGTLS------PAFSASGEVLLNGRRLTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEaQRRLrgsalAMIFQDPLttLNPVLTIGEQMAEAIleHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGM 163
Cdd:COG4136 72 PAE-QRRI-----GILFQDDL--LFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDlgvvaeLADRIAvmyAGDIVEIGAT 243
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD------EEDAPA---AGRVLDLGNW 209
|
..
gi 1208293942 244 DD 245
Cdd:COG4136 210 QH 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
23-249 |
1.77e-26 |
|
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: 106.32 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEAQRRLrgsalAMIFQD 102
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTT-IRMLTTLLRP---TSGTARVAGYDVVREPRKVRRSI-----GIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 PltTLNPVLTIGEQMaeaiLEHAR---VAPAEVRRRCIDSLRRVGITSPETRLSQYpheFSGGMRQRVAIAIALLNSPDL 179
Cdd:TIGR01188 75 A--SVDEDLTGRENL----EMMGRlygLPKDEAEERAEELLELFELGEAADRPVGT---YSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRR 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-241 |
1.81e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 104.76 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlvdRPG-EITRGEVIFKGRDLLALPPEa 87
Cdd:COG0396 1 LEIKNLHVSVEGK----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPKyEVTSGSILLDGEDILELSPD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAmiFQDP-----LTTLNpVLTIgeqMAEAILEhARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHE-FSG 161
Cdd:COG0396 73 ERARAGIFLA--FQYPveipgVSVSN-FLRT---ALNARRG-EELSAREFLKLLKEKMKELGL--DEDFLDRYVNEgFSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIA-IALLNsPDLIIADEPTTALDV-TIqgQIIAE-MQALqRETGTAMIWITHDLGVVAEL-ADRIAVMYAGDI 237
Cdd:COG0396 144 GEKKRNEILqMLLLE-PKLAILDETDSGLDIdAL--RIVAEgVNKL-RSPDRGILIITHYQRILDYIkPDFVHVLVDGRI 219
|
....
gi 1208293942 238 VEIG 241
Cdd:COG0396 220 VKSG 223
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
237-321 |
2.22e-26 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 99.74 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 237 IVEIGATDDVLDRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPPLSARPVGCAFHPRCDRATDICHRAEPPDTAGPAGR 316
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEGH 81
|
....*
gi 1208293942 317 RWRCH 321
Cdd:TIGR01727 82 RVACH 86
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-241 |
4.41e-26 |
|
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: 102.61 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlvdRPG-EITRGEVIFKGRDLLALPPEa 87
Cdd:cd03217 1 LEIKDLHVSVGGKE----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKyEVTEGEILFKGEDITDLPPE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGsaLAMIFQDPLTTlnPVLTIgeqmaeaileharvapaevrrrcIDSLRRVGITspetrlsqypheFSGGMRQRV 167
Cdd:cd03217 73 ERARLG--IFLAFQYPPEI--PGVKN-----------------------ADFLRYVNEG------------FSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVT---IQGQIIAEMqalqRETGTAMIWITHdLGVVAEL--ADRIAVMYAGDIVEIG 241
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDalrLVAEVINKL----REEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSG 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-241 |
5.06e-26 |
|
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: 102.83 E-value: 5.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL----EPDAGFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRgsalamiFQDPLTTLNPVLTIGEQMAEAILEHArVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVA 168
Cdd:cd03266 78 RRLG-------FVSDSTGLYDRLTARENLEYFAGLYG-LKGDELTARLEELADRLGM---EELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQgQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMAT-RALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-247 |
7.52e-26 |
|
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: 103.00 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLrgsaLAMIFQDPL- 104
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQEPVl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 --TTL--NPVLTIGEQMAEAILEHARVAPAEvrrRCIDSLrrvgitsPE---TRLSQYPHEFSGGMRQRVAIAIALLNSP 177
Cdd:cd03249 89 fdGTIaeNIRYGKPDATDEEVEEAAKKANIH---DFIMSL-------PDgydTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 178 DLIIADEPTTALDVTIQGQIiaeMQALQR-ETGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVL 247
Cdd:cd03249 159 KILLLDEATSALDAESEKLV---QEALDRaMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-218 |
1.16e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.79 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSilglvdRPgeiTRGEVIFKGRDLL 81
Cdd:COG4133 1 MMLEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKTtllriLAGLL------PP---SAGEVLWNGEPIR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPPEAQRRLrgsalAMIFQDPLttLNPVLTIGEQmaeaiLE-HARVAPAEVRRRCIDS-LRRVGITSpetRLSQYPHEF 159
Cdd:COG4133 68 DAREDYRRRL-----AYLGHADG--LKPELTVREN-----LRfWAALYGLRADREAIDEaLEAVGLAG---LADLPVRQL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQAlQRETGTAMIWITHD 218
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-246 |
1.89e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDlrgAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKG-------RDL 80
Cdd:PRK13639 1 ILETRDLKYSYPD---GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL-KP---TSGEVLIKGepikydkKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALppeaqRRLRGsalaMIFQDPLTTL-NPvlTIGEQMAEAILeHARVAPAEVRRRCIDSLRRVGITSPETRLsqyPHEF 159
Cdd:PRK13639 74 LEV-----RKTVG----IVFQNPDDQLfAP--TVEEDVAFGPL-NLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:PRK13639 139 SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIK 217
|
....*..
gi 1208293942 240 IGATDDV 246
Cdd:PRK13639 218 EGTPKEV 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-249 |
2.97e-25 |
|
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: 101.41 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGsalaMIFQDPlTT 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKS----TLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG----VVLQEN-VL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNPvlTIGEQMAEAileharvAPAEVRRRCIDSLRRVGITS-----PE---TRLSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:cd03252 88 FNR--SIRDNIALA-------DPGMSMERVIEAAKLAGAHDfiselPEgydTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAEMQALQreTGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
27-241 |
3.06e-25 |
|
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: 100.73 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGeVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEAQRRLrgsalAMIFQDPltT 106
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTL-MRILATLTPP---SSGTIRIDGQDVLKQPQKLRRRI-----GYLPQEF--G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNPVLTIGEQMAE-AILEhaRVAPAEVRRRCIDSLRRVGITspeTRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:cd03264 83 VYPNFTVREFLDYiAWLK--GIPSKEVKARVDEVLELVNLG---DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 186 TTALDVtiqGQIIAeMQALQRETGTAMIWI--THDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03264 158 TAGLDP---EERIR-FRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-255 |
6.08e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.28 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEI------TRGEVIFKGRDLLALPPEAQRRLRGsalaMIFQ 101
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKS----TLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKLRKEVG----MVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 DPlttlNPV--LTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGI-TSPETRLSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:PRK14246 98 QP----NPFphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAEMQALQREtgTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYT 255
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-261 |
7.41e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.19 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 33 LTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPPeAQRrlrgsALAMIFQDplTTLNPVLT 112
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLFIGEKRMNDVPP-AER-----GVGMVFQS--YALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 113 IGEQMAEAiLEHARVAPAEVRRRCIDSLRrvgITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVT 192
Cdd:PRK11000 92 VAENMSFG-LKLAGAKKEEINQRVNQVAE---VLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 193 IQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLLNS 261
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-257 |
1.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.96 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEA 87
Cdd:PRK13650 4 IIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGsalaMIFQDPLTTLnpvltIGEQMAEAI---LEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMR 164
Cdd:PRK13650 79 IRHKIG----MVFQNPDNQF-----VGATVEDDVafgLENKGIPHEEMKERVNEALELVGMQDFKER---EPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAeLADRIAVMYAGDiVEIGATd 244
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTST- 223
|
250
....*....|...
gi 1208293942 245 dvldrPRHPYTRG 257
Cdd:PRK13650 224 -----PRELFSRG 231
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
9-229 |
1.52e-24 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 99.39 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVF--HDLRGA-WPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILG--LVDRpGEI---TRGEVIfkgrDL 80
Cdd:TIGR02324 2 LEVEDLSKTFtlHQQGGVrLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnyLPDS-GRIlvrHEGAWV----DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALPPEAQRRLRGSALAMIFQdpLTTLNPVLTIGEQMAEAILEHArVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFS 160
Cdd:TIGR02324 77 AQASPREVLEVRRKTIGYVSQ--FLRVIPRVSALEVVAEPLLERG-VPREAARARARELLARLNI--PERLWHLPPATFS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRI 229
Cdd:TIGR02324 152 GGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-249 |
2.10e-24 |
|
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: 103.64 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDlRGAwPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQ 88
Cdd:TIGR02203 331 VEFRNVTFRYPG-RDR-PALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgsALAMIFQDpLTTLNPvlTIGEQMAEAilEHARVAPAEVRRRCIDS-LRRVGITSPE---TRLSQYPHEFSGGMR 164
Cdd:TIGR02203 405 RR----QVALVSQD-VVLFND--TIANNIAYG--RTEQADRAEIERALAAAyAQDFVDKLPLgldTPIGENGVLLSGGQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 165 QRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTamIWITHDLGVVaELADRIAVMYAGDIVEIGATD 244
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTI-EKADRIVVMDDGRIVERGTHN 552
|
....*
gi 1208293942 245 DVLDR 249
Cdd:TIGR02203 553 ELLAR 557
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-249 |
2.23e-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: 99.23 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgsALAMIFQDplTTL-NPvlTIGEQMA--------EAILEHARVApaevrrrCIDslrRVGITSPE---TRLSQYP 156
Cdd:cd03253 74 RR----AIGVVPQD--TVLfND--TIGYNIRygrpdatdEEVIEAAKAA-------QIH---DKIMRFPDgydTIVGERG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQreTGTAMIWITHDLGVVAElADRIAVMYAGD 236
Cdd:cd03253 136 LKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
250
....*....|...
gi 1208293942 237 IVEIGATDDVLDR 249
Cdd:cd03253 213 IVERGTHEELLAK 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-246 |
2.73e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLlalppeAQRRLRGSAL----AMIFQD 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL-KP---TSGKIIIDGVDI------TDKKVKLSDIrkkvGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 PLTTLnpvltigeqMAEAILEHARVAPA-------EVRRRCIDSLRRVGItSPETRLSQYPHEFSGGMRQRVAIAIALLN 175
Cdd:PRK13637 92 PEYQL---------FEETIEKDIAFGPInlglseeEIENRVKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 176 SPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDV 246
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
26-249 |
9.65e-24 |
|
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: 97.30 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLrgsaLAMIFQDPL- 104
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ----IGLVSQDVFl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 --TTLNPVLTIGEQMA--EAILEHARVAPAEvrrRCIDSLrrvgitsPE---TRLSQYPHEFSGGMRQRVAIAIALLNSP 177
Cdd:cd03251 88 fnDTVAENIAYGRPGAtrEEVEEAARAANAH---EFIMEL-------PEgydTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 178 DLIIADEPTTALDVTIQGQIIAEMQALQRETgTAMIwITHDLGVVaELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAHRLSTI-ENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-235 |
1.18e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPGEITrGEVIFKGRDLLAlppe 86
Cdd:PRK13549 4 YLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHGTYE-GEIIFEGEELQA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 aqRRLRGS---ALAMIFQDplTTLNPVLTIGEQM--AEAILEHARVAPAEVRRRCIDSLRRVGIT-SPETRLSQYphefS 160
Cdd:PRK13549 74 --SNIRDTeraGIAIIHQE--LALVKELSVLENIflGNEITPGGIMDYDAMYLRAQKLLAQLKLDiNPATPVGNL----G 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTAL---DVTIQGQIIAEMQAlqreTGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKA----HGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-251 |
1.47e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.59 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPP 85
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EaQRRLRGSALAM----IFQDplttlnpvLTIGE--QMAEaileHARVAPAEVRRRcidsLRRVGITSP--ETRLSQYPH 157
Cdd:COG0410 73 H-RIARLGIGYVPegrrIFPS--------LTVEEnlLLGA----YARRDRAEVRAD----LERVYELFPrlKERRRQRAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALdvtiQGQIIAEM-QALQR--ETGTAMIWITHDLGVVAELADRIAVMYA 234
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL----APLIVEEIfEIIRRlnREGVTILLVEQNARFALEIADRAYVLER 211
|
250
....*....|....*..
gi 1208293942 235 GDIVEIGATDDVLDRPR 251
Cdd:COG0410 212 GRIVLEGTAAELLADPE 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-241 |
2.31e-23 |
|
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: 95.64 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 31 LSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvDRPgeiTRGEVIFKGRDLLALPPEAQrrlrgsALAMIFQDplT 105
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKStllnlIAGF------ETP---QSGRVLINGVDVTAAPPADR------PVSMLFQE--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVLTIGEQMAEAILEHARVAPaEVRRRCIDSLRRVGITSPETRLsqyPHEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:cd03298 80 NLFAHLTVEQNVGLGLSPGLKLTA-EDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 186 TTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
26-238 |
2.67e-23 |
|
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: 95.73 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQRRLRGSALamifQDPLT 105
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY-KP---TSGSVLLDGTDIRQLDPADLRRNIGYVP----QDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 ---TLNPVLTIGEQMA--EAILEHARVApaevrrrCIDSLRRVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:cd03245 90 fygTLRDNITLGAPLAddERILRAAELA-------GVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLGVVaELADRIAVMYAGDIV 238
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-247 |
3.12e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLqTVFhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDrpGEIT--RGEVIFKGRDLLALP 84
Cdd:PRK13548 1 AMLEARNL-SVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALS--GELSpdSGEVRLNGRPLADWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLRG-----SALAmiFqdPLTTLNPV------LTIGEQMAEAILEHArvapaevrrrcidsLRRVGITSPETRLs 153
Cdd:PRK13548 71 PAELARRRAvlpqhSSLS--F--PFTVEEVVamgrapHGLSRAEDDALVAAA--------------LAQVDLAHLAGRD- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 154 qYPhEFSGGMRQRVAIAIALL------NSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELAD 227
Cdd:PRK13548 132 -YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYAD 209
|
250 260
....*....|....*....|
gi 1208293942 228 RIAVMYAGDIVEIGATDDVL 247
Cdd:PRK13548 210 RIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-250 |
3.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 14 LQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDllALPPEAQRRLRg 93
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL-RP---QKGKVLVSGID--TGDFSKLQGIR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 94 SALAMIFQDPLTTLnpvltIGEQMAEAIL---EHARVAPAEVRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIA 170
Cdd:PRK13644 77 KLVGIVFQNPETQF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGL---EKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 171 IALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVaELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-271 |
4.04e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDR-PGEITRGEVIFKGRDLLALP 84
Cdd:PRK14271 19 APAMAAVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYRYSGDVLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLRgsaLAMIFQDPlttlNPV-LTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGI-TSPETRLSQYPHEFSGG 162
Cdd:PRK14271 95 DVLEFRRR---VGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtgTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250 260
....*....|....*....|....*....
gi 1208293942 243 TDDVLDRPRHPYTRGLLNSVPGDTARGER 271
Cdd:PRK14271 246 TEQLFSSPKHAETARYVAGLSGDVKDAKR 274
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-246 |
4.67e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLqtvfhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIFKGRDL-LALP 84
Cdd:COG1129 254 EVVLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA-DPA---DSGEIRLDGKPVrIRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRlrGsaLAMIFQDPLTT-LNPVLTIGEQMAEAILEHAR----VAPAEVRRRCIDSLRRVGI--TSPETRLSQyph 157
Cdd:COG1129 322 RDAIRA--G--IAYVPEDRKGEgLVLDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRIktPSPEQPVGN--- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 eFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:COG1129 395 -LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
....*....
gi 1208293942 238 VEIGATDDV 246
Cdd:COG1129 473 VGELDREEA 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-246 |
6.14e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.95 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKS--VagfSIL-GLVdRPgeiTRGEVIFKGRdlla 82
Cdd:COG3845 3 PPALELRGITKRFGGVV----ANDDVSLTVRPGEIHALLGENGAGKStlM---KILyGLY-QP---DSGEILIDGK---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 lppeaQRRLRGSALA------MIFQDPltTLNPVLTIgeqmAEAIL------EHARVAPAEVRRRCIDSLRRVGItspET 150
Cdd:COG3845 68 -----PVRIRSPRDAialgigMVHQHF--MLVPNLTV----AENIVlgleptKGGRLDRKAARARIRELSERYGL---DV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 151 RLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALdvTIQ--GQIIAEMQALqRETGTAMIWITHDLGVVAELADR 228
Cdd:COG3845 134 DPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRL-AAEGKSIIFITHKLREVMAIADR 210
|
250
....*....|....*...
gi 1208293942 229 IAVMYAGDIVEIGATDDV 246
Cdd:COG3845 211 VTVLRRGKVVGTVDTAET 228
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
238-302 |
1.72e-22 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 89.00 E-value: 1.72e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 238 VEIGATDDVLDRPRHPYTRGLLNSVPGDTARGERLRQIEGTAPPLSARPVGCAFHPRCDRATDIC 302
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-251 |
2.21e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.03 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLqTVFhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDrpGEI--TRGEVIFKGRDLLALPPE 86
Cdd:COG4559 2 LEAENL-SVR---LGGRTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLT--GELtpSSGEVRLNGRPLAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRG-----SALAmiFqdPLTTLNpVLTIGeqmaeaiLEHARVAPAEVRRRCIDSLRRVGITSPETRLsqYPhEFSG 161
Cdd:COG4559 72 ELARRRAvlpqhSSLA--F--PFTVEE-VVALG-------RAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 162 GMRQRVAIAIALL-------NSPDLIIADEPTTALDVTIQGQIiaeMQALQR--ETGTAMIWITHDLGVVAELADRIAVM 232
Cdd:COG4559 137 GEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAV---LRLARQlaRRGGGVVAVLHDLNLAAQYADRILLL 213
|
250
....*....|....*....
gi 1208293942 233 YAGDIVEIGATDDVLDRPR 251
Cdd:COG4559 214 HQGRLVAQGTPEEVLTDEL 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-229 |
8.90e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 91.76 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDPL--T 105
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLN-------PVLTIGEQMAEAileharvapaevRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:PRK10584 102 TLNalenvelPALLRGESSRQS------------RNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRI 229
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-286 |
1.20e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRDLLALppEAQRRLRGsalaMIFQDplTTL 107
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ----TSGHIRFHGTDVSRL--HARDRKVG----FVFQH--YAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMAEAIL---EHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIADE 184
Cdd:PRK10851 86 FRHMTVFDNIAFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 185 PTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLdrpRHPYTR------GL 258
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW---REPATRfvlefmGE 239
|
250 260
....*....|....*....|....*...
gi 1208293942 259 LNSVPGdTARGERLrQIEGTAPPLSARP 286
Cdd:PRK10851 240 VNRLQG-TIRGGQF-HVGAHRWPLGYTP 265
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-264 |
1.72e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.83 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpGEITR--GEVIFKGRDLLAL--- 83
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLEL-NEEARveGEVRLFGRNIYSPdvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEAQRRLrgsalAMIFQDPlttlNPV--LTIGEQMAEAILEHARVAP-AEVRRRCIDSLRRVGI-TSPETRLSQYPHEF 159
Cdd:PRK14267 80 PIEVRREV-----GMVFQYP----NPFphLTIYDNVAIGVKLNGLVKSkKELDERVEWALKKAALwDEVKDRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIiaEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKI--EELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|....*
gi 1208293942 240 IGATDDVLDRPRHPYTRGLLNSVPG 264
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYVTGALG 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-242 |
1.86e-21 |
|
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: 90.63 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEaqrRLRgSALAMIFQDPLT 105
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV----ELSSGSILIDGVDISKIGLH---DLR-SRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 ---TLNPVLTIGEQMAEAILEHArvapaevrrrcidsLRRVG----ITSPETRLSQYPHE----FSGGMRQRVAIAIALL 174
Cdd:cd03244 90 fsgTIRSNLDPFGEYSDEELWQA--------------LERVGlkefVESLPGGLDTVVEEggenLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 175 NSPDLIIADEPTTALDVTIQGQIiaeMQALQRE-TGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGA 242
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALI---QKTIREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-238 |
2.15e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFH-DLRGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfSILglvdrpgeITRGEVIFKGRDLLA 82
Cdd:COG1101 2 LELKNLSKTFNpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKStllnaIAG-SLP--------PDSGSILIDGKDVTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 LPPEAqrrlRGSALAMIFQDPLTTLNPVLTIGEQMAEAILEHAR------VAPAEvRRRCIDSLRRVGItSPETRLSQYP 156
Cdd:COG1101 73 LPEYK----RAKYIGRVFQDPMMGTAPSMTIEENLALAYRRGKRrglrrgLTKKR-RELFRELLATLGL-GLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALD-------VTIQGQIIAEMQaLqretgTAMIwITHDLGVVAELADRI 229
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvLELTEKIVEENN-L-----TTLM-VTHNMEQALDYGNRL 219
|
....*....
gi 1208293942 230 AVMYAGDIV 238
Cdd:COG1101 220 IMMHEGRII 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-249 |
4.96e-21 |
|
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: 93.66 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAqrrlRGSALAMIFQDPlt 105
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW-PP---TAGSVRLDGADLSQWDREE----LGRHIGYLPQDV-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlnpVL---TIGEQMA-------EAILEHARVAPA-EVrrrcIDSLrrvgitsP---ETRLSQYPHEFSGGMRQRVAIAI 171
Cdd:COG4618 416 ----ELfdgTIAENIArfgdadpEKVVAAAKLAGVhEM----ILRL-------PdgyDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 172 ALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-247 |
8.52e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.15 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLqtVF-HDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPE 86
Cdd:PRK13642 4 ILEVENL--VFkYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF----EEFEGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRlrgsALAMIFQDPLTTLnpvltIGEQMAEAI---LEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGM 163
Cdd:PRK13642 78 NLRR----KIGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGAT 243
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
....
gi 1208293942 244 DDVL 247
Cdd:PRK13642 225 SELF 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-247 |
1.01e-20 |
|
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: 89.14 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPGEitrGEVIFKGRDLLALPPEAQ 88
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV-KPDS---GKILLDGQDITKLPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGSAL---AMIFQDplttlnpvLTIgEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYpheFSGGMRQ 165
Cdd:cd03218 73 ARLGIGYLpqeASIFRK--------LTV-EENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASS---LSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALD----VTIQgQIIAEMQalQRETGtamIWIT-HDLGVVAELADRIAVMYAGDIVEI 240
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDpiavQDIQ-KIIKILK--DRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAE 214
|
....*..
gi 1208293942 241 GATDDVL 247
Cdd:cd03218 215 GTPEEIA 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-248 |
1.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 24 AWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGrdlLALPPEAQRRLRgSALAMIFQDP 103
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE----KVKSGEIFYNN---QAITDDNFEKLR-KHIGIVFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 104 LTTLnpvltIGEQMAEAI---LEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:PRK13648 93 DNQF-----VGSIVKYDVafgLENHAVPYDEMHRRVSEALKQVDMLE---RADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLD 248
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-249 |
2.46e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsilglVDRPgeiTRGEVIFKGRD--LLALppeaqrrlrGSALami 99
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKStllklIAG------ILEP---TSGRVEVNGRVsaLLEL---------GAGF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 100 fqdplttlNPVLTiGEQ---MAEAILEHARvapAEVRRRcIDSLRrvgitspetrlsqyphEFSG--------------G 162
Cdd:COG1134 100 --------HPELT-GREniyLNGRLLGLSR---KEIDEK-FDEIV----------------EFAElgdfidqpvktyssG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
....*..
gi 1208293942 243 TDDVLDR 249
Cdd:COG1134 230 PEEVIAA 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-249 |
2.61e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDlrgAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvdrpGEITRGEVIFKGRdllALPPEA 87
Cdd:PRK13647 4 IIEVEDLHFRYKD---GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI----YLPQRGRVKVMGR---EVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRgSALAMIFQDPLTTLNPVlTIGEQMAEAILeHARVAPAEVRRRCIDSLRRVGITSPETRLsqyPHEFSGGMRQRV 167
Cdd:PRK13647 74 EKWVR-SKVGLVFQDPDDQVFSS-TVWDDVAFGPV-NMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
..
gi 1208293942 248 DR 249
Cdd:PRK13647 227 DE 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-247 |
2.87e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDlrgAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRdllalPPEA 87
Cdd:PRK13636 5 ILKVEELNYNYSD---GTHALKGININIKKGEVTAILGGNGAGKSTL-FQNLNGILKP---SSGRILFDGK-----PIDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRR----LRgSALAMIFQDPLTTLNPVlTIGEQMAEAILeHARVAPAEVRRRCIDSLRRVGITspetRLSQYP-HEFSGG 162
Cdd:PRK13636 73 SRKglmkLR-ESVGMVFQDPDNQLFSA-SVYQDVSFGAV-NLKLPEDEVRKRVDNALKRTGIE----HLKDKPtHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*
gi 1208293942 243 TDDVL 247
Cdd:PRK13636 226 PKEVF 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-218 |
3.88e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 3 RDRAPVLEVRNLqtvfHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLA 82
Cdd:PRK10247 2 QENSPLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKS----TLLKIVASLISPTSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 LPPEAQRRlrgsalamifQDPLTTLNPVLtIGEQMAEAILeharvAPAEVRR------RCIDSLRRVGItsPETRLSQYP 156
Cdd:PRK10247 74 LKPEIYRQ----------QVSYCAQTPTL-FGDTVYDNLI-----FPWQIRNqqpdpaIFLDDLERFAL--PDTILTKNI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 157 HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALD---VTIQGQIIaemQALQRETGTAMIWITHD 218
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHNVNEII---HRYVREQNIAVLWVTHD 197
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-238 |
4.13e-20 |
|
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: 87.39 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 14 LQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRdllaLPPEAQRRLRG 93
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-LKILSGLLQP---TSGEVRVAGL----VPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 94 SALAMIFQDplTTLNPVLTIGEQMAeaILEHA-RVAPAEVRRRcIDSLrrVGITSPETRLSQYPHEFSGGMRQRVAIAIA 172
Cdd:cd03267 95 RIGVVFGQK--TQLWWDLPVIDSFY--LLAAIyDLPPARFKKR-LDEL--SELLDLEELLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 173 LLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-239 |
4.60e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.30 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDPLTT 106
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL-KP---TTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LnpvltIGEQMAEAIL---EHARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIAD 183
Cdd:PRK13646 98 L-----FEDTVEREIIfgpKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 184 EPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-249 |
4.71e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKG-------RDLLALPPEaqrrlrgsaLAM 98
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL-RP---QKGAVLWQGkpldyskRGLLALRQQ---------VAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 99 IFQDPLTTLNpVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGitspETRLSQYPHE-FSGGMRQRVAIAIALLNSP 177
Cdd:PRK13638 82 VFQDPEQQIF-YTDIDSDIAFS-LRNLGVPEAEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 178 DLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-262 |
4.73e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPeaq 88
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKS----TLLKCFARLLTPQSGTVFLGDKPISMLSS--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLrGSALAMIFQDPLTT------------LNPVLTIGEQMAEAilEHARVAPAeVRRRCIDSLrrvgitsPETRLSqyp 156
Cdd:PRK11231 72 RQL-ARRLALLPQHHLTPegitvrelvaygRSPWLSLWGRLSAE--DNARVNQA-MEQTRINHL-------ADRRLT--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 hEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGD 236
Cdd:PRK11231 138 -DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
250 260
....*....|....*....|....*.
gi 1208293942 237 IVEIGATDDVLdrprhpyTRGLLNSV 262
Cdd:PRK11231 216 VMAQGTPEEVM-------TPGLLRTV 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-243 |
5.69e-20 |
|
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: 86.45 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 32 SLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPeAQRrlrgsALAMIFQDplTTLNPVL 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS----TLLNLIAGFIEPASGSIKVNDQSHTGLAP-YQR-----PVSMLFQE--NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 112 TIGEQMAEAILEHARVApAEVRRRCIDSLRRVGITSPETRLsqyPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDV 191
Cdd:TIGR01277 86 TVRQNIGLGLHPGLKLN-AEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 192 TIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGAT 243
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-241 |
5.71e-20 |
|
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: 86.94 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpGEITRGEVIFKGRdllalPPEAQRRLRGSAlamiFQDPLTTL 107
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG-GGTTSGQILFNGQ-----PRKPDQFQKCVA----YVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMA-EAILEHARVAPAEVRRRCID--SLRRVGITSPETRLSQYpheFSGGMRQRVAIAIALLNSPDLIIADE 184
Cdd:cd03234 93 LPGLTVRETLTyTAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 185 PTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-241 |
5.73e-20 |
|
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: 85.44 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQtvFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALppEAQ 88
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPVSDL--EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgSALAMIFQDPL---TTLNPvlTIGEQmaeaileharvapaevrrrcidslrrvgitspetrlsqypheFSGGMRQ 165
Cdd:cd03247 73 LS---SLISVLNQRPYlfdTTLRN--NLGRR------------------------------------------FSGGERQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEM-QALQRETgtaMIWITHDLGVVaELADRIAVMYAGDIVEIG 241
Cdd:cd03247 106 RLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVLKDKT---LIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-250 |
6.08e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLV---DRPgeiTRGEVIFKGRDLlalpp 85
Cdd:PRK11432 7 VVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLVaglEKP---TEGQIFIDGEDV----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 eAQRRLRGSALAMIFQDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQ 165
Cdd:PRK11432 71 -THRSIQQRDICMVFQS--YALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDR---YVDQISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDD 245
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
....*
gi 1208293942 246 VLDRP 250
Cdd:PRK11432 224 LYRQP 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-249 |
6.20e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.41 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 3 RDRAPVLEVRNLQ--TVFHDLR----GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgfsiLGLVDRPGEITRGEVIFK 76
Cdd:PRK13657 320 RDPPGAIDLGRVKgaVEFDDVSfsydNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRVFDPQSGRILID 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 77 GRDLLALPPEAQRRlrgsALAMIFQDPL---TTLNPVLTIGEQMA--EAILEHARVAPA----EVRRRCIDSlrRVGits 147
Cdd:PRK13657 396 GTDIRTVTRASLRR----NIAVVFQDAGlfnRSIEDNIRVGRPDAtdEEMRAAAERAQAhdfiERKPDGYDT--VVG--- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 148 peTRLSQypheFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIwITHDLGVVAElAD 227
Cdd:PRK13657 467 --ERGRQ----LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFI-IAHRLSTVRN-AD 537
|
250 260
....*....|....*....|..
gi 1208293942 228 RIAVMYAGDIVEIGATDDVLDR 249
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVAR 559
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-250 |
7.01e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQtvfHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPEA 87
Cdd:PRK13652 3 LIETRDLC---YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTL-FRHFNGILKP---TSGSVLIRGEPITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGsalaMIFQDP-----LTTLNPVLTIGE---QMAEAILEHaRVAPAevrrrcidsLRRVGITSPETRLsqyPHEF 159
Cdd:PRK13652 76 VRKFVG----LVFQNPddqifSPTVEQDIAFGPinlGLDEETVAH-RVSSA---------LHMLGLEELRDRV---PHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
250
....*....|.
gi 1208293942 240 IGATDDVLDRP 250
Cdd:PRK13652 219 YGTVEEIFLQP 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-249 |
8.58e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.08 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLlalppeaqRRLRGSALAMifQDPLT 105
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKS----TIANLLTRFYDIDEGEILLDGHDL--------RDYTLASLRN--QVALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVL---TIGEQMA---------EAILEHARVAPAevrRRCIDSLRRvGItspETRLSQYPHEFSGGMRQRVAIAIAL 173
Cdd:PRK11176 423 SQNVHLfndTIANNIAyarteqysrEQIEEAARMAYA---MDFINKMDN-GL---DTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 174 L-NSPDLIIaDEPTTALDVTIQGQIIAEMQALQRETgTAMIwITHDLGVVaELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:PRK11176 496 LrDSPILIL-DEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTI-EKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-244 |
8.64e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.88 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVdRPGEITRGEVIFKGRDLLAlppEA 87
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGV-YPHGTWDGEIYWSGSPLKA---SN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDplTTLNPVLTIGEQM---AEAILEHARVAPAEVRRRCIDSLRRVGIT-SPETRLSQyphEFSGGM 163
Cdd:TIGR02633 72 IRDTERAGIVIIHQE--LTLVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDaDNVTRPVG---DYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTAL---DVTIQGQIIAEMQAlqreTGTAMIWITHDLGVVAELADRIAVMYAGDivEI 240
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKA----HGVACVYISHKLNEVKAVCDTICVIRDGQ--HV 220
|
....
gi 1208293942 241 GATD 244
Cdd:TIGR02633 221 ATKD 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-238 |
8.88e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.08 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlVDRPgeiTRGEVIFKGRDLLALPPEAQRRLRgSALAMIFQD 102
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERP---SAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 PLTTLNPVLTIGEQMAEAIlehARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLII---AGASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQReTGTAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-249 |
9.74e-20 |
|
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: 86.13 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLrgsaLAMIFQDPLT 105
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKT----TLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM----IGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlnpvltigeqMAEAILEHARVAPAEVRR-RCIDSLRRVGIT-----SP---ETRLSQYPHEFSGGMRQRVAIAIALLNS 176
Cdd:cd03254 89 -----------FSGTIMENIRLGRPNATDeEVIEAAKEAGAHdfimkLPngyDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 177 PDLIIADEPTTALDVTIQGQIIAEMQALQRetGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-249 |
2.67e-19 |
|
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: 88.34 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRGAW----PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLL 81
Cdd:COG5265 348 APPLVVGGGEVRFENVSFGYdperPILKGVSFEVPAGKTVAIVGPSGAGKS----TLARLLFRFYDVTSGRILIDGQDIR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPPEAQRRlrgsALAMIFQDPlttlnpVL---TIGEQMA--------EAILEHARVAPAEvrrRCIDSL-----RRVGi 145
Cdd:COG5265 424 DVTQASLRA----AIGIVPQDT------VLfndTIAYNIAygrpdaseEEVEAAARAAQIH---DFIESLpdgydTRVG- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 146 tspETRLsqyphEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETgTAMIwITHDLGVVAEl 225
Cdd:COG5265 490 ---ERGL-----KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR-TTLV-IAHRLSTIVD- 558
|
250 260
....*....|....*....|....
gi 1208293942 226 ADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:COG5265 559 ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-250 |
5.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPGEITRGEVIFKGRDLLAlppEAQRRLRgSALAMIFQDPLT 105
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-LPDDNPNSKITVDGITLTA---KTVWDIR-EKVGIVFQNPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVlTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:PRK13640 96 QFVGA-TVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLD---YIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 186 TTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGvVAELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-251 |
7.07e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 7.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPe 86
Cdd:COG1137 2 MTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV-KP---DSGRIFLDGEDITHLPM- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRG-SAL---AMIFQDplttlnpvLTIGEQMAeAILEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGG 162
Cdd:COG1137 73 HKRARLGiGYLpqeASIFRK--------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITH---LRKSKAYSLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALD---VT-IQgQIIAEMQalQRETGtamIWIT-HD----LGVVaelaDRIAVMY 233
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQ-KIIRHLK--ERGIG---VLITdHNvretLGIC----DRAYIIS 210
|
250
....*....|....*...
gi 1208293942 234 AGDIVEIGATDDVLDRPR 251
Cdd:COG1137 211 EGKVLAEGTPEEILNNPL 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-250 |
7.23e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.47 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLlalpPEAQRRLRGSALAMIFQDPLT 105
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPL----VQYDHHYLHRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlnpvltIGEQMAEAILEHARVAPAE-----VRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:TIGR00958 567 -------FSGSVRENIAYGLTDTPDEeimaaAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 181 IADEPTTALDVTIQgqiiAEMQALQRETGTAMIWITHDLGVVaELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:TIGR00958 640 ILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-246 |
7.80e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 33 LTLHAGEVLGLVGESGSGKSVAGFSILGLVdRP--GEITRGE-VIFKGRDLLALPPEaQRRLrgsalAMIFQD----PLT 105
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLT-RPqkGRIVLNGrVLFDAEKGICLPPE-KRRI-----GYVFQDarlfPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVLTIGeqMAEAILEHarvapaevrrrcIDSLrrVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:PRK11144 92 KVRGNLRYG--MAKSMVAQ------------FDKI--VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 186 TTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDV 246
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-283 |
9.34e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.69 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRP--GEITRGE-VIFKGRDLLALPPeaqrrLRgSALAMIFQDP 103
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-QPtsGTVTIGErVITAGKKNKKLKP-----LR-KKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 104 lttlnpvltiGEQMAEAILE--------HARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMRQRVAIAIALLN 175
Cdd:PRK13634 95 ----------EHQLFEETVEkdicfgpmNFGVSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 176 SPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRPRHPYT 255
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
250 260 270
....*....|....*....|....*....|.
gi 1208293942 256 RGLlnSVPGDTARGERLRQIEG---TAPPLS 283
Cdd:PRK13634 243 IGL--DLPETVKFKRALEEKFGisfPKPCLT 271
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-237 |
1.15e-18 |
|
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: 83.29 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 22 RGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLlalpPEAQRRLRGSALAMIFQ 101
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPI----SQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 DPLT---TLNPVLTIGEQMA--EAILEHARVAPAevrrrciDSLRRVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNS 176
Cdd:cd03248 96 EPVLfarSLQDNIAYGLQSCsfECVKEAAQKAHA-------HSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 177 PDLIIADEPTTALDVTIQGQIiaeMQALQR-ETGTAMIWITHDLGVVaELADRIAVMYAGDI 237
Cdd:cd03248 169 PQVLILDEATSALDAESEQQV---QQALYDwPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
26-232 |
1.53e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsilglVDRPgeiTRGEVIFKGRDLLALPPeaQRrlrgSALAMIF 100
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKStllkvLAG------VLRP---TSGTVRRAGGARVAYVP--QR----SEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 101 qdPLTTLNPVlTIGEQMAEAILEHARvapAEVRRRCIDSLRRVGITSPETRLSQyphEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:NF040873 71 --PLTVRDLV-AMGRWARRGLWRRLT---RDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAeLADRIAVM 232
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-249 |
1.54e-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: 86.01 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeiTRGEVI-------------- 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP--TSGRIIyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 75 --FKGR--------------DLLALPPEAQRRLRgSALAMIFQDPLTtLNPVLTIGEQMAEAiLEHARVAPAEVRRRCID 138
Cdd:TIGR03269 75 psKVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTFA-LYGDDTVLDNVLEA-LEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 139 SLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHD 218
Cdd:TIGR03269 152 LIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|.
gi 1208293942 219 LGVVAELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
26-219 |
1.74e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilgLVDRPGEITRGEVIFKGrdllalpPEAQRrlrgsalAMIF 100
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTtllnlIAGF----VPYQHGSITLDGKPVEG-------PGAER-------GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 101 QDplTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCIDSLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:PRK11248 77 QN--EGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDL 219
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-237 |
2.72e-18 |
|
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: 80.72 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL-RP---TSGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRGSALamifQDplttlnpVLTIGEQMAEAILeharvapaevrrrcidslrrvgitspetrlsqyphefSGGMRQRVA 168
Cdd:cd03246 75 GDHVGYLP----QD-------DELFSGSIAENIL-------------------------------------SGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAeLADRIAVMYAGDI 237
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-248 |
9.88e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.78 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 32 SLTLHAGEVLGLVGESGSGKS-----VAGFSilglvdrpgEITRGEVIFKGRDLLALPPeAQRrlrgsALAMIFQDplTT 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKStllnlIAGFL---------TPASGSLTLNGQDHTTTPP-SRR-----PVSMLFQE--NN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNPVLTIGEQMAEAILEHARVAPAEvRRRCIDSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPT 186
Cdd:PRK10771 82 LFSHLTVAQNIGLGLNPGLKLNAAQ-REKLHAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 187 TALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-246 |
1.07e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDPLT 105
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLnpvltigeqMAEAILEHAR-------VAPAEVRRRCIDSLRRVGITspETRLSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:PRK13649 97 QL---------FEETVLKDVAfgpqnfgVSQEEAEALAREKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDV 246
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-246 |
1.09e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPPE 86
Cdd:PRK09700 4 PYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTL-MKVLSGIHEP---TKGTITINNINYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLrgsALAMIFQ-----DPLTTLNPvLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGI-TSPETRLSqyphEFS 160
Cdd:PRK09700 76 LAAQL---GIGIIYQelsviDELTVLEN-LYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLkVDLDEKVA----NLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
|
....*.
gi 1208293942 241 GATDDV 246
Cdd:PRK09700 227 GMVSDV 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-219 |
3.46e-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: 82.02 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 5 RAPVLEVRNLQTVFHDLRGAWP----ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeitrGEVIFKGRDL 80
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYPgappVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LALPPEAQRRlRGSALAmifQDP---LTTLNPVLTIGEqmaeailehARVAPAEVRrrciDSLRRVGITSP--------E 149
Cdd:TIGR02868 400 SSLDQDEVRR-RVSVCA---QDAhlfDTTVRENLRLAR---------PDATDEELW----AALERVGLADWlralpdglD 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 150 TRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMqaLQRETGTAMIWITHDL 219
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-247 |
3.63e-17 |
|
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: 82.01 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlVDRPgeiTRGEVIFKGRDLlalpPEAQRRLRGSALAMIFQD 102
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVG-IWPP---TSGSVRLDGADL----KQWDRETFGKHIGYLPQD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plTTLNPVlTIGEQMA--------EAILEHARVAPA-EVRRRCIDSLrrvgitspETRLSQYPHEFSGGMRQRVAIAIAL 173
Cdd:TIGR01842 401 --VELFPG-TVAENIArfgenadpEKIIEAAKLAGVhELILRLPDGY--------DTVIGPGGATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 174 LNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIwITHDLGVVaELADRIAVMYAGDIVEIGATDDVL 247
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLL-GCVDKILVLQDGRIARFGERDEVL 541
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-247 |
4.19e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 31 LSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITrgeviFKGRDLLALPPEAQRRLRGSaLAMifQDPLTTLNPV 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQ-----FAGQPLEAWSAAELARHRAY-LSQ--QQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 111 LtigeQMAeAILEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEFSGGMRQRVAIAIALL-----NSPD--LIIAD 183
Cdd:PRK03695 87 F----QYL-TLHQPDKTRTEAVASALNEVAEALGLDD---KLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 184 EPTTALDVTIQG---QIIAEMQALqretGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK03695 159 EPMNSLDVAQQAaldRLLSELCQQ----GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-247 |
4.84e-17 |
|
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: 78.97 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLqTVFhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVdrPGEI--TRGEV--IFkGRDLLA 82
Cdd:COG1119 2 PLLELRNV-TVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI--TGDLppTYGNDvrLF-GERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 LPPEAQRRLRG---SALAMIFQDPLTTLNPVLTiGeqmAEAILEHARVAPAEVRRRCIDSLRRVGITSpetRLSQYPHEF 159
Cdd:COG1119 71 EDVWELRKRIGlvsPALQLRFPRDETVLDVVLS-G---FFDSIGLYREPTDEQRERARELLELLGLAH---LADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
....*...
gi 1208293942 240 IGATDDVL 247
Cdd:COG1119 224 AGPKEEVL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-241 |
5.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHD-LRGAWPALNGLSLTLHAGEVLGLVGESGSGKS--VAGFSILgLVDRPGEITRGEVIFKGRDLLALP 84
Cdd:PRK13631 21 ILRVKNLYCVFDEkQENELVALNNISYTFEKNKIYFIIGNSGSGKStlVTHFNGL-IKSKYGTIQVGDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQ--------RRLRgSALAMIFQDPLTTLNPVLTIGEQMAEAIleHARVAPAEVRRRCIDSLRRVGITSPetRLSQYP 156
Cdd:PRK13631 100 ITNPyskkiknfKELR-RRVSMVFQFPEYQLFKDTIEKDIMFGPV--ALGVKKSEAKKLAKFYLNKMGLDDS--YLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVtiQGQiiAEMQAL---QRETGTAMIWITHDLGVVAELADRIAVMY 233
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP--KGE--HEMMQLildAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
....*...
gi 1208293942 234 AGDIVEIG 241
Cdd:PRK13631 251 KGKILKTG 258
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-254 |
5.74e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.92 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlvdRPG-EITRGEVIFKGRDLLALPP 85
Cdd:CHL00131 6 PILEIKNLHASVNEN----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAyKILEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EaQRRLRGSALAmiFQDPLTTlnPVLTiGEQMAEAILEHARVA-------PAEVRRRCIDSLRRVGITspETRLSQYPHE 158
Cdd:CHL00131 79 E-ERAHLGIFLA--FQYPIEI--PGVS-NADFLRLAYNSKRKFqglpeldPLEFLEIINEKLKLVGMD--PSFLSRNVNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 -FSGGMRQRVAI-AIALLNsPDLIIADEPTTALDVTIQgQIIAEMQALQRETGTAMIWITHdlgvVAELADRIA-----V 231
Cdd:CHL00131 151 gFSGGEKKRNEIlQMALLD-SELAILDETDSGLDIDAL-KIIAEGINKLMTSENSIILITH----YQRLLDYIKpdyvhV 224
|
250 260
....*....|....*....|...
gi 1208293942 232 MYAGDIVEIGATDDVLDRPRHPY 254
Cdd:CHL00131 225 MQNGKIIKTGDAELAKELEKKGY 247
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-241 |
5.80e-17 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 79.06 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgEITRGEVIFKGRDLLALPPEA 87
Cdd:PRK09580 1 MLSIKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QrrlRGSALAMIFQDPL------------TTLNPVLTIGEQ-------MAEAILEHARV--APAEVRRRCIDslrrVGit 146
Cdd:PRK09580 75 R---AGEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQepldrfdFQDLMEEKIALlkMPEDLLTRSVN----VG-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 147 spetrlsqypheFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQgQIIAEMQALQRETGTAMIWITHDLGVVAELA 226
Cdd:PRK09580 146 ------------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDAL-KIVADGVNSLRDGKRSFIIVTHYQRILDYIK 212
|
250
....*....|....*.
gi 1208293942 227 -DRIAVMYAGDIVEIG 241
Cdd:PRK09580 213 pDYVHVLYQGRIVKSG 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-239 |
7.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLA-LPPEAQRRLRgSALAMIFQDPLTT 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL-KP---SSGTITIAGYHITPeTGNKNLKKLR-KKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LnpvltigeqMAEAILEHARVAPA-------EVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:PRK13641 98 L---------FENTVLKDVEFGPKnfgfsedEAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-251 |
1.11e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.11 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLLALPP 85
Cdd:PRK11300 3 QPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTV-FNCLTGFYKP---TGGTILLRGQHIEGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLrgsALAMIFQD-----PLTTLNPVLTIGEQMAEAILEHA-------RVAPAEVRRRCIDSLRRVGITSPETRLS 153
Cdd:PRK11300 75 HQIARM---GVVRTFQHvrlfrEMTVIENLLVAQHQQLKTGLFSGllktpafRRAESEALDRAATWLERVGLLEHANRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 154 QyphEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDV--TIQ-GQIIAEmqaLQRETGTAMIWITHDLGVVAELADRIA 230
Cdd:PRK11300 152 G---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPkeTKElDELIAE---LRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
250 260
....*....|....*....|.
gi 1208293942 231 VMYAGDIVEIGATDDVLDRPR 251
Cdd:PRK11300 226 VVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-247 |
1.20e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQtvFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPp 85
Cdd:PRK11160 336 QVSLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYS- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRlrgSALAMIFQDP---LTTLNPVLTIGeqmaeaileharvAPAEVRRRCIDSLRRVGI---TSPETRLSQYPHE- 158
Cdd:PRK11160 409 EAALR---QAISVVSQRVhlfSATLRDNLLLA-------------APNASDEALIEVLQQVGLeklLEDDKGLNAWLGEg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 ---FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMqaLQRETGTAMIWITHDLGVVAELaDRIAVMYAG 235
Cdd:PRK11160 473 grqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQF-DRICVMDNG 549
|
250
....*....|..
gi 1208293942 236 DIVEIGATDDVL 247
Cdd:PRK11160 550 QIIEQGTHQELL 561
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-241 |
1.33e-16 |
|
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: 77.57 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsilglVDRPgeiTRGEVIFKGRDLLALppeaqrrlrgsALAMIFQ 101
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKStllrlLAG------IYPP---DSGTVTVRGRVSSLL-----------GLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 DPLTTLNPVLTIGeqmaeAILEHARVAPAEVRRRCIDsLRRVG--ITSPetrLSQYphefSGGMRQRVAIAIALLNSPDL 179
Cdd:cd03220 97 PELTGRENIYLNG-----RLLGLSRKEIDEKIDEIIE-FSELGdfIDLP---VKTY----SSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIG 241
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
26-250 |
1.59e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPE--AQRrlrgsaLAMIFQDP 103
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKS----TLLSMISRLLPPDSGEVLVDGLDVATTPSRelAKR------LAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 104 ltTLNPVLTIGEQMAEAILEHARVAPAEVRRRCID-SLRRVGITSPETRlsqYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:COG4604 85 --HINSRLTVRELVAFGRFPYSKGRLTAEDREIIDeAIAYLDLEDLADR---YLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 183 DEPTTALDVTIQGQIiaeMQALQR---ETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:COG4604 160 DEPLNNLDMKHSVQM---MKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-248 |
1.68e-16 |
|
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: 77.20 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 33 LTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRdllalPPEAQRRLRG---SALAMIFQDPLTTLNP 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPP----AKGTVKVAGA-----SPGKGWRHIGyvpQRHEFAWDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 110 VLT-----IGEQMAEAILEHARVApaevrrrciDSLRRVGITspetRLSQYP-HEFSGGMRQRVAIAIALLNSPDLIIAD 183
Cdd:TIGR03771 72 VMSgrtghIGWLRRPCVADFAAVR---------DALRRVGLT----ELADRPvGELSGGQRQRVLVARALATRPSVLLLD 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 184 EPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIaVMYAGDIVEIGATDDVLD 248
Cdd:TIGR03771 139 EPFTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQD 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-241 |
1.91e-16 |
|
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: 76.68 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQRRlrgsALAMIFQDPL- 104
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGIDISTIPLEDLRS----SLTIIPQDPTl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 ------TTLNPvltIGEQMAEAILEharvapaevrrrcidSLRrvgITSPETRLSQyphefsgGMRQRVAIAIALLNSPD 178
Cdd:cd03369 94 fsgtirSNLDP---FDEYSDEEIYG---------------ALR---VSEGGLNLSQ-------GQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 179 LIIADEPTTALDVtiqgQIIAEMQALQRE--TGTAMIWITHDLGVVAELaDRIAVMYAGDIVEIG 241
Cdd:cd03369 146 VLVLDEATASIDY----ATDALIQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-247 |
2.10e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFhDLRGAW--PALNGLSLTLHAGEVLGLVGESGSGKS--VAGFSILgLVDRPGEItrgEVIFKGRDLLALP 84
Cdd:PRK13651 3 IKVKNIVKIF-NKKLPTelKALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPDTGTI---EWIFKDEKNKKKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLrgsaLAMIFQdpLTTLNPVLTIGE---------QMAEAILEHAR-------------VAPAEVRRRCIDSLRR 142
Cdd:PRK13651 78 KEKEKVL----EKLVIQ--KTRFKKIKKIKEirrrvgvvfQFAEYQLFEQTiekdiifgpvsmgVSKEEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 143 VGItsPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVtiQGQI-IAEMQALQRETGTAMIWITHDLGV 221
Cdd:PRK13651 152 VGL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP--QGVKeILEIFDNLNKQGKTIILVTHDLDN 227
|
250 260
....*....|....*....|....*.
gi 1208293942 222 VAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK13651 228 VLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-241 |
3.44e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDlrGAwPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:PRK11174 350 IEAEDLEILSPD--GK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL--P---YQGSLKINGIELRELDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgsALAMIFQDPL----TTLNPVLTIGEQMAEAILEHArvapaevrrrcidsLRRVGITSPETRLSQ-YPHE----- 158
Cdd:PRK11174 422 RK----HLSWVGQNPQlphgTLRDNVLLGNPDASDEQLQQA--------------LENAWVSEFLPLLPQgLDTPigdqa 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 --FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIiaeMQALQRET-GTAMIWITHDLgvvAELA--DRIAVMY 233
Cdd:PRK11174 484 agLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV---MQALNAASrRQTTLMVTHQL---EDLAqwDQIWVMQ 557
|
....*...
gi 1208293942 234 AGDIVEIG 241
Cdd:PRK11174 558 DGQIVQQG 565
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-247 |
3.71e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDPLTTL 107
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKS----TLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMAEAILEHARvapAEVRRRCIDSLRRVGITSPETRLSQyphEFSGGMRQRVAIAIALLNSPDLIIADEPTT 187
Cdd:PRK10575 103 RELVAIGRYPWHGALGRFG---AADREKVEEAISLVGLKPLAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 188 ALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-256 |
5.02e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDR-----PGEITRGEVIFKGRDLLA 82
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKS----TILRCFNRlndliPGFRVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 83 L---PPEAQRRLrgsalAMIFQDPlttlNPvltIGEQMAEAILEHARVAPA-----EVRRRcidSLRRVGI-TSPETRLS 153
Cdd:PRK14243 82 PdvdPVEVRRRI-----GMVFQKP----NP---FPKSIYDNIAYGARINGYkgdmdELVER---SLRQAALwDEVKDKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 154 QYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDvTIQGQIIAEMQALQRETGTAMIwITHDLGVVAELADRIAVMY 233
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-PISTLRIEELMHELKEQYTIII-VTHNMQQAARVSDMTAFFN 224
|
250 260 270
....*....|....*....|....*....|..
gi 1208293942 234 A---------GDIVEIGATDDVLDRPRHPYTR 256
Cdd:PRK14243 225 VeltegggryGYLVEFDRTEKIFNSPQQQATR 256
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-217 |
5.20e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 2 TRDRAPVLEVRNLqTVFHDlRGAwPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsiL-----GLVDRPgeitrg 71
Cdd:COG4178 356 ETSEDGALALEDL-TLRTP-DGR-PLLEDLSLSLKPGERLLITGPSGSGKStllraIAG---LwpygsGRIARP------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 72 evifKGRDLLALPpeaQR-RLrgsalamifqdPLTTLNPVLT---IGEQMAEAILEHArvapaevrrrcidsLRRVGITS 147
Cdd:COG4178 424 ----AGARVLFLP---QRpYL-----------PLGTLREALLypaTAEAFSDAELREA--------------LEAVGLGH 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 148 PETRLSQ---YPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIiaeMQALQRET-GTAMIWITH 217
Cdd:COG4178 472 LAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-248 |
5.92e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPGEITRGEVIFKGRdllalPPEAQRRLRGSALAMifQDPLttL 107
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTL-MNALAFRSPKGVKGSGSVLLNGM-----PIDAKEMRAISAYVQ--QDDL--F 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQ-MAEAILEHARVAPAEVRRRCIDS-LRRVGITSPETRLSQYPHE---FSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:TIGR00955 111 IPTLTVREHlMFQAHLRMPRRVTKKEKRERVDEvLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-247 |
6.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVifKGRDLLALPPEAQRRLRG--SALAMIFQDPL 104
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL----QPTEGKV--TVGDIVVSSTSKQKEIKPvrKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 TTLnpvltigeqMAEAILEHARVAPA-------EVRRRCIDSLRRVGITspETRLSQYPHEFSGGMRQRVAIAIALLNSP 177
Cdd:PRK13643 95 SQL---------FEETVLKDVAFGPQnfgipkeKAEKIAAEKLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 178 DLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-248 |
7.69e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 7.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrPGEitrGEVIFKGRDLLALPPEAQRRLRgsalAMIFQ-DPLTT 106
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL--PGQ---GEILLNGRPLSDWSAAELARHR----AYLSQqQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNPV---LTIGeQMAEAILEHARVAPAEVrrrcidsLRRVGITSPETR-LSQypheFSGGMRQRVAIAIALL-----NSP 177
Cdd:COG4138 83 AMPVfqyLALH-QPAGASSEAVEQLLAQL-------AEALGLEDKLSRpLTQ----LSGGEWQRVRLAAVLLqvwptINP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 178 D--LIIADEPTTALDVTIQG---QIIAEMQALqretGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:COG4138 151 EgqLLLLDEPMNSLDVAQQAaldRLLRELCQQ----GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-248 |
1.20e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVD-RPGEITrgevifkgrdLLALPPEAQRRLRGSALAMIFQ 101
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKIT----------VLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 dpLTTLNPVLTIGEQMaeaiLEHARVAPAEVRR--RCIDSLrrVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:PRK13536 122 --FDNLDLEFTVRENL----LVFGRYFGMSTREieAVIPSL--LEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-237 |
2.03e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLqTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrPGEITrGEVIFKGRDL-LALPPE 86
Cdd:PRK13549 259 ILEVRNL-TAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY--PGRWE-GEIFIDGKPVkIRNPQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRlrgsALAMIFQD-PLTTLNPVLTIGEQMAEAILE----HARV-APAEVR--RRCIDSLRrVGITSPETRLSQyphe 158
Cdd:PRK13549 335 AIAQ----GIAMVPEDrKRDGIVPVMGVGKNITLAALDrftgGSRIdDAAELKtiLESIQRLK-VKTASPELAIAR---- 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 159 FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-242 |
2.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGL-VDRPGEITRGEvifkgrdlLALPPEAQR-----RLRgSALAMIF 100
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGD--------YAIPANLKKikevkRLR-KEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 101 QDPLTTLNPVlTIGEQMAEAILeHARVAPAEVRRRCIDSLRRVGItsPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLI 180
Cdd:PRK13645 97 QFPEYQLFQE-TIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 181 IADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-236 |
2.63e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 22 RGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFSIL--GLVDRPGEITRG---------------EVIFKGRD 79
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKStllkiLAGELEPdsGEVSIPKGLRIGylpqeppldddltvlDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 80 LLAlppEAQRRLRgsALAMIFQDPLTTLNPVLTIGEQMAEAileHARVAPAEVRRrcidSLRRVGItsPETRLSQYPHEF 159
Cdd:COG0488 88 ELR---ALEAELE--ELEAKLAEPDEDLERLAELQEEFEAL---GGWEAEARAEE----ILSGLGF--PEEDLDRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDvtiqgqiiAEMQA-----LQRETGTaMIWITHD---L----GVVAELAD 227
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LESIEwleefLKNYPGT-VLVVSHDryfLdrvaTRILELDR 224
|
....*....
gi 1208293942 228 RIAVMYAGD 236
Cdd:COG0488 225 GKLTLYPGN 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-239 |
2.86e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRP--GEITRG--EVIFKG-RDL 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK----ALDDISFDCRAGQVHALMGENGAGKSTL-LKILSGNYQPdaGSILIDgqEMRFAStTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 LAlppeaqrrlrgSALAMIFQDplTTLNPVLTIGEQMAEAILEHAR--VAPAEVRRRCIDSLRRVGI-TSPETRLSqyph 157
Cdd:PRK11288 77 LA-----------AGVAIIYQE--LHLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGVdIDPDTPLK---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTAL---DVTIQGQIIAEMqalqRETGTAMIWITHDLGVVAELADRIAVMYA 234
Cdd:PRK11288 140 YLSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIREL----RAEGRVILYVSHRMEEIFALCDAITVFKD 215
|
....*
gi 1208293942 235 GDIVE 239
Cdd:PRK11288 216 GRYVA 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-249 |
4.66e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFH------DLRGAW-----------PALNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsILglvdRP 65
Cdd:COG4586 1 IIEVENLSKTYRvyekepGLKGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSttikmLTG--IL----VP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 66 geiTRGEVIFKGRDllalPPEAQRRLRGSaLAMIF-QDplTTLNPVLTIGE--QMAEAILehaRVAPAEVRRRcIDSLrr 142
Cdd:COG4586 75 ---TSGEVRVLGYV----PFKRRKEFARR-IGVVFgQR--SQLWWDLPAIDsfRLLKAIY---RIPDAEYKKR-LDEL-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 143 VGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVV 222
Cdd:COG4586 139 VELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI 218
|
250 260
....*....|....*....|....*..
gi 1208293942 223 AELADRIAVMYAGDIVEIGATDDVLDR 249
Cdd:COG4586 219 EALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-244 |
8.76e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 22 RGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVifkgrDLLALPpeAQRRLRGSALAMIFQ 101
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKI-----SILGQP--TRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 DPLTTLN-PVLTIGEQMAEAI--LEHARVAPAEVRRRCIDSLRRVGITspETRLSQYpHEFSGGMRQRVAIAIALLNSPD 178
Cdd:PRK15056 86 SEEVDWSfPVLVEDVVMMGRYghMGWLRRAKKRDRQIVTAALARVDMV--EFRHRQI-GELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADrIAVMYAGDIVEIGATD 244
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-241 |
9.22e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQ 88
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY----PLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRlrgsALAMIFQDPLTTLNPVL---TIGEQMAEAILEHA--RVAPAEVRRRCIDSLrrvgitspETRLSQYPHEFSGGM 163
Cdd:PRK10790 414 RQ----GVAMVQQDPVVLADTFLanvTLGRDISEEQVWQAleTVQLAELARSLPDGL--------YTPLGEQGNNLSVGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 164 RQRVAIAIALLNSPDLIIADEPTTALDVTIQgQIIAEMQALQRETgTAMIWITHDLGVVAElADRIAVMYAGDIVEIG 241
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTE-QAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-245 |
1.09e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeitrGEVIFKGRDLLALPPE 86
Cdd:PRK15439 10 PLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS----GTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLrgsALAMIFQDPLttLNPVLTIGEQMAEAILEHArvapaevrrrciDSLRRVGITSPETRLSQYPHEFSGGM--- 163
Cdd:PRK15439 82 KAHQL---GIYLVPQEPL--LFPNLSVKENILFGLPKRQ------------ASMQKMKQLLAALGCQLDLDSSAGSLeva 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 164 -RQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:PRK15439 145 dRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
...
gi 1208293942 243 TDD 245
Cdd:PRK15439 224 TAD 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-251 |
1.11e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.11 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRDLLALPP 85
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLrgsaLAMIFQDplTTLNPVLTIGEQMAEAILEH-ARVAPA-EVRRRCIDS-LRRVGITSPETRLSQyphEFSGG 162
Cdd:PRK09536 73 RAASRR----VASVPQD--TSLSFEFDVRQVVEMGRTPHrSRFDTWtETDRAAVERaMERTGVAQFADRPVT---SLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGA 242
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
....*....
gi 1208293942 243 TDDVLDRPR 251
Cdd:PRK09536 223 PADVLTADT 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-243 |
1.89e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpGEITRGEVIfkgrDLLALPPEA 87
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT--GDKSAGSHI----ELLGRTVQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRG------SALAMIFQ-----DPLTTLNPVLtIGEQMAEAILEHA-RVAPAEVRRRCIDSLRRVGitspetrLSQY 155
Cdd:PRK09984 74 EGRLARdirksrANTGYIFQqfnlvNRLSVLENVL-IGALGSTPFWRTCfSWFTREQKQRALQALTRVG-------MVHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 156 PHE----FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAV 231
Cdd:PRK09984 146 AHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVA 225
|
250
....*....|..
gi 1208293942 232 MYAGDIVEIGAT 243
Cdd:PRK09984 226 LRQGHVFYDGSS 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-265 |
2.15e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRlrgsALAMIFQdplt 105
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKS----SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR----VLSIIPQ---- 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlNPVLTIGEQM--AEAILEH--ARVAPAEVRRRCIDSLRRvgitSP---ETRLSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:PLN03232 1318 --SPVLFSGTVRfnIDPFSEHndADLWEALERAHIKDVIDR----NPfglDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 179 LIIADEPTTALDVTIQGQIiaemQALQRE--TGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLDRPRHPYTR 256
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLI----QRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
....*....
gi 1208293942 257 GLLNSVPGD 265
Cdd:PLN03232 1467 MVHSTGPAN 1475
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-250 |
2.23e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 22 RGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRgSALAMIFQ 101
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 DplTTLNPVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLsqyPHEFSGGMRQRVAIAIALLNSPDLII 181
Cdd:PRK11831 92 S--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 182 ADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-238 |
2.79e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 70.27 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLqTVFHD---LRGAWPALNGLSLTLHAGEVLGLVGESGSGKS-----VAGFsilglvdRPGEITRGEVIFKGRD 79
Cdd:cd03213 3 TLSFRNL-TVTVKsspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKStllnaLAGR-------RTGLGVSGEVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 80 LlalPPEAQRRLrgsaLAMIFQDplTTLNPVLTIGEQMAEAileharvapAEVRrrcidslrrvGItspetrlsqyphef 159
Cdd:cd03213 75 L---DKRSFRKI----IGYVPQD--DILHPTLTVRETLMFA---------AKLR----------GL-------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIiaeMQALQR--ETGTAMIWITHDL-GVVAELADRIAVMYAGD 236
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV---MSLLRRlaDTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
..
gi 1208293942 237 IV 238
Cdd:cd03213 190 VI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-237 |
3.00e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQ-TVFHDLrgawpalnglSLTLHAGEVLGLVGESGSGKSVAGFSILGLvdRPgeITRGEVIFKGRDLLALP 84
Cdd:PRK15439 266 APVLTVEDLTgEGFRNI----------SLEVRAGEILGLAGVVGAGRTELAETLYGL--RP--ARGGRIMLNGKEINALS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PeAQRRLRG--------SALAMIFQDPL-------TTLNPVLTIGEQMAEAILEHARvapaevrrrcidslRRVGITSpe 149
Cdd:PRK15439 332 T-AQRLARGlvylpedrQSSGLYLDAPLawnvcalTHNRRGFWIKPARENAVLERYR--------------RALNIKF-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 150 TRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRI 229
Cdd:PRK15439 395 NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRV 473
|
....*...
gi 1208293942 230 AVMYAGDI 237
Cdd:PRK15439 474 LVMHQGEI 481
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-256 |
3.13e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLqTVFHDLRgawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEI-TRGEVIFKGRDLLALPP 85
Cdd:PRK14258 6 PAIKVNNL-SFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EAQRRLRgsALAMIFQDPltTLNPvLTIGEQMA---EAILEHARVApaevrrrcIDSLRRVGITSPE------TRLSQYP 156
Cdd:PRK14258 82 NLNRLRR--QVSMVHPKP--NLFP-MSVYDNVAygvKIVGWRPKLE--------IDDIVESALKDADlwdeikHKIHKSA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYA-- 234
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGne 228
|
250 260
....*....|....*....|....*
gi 1208293942 235 ---GDIVEIGATDDVLDRPRHPYTR 256
Cdd:PRK14258 229 nriGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-222 |
1.03e-13 |
|
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: 68.92 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVfhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL-RP---DSGEVRWNGTPLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RrlrgsalAMIFQDPLTTLNPVLTIGE--QMAEAILEHARvapaevrRRCIDSLRRVGITSPETRLSqypHEFSGGMRQR 166
Cdd:TIGR01189 73 E-------NILYLGHLPGLKPELSALEnlHFWAAIHGGAQ-------RTIEDALAAVGLTGFEDLPA---AQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 167 VAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQA-LQRetGTAMIWITH-DLGVV 222
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-250 |
1.12e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRrlrgSALAMIFQDPLT 105
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR----SRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPV---LTIGEQMA--EAILEHARVApaevrrrCI--DSLRRvgitsP---ETRLSQYPHEFSGGMRQRVAIAIALLN 175
Cdd:PRK10789 401 FSDTVannIALGRPDAtqQEIEHVARLA-------SVhdDILRL-----PqgyDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 176 SPDLIIADEPTTALDVTIQGQIIAEMQalQRETGTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-252 |
1.35e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.71 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIfKGRDLLAlppEAQRRLRgsalaMIFQDplTTL 107
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETP---SAGELL-AGTAPLA---EAREDTR-----LMFQD--ARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMAEAILEHARVAPAEvrrrcidSLRRVGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTT 187
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQWRDAALQ-------ALAAVGL---ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 188 ALDVTIQgqiiAEMQ----ALQRETGTAMIWITHDLGVVAELADRIAVMYAGdivEIGATDDV-LDRPRH 252
Cdd:PRK11247 163 ALDALTR----IEMQdlieSLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTVdLPRPRR 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-237 |
1.38e-13 |
|
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: 71.01 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLqTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrPGEItRGEVIFKGRDLLALPPEA 87
Cdd:TIGR02633 257 ILEARNL-TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY--PGKF-EGNVFINGKPVDIRNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRlrgSALAMIFQD-PLTTLNPVLTIGEQMAEAILEH---ARVAPAEVRRRCIDS-LRRVGITS-----PETRLSqyph 157
Cdd:TIGR02633 333 AIR---AGIAMVPEDrKRHGIVPILGVGKNITLSVLKSfcfKMRIDAAAELQIIGSaIQRLKVKTaspflPIGRLS---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 efsGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDI 237
Cdd:TIGR02633 406 ---GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-239 |
5.17e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPGEITrGEVIFKGRdllalppEA 87
Cdd:NF040905 1 ILEMRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVYPHGSYE-GEILFDGE-------VC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 Q-RRLRGS---ALAMIFQDplTTLNPVLTIgeqmAEAIL---EHAR---VAPAEVRRRCIDSLRRVGIT-SPETRLSQYp 156
Cdd:NF040905 68 RfKDIRDSealGIVIIHQE--LALIPYLSI----AENIFlgnERAKrgvIDWNETNRRARELLAKVGLDeSPDTLVTDI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 157 hefsG-GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:NF040905 141 ----GvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
....
gi 1208293942 236 DIVE 239
Cdd:NF040905 216 RTIE 219
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-247 |
6.52e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.53 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILG-LVDRPGEITR-GEVifkgrDLLALPPEAQRRLRG------SALAM 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGsLSPTVGKVDRnGEV-----SVIAISAGLSGQLTGieniefKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 99 IF-QDPLTTLNPVLTIGEQMAEAILEHARvapaevrrrcidslrrvgitspetrlsqyphEFSGGMRQRVAIAIALLNSP 177
Cdd:PRK13546 114 GFkRKEIKAMTPKIIEFSELGEFIYQPVK-------------------------------KYSSGMRAKLGFSINITVNP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 178 DLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK13546 163 DILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-252 |
7.34e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKS-----VAGfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRRLRgSALAMIFQD 102
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKStllkaLAG-DLTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLR-AVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 PLTtlnpvLTIGEQMAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQRVAIAIAL--------- 173
Cdd:PRK13547 95 AFA-----FSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 174 LNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLdRPRH 252
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAH 247
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-235 |
8.46e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLRgawpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDR-PGEIT-RG-EVIFKGrdllal 83
Cdd:PRK10762 3 ALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdAGSILyLGkEVTFNG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEAQRrlrgSALAMIFQDplttLN--PVLTIGEQM---AEAILEHARVAPAEVRRRCIDSLRRVGIT-SPETRLSqyph 157
Cdd:PRK10762 73 PKSSQE----AGIGIIHQE----LNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRfSSDKLVG---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTiqgqiiaEMQAL------QRETGTAMIWITHDLGVVAELADRIAV 231
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT-------ETESLfrvireLKSQGRGIVYISHRLKEIFEICDDVTV 213
|
....
gi 1208293942 232 MYAG 235
Cdd:PRK10762 214 FRDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-229 |
8.72e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVifkgrdllalppEAQRRLR-GSALAMIFQDPltT 106
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV----APDEGVI------------KRNGKLRiGYVPQKLYLDT--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNpvLTIGEQMaeailehaRVAPAEVRRRCIDSLRRVGitspETRLSQYP-HEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:PRK09544 82 LP--LTVNRFL--------RLRPGTKKEDILPALKRVQ----AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1208293942 186 TTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRI 229
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-247 |
8.93e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALppeAQRRLRgSALAMIFQdplt 105
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKS----SMLNALFRIVELERGRILIDGCDISKF---GLMDLR-KVLGIIPQ---- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 tlNPVLTIGEQM--AEAILEH--ARVAPAEVRRRCIDSLRR--VGItspETRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:PLN03130 1321 --APVLFSGTVRfnLDPFNEHndADLWESLERAHLKDVIRRnsLGL---DAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 180 IIADEPTTALDV----TIQGQIIAEMQAlqretgTAMIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVL 247
Cdd:PLN03130 1396 LVLDEATAAVDVrtdaLIQKTIREEFKS------CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
145-232 |
9.77e-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: 64.78 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 145 ITSPETRLSQYPHeFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIaemQALQRETGTaMIWITHDLGVVAE 224
Cdd:cd03221 58 TWGSTVKIGYFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE---EALKEYPGT-VILVSHDRYFLDQ 132
|
....*...
gi 1208293942 225 LADRIAVM 232
Cdd:cd03221 133 VATKIIEL 140
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-237 |
2.10e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLqtvfhdlrgAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRDLLALPPE-- 86
Cdd:PRK10762 258 LKVDNL---------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPR----TSGYVTLDGHEVVTRSPQdg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 ---------AQRRLRGSALAMifqdplttlnpvlTIGEQMAEAILEH-----ARVAPAEVRRRCIDSLRRVGITSPEtrL 152
Cdd:PRK10762 325 langivyisEDRKRDGLVLGM-------------SVKENMSLTALRYfsragGSLKHADEQQAVSDFIRLFNIKTPS--M 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 153 SQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVM 232
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVM 468
|
....*
gi 1208293942 233 YAGDI 237
Cdd:PRK10762 469 HEGRI 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-235 |
3.39e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPPEAQRrlrgsalAMIFQDPLT 105
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKT----TTFKMLTGDTTVTSGDATVAGKSILTNISDVHQ-------NMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVLTIGEQMAeaILEHARVAPAEVRRRCID-SLRRVGITSPETRLSQyphEFSGGMRQRVAIAIALLNSPDLIIADE 184
Cdd:TIGR01257 2022 AIDDLLTGREHLY--LYARLRGVPAEEIEKVANwSIQSLGLSLYADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 185 PTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-246 |
3.56e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 2 TRDRAPVLEVRNLQTvfHDLRGAwpalNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlVDRpgeITRGEVIFKGRDLL 81
Cdd:PRK09700 259 NLAHETVFEVRNVTS--RDRKKV----RDISFSVCRGEILGFAGLVGSGRTELMNCLFG-VDK---RAGGEIRLNGKDIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 82 ALPP-EAQRRlrgsALAMIFQDPLTT-LNPVLTIGEQMAEA-ILEHARVAPA-----EVRRRCIDSLRRVGITSPETRLS 153
Cdd:PRK09700 329 PRSPlDAVKK----GMAYITESRRDNgFFPNFSIAQNMAISrSLKDGGYKGAmglfhEVDEQRTAENQRELLALKCHSVN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 154 QYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMY 233
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFC 483
|
250
....*....|....
gi 1208293942 234 AGDIVEI-GATDDV 246
Cdd:PRK09700 484 EGRLTQIlTNRDDM 497
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-238 |
4.11e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDL------ 80
Cdd:PRK11614 4 VMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDItdwqta 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 ------LALPPEAQRrlrgsalamIFQDplTTLNPVLTIGEQMAEAILEHARVApaevrrRCIDSLRRVgitspETRLSQ 154
Cdd:PRK11614 76 kimreaVAIVPEGRR---------VFSR--MTVEENLAMGGFFAERDQFQERIK------WVYELFPRL-----HERRIQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 155 YPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYA 234
Cdd:PRK11614 134 RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLEN 212
|
....
gi 1208293942 235 GDIV 238
Cdd:PRK11614 213 GHVV 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-229 |
7.10e-12 |
|
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: 63.67 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVfhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03231 1 LEADELTCE----RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLS-PP---LAGRVLLNGGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RrlrgsalAMIFQDPLTTLNPVLTIGEQMAEAILEHARVApaevrrrCIDSLRRVGITSPETRLSqypHEFSGGMRQRVA 168
Cdd:cd03231 73 R-------GLLYLGHAPGIKTTLSVLENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPV---AQLSAGQQRRVA 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 169 IAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRI 229
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-233 |
8.35e-12 |
|
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: 64.31 E-value: 8.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 38 GEVLGLVGESGSGKS-----VAGFSI--LGLVDRPGEITrgEVIfkgrdllalppeaqRRLRGSALAMIFQDPLT-TLNP 109
Cdd:cd03236 26 GQVLGLVGPNGIGKStalkiLAGKLKpnLGKFDDPPDWD--EIL--------------DEFRGSELQNYFTKLLEgDVKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 110 VltIGEQMAEAIleharvaPAEVRRRCIDSLRR----------VGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:cd03236 90 I--VKPQYVDLI-------PKAVKGKVGELLKKkdergkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 180 IIADEPTTALDVtiqGQIIAEMQALQR--ETGTAMIWITHDLGVVAELADRIAVMY 233
Cdd:cd03236 161 YFFDEPSSYLDI---KQRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-247 |
9.54e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 31 LSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeitrGEVIFKGRDLLALPPEAqRRLRGSAL----AMIFQDpLTT 106
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----GNIIIDDEDISLLPLHA-RARRGIGYlpqeASIFRR-LSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 107 LNPVLtigeqmaeAILEHARVAPAEVRR-RCIDSLRRVGITSPETRLSQyphEFSGGMRQRVAIAIALLNSPDLIIADEP 185
Cdd:PRK10895 96 YDNLM--------AVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 186 TTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-238 |
1.11e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.05 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 12 RNLQTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITrGEVIFKGRDLLalppEAQRRL 91
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVE-GDIHYNGIPYK----EFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 92 RGSAlAMIFQDPLTtlNPVLTIGEQMaeaileharvapaEVRRRCidslrrvgitspetRLSQYPHEFSGGMRQRVAIAI 171
Cdd:cd03233 82 PGEI-IYVSEEDVH--FPTLTVRETL-------------DFALRC--------------KGNEFVRGISGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 172 ALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETG-TAMIWITHDLGVVAELADRIAVMYAGDIV 238
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-265 |
1.11e-11 |
|
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: 65.74 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAgfsILGLVdRPGEITRGEVIFKGRDLLALppeAQRRLRgSALAMIFQDPL--- 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSL---TLGLF-RINESAEGEIIIDGLNIAKI---GLHDLR-FKITIIPQDPVlfs 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 ----TTLNPVLTIGEQMAEAILEHARVA------PAEVRRRCidslrrvgitspetrlSQYPHEFSGGMRQRVAIAIALL 174
Cdd:TIGR00957 1374 gslrMNLDPFSQYSDEEVWWALELAHLKtfvsalPDKLDHEC----------------AEGGENLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 175 NSPDLIIADEPTTALDVTIQGQIIAEMQAlQRETGTAMIwITHDLGVVAELAdRIAVMYAGDIVEIGATDDVLDRprhpy 254
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLT-IAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ----- 1509
|
250
....*....|.
gi 1208293942 255 tRGLLNSVPGD 265
Cdd:TIGR00957 1510 -RGIFYSMAKD 1519
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-249 |
1.31e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhdlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLV-DRPGEITR-GEVIfkgrdllal 83
Cdd:PRK13537 5 VAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDAGSISLcGEPV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 pPEAQRRLRgSALAMIFQdpLTTLNPVLTIGEQMaeaiLEHAR---VAPAEVRRRCIDSLRRVGItspETRLSQYPHEFS 160
Cdd:PRK13537 72 -PSRARHAR-QRVGVVPQ--FDNLDPDFTVRENL----LVFGRyfgLSAAAARALVPPLLEFAKL---ENKADAKVGELS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 161 GGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVAELADRIAVMYAGDIVEI 240
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
....*....
gi 1208293942 241 GATDDVLDR 249
Cdd:PRK13537 220 GAPHALIES 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-250 |
1.72e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeitrGEVIFKGRDLLALPPEAQRRLrgsaLAMIFQDplttl 107
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCG----GEIRVNGREIGAYGLRELRRQ----FSMIPQD----- 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 nPVLTIG--EQMAEAILEharVAPAEVRRRC-IDSLR-RVGITSP--ETRLSQYPHEFSGGMRQRVAIAIALLN-SPDLI 180
Cdd:PTZ00243 1393 -PVLFDGtvRQNVDPFLE---ASSAEVWAALeLVGLReRVASESEgiDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFI 1468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 181 IADEPTTALDVTIQGQIIAE-MQALQRETgtaMIWITHDLGVVAELaDRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATvMSAFSAYT---VITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-249 |
6.33e-11 |
|
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: 63.43 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 22 RGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRdlLALPPEaQRRLRGSALA--MI 99
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK----VEGHVHMKGS--VAYVPQ-QAWIQNDSLRenIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 100 FQDPLttlNPVLTIGEQMAEAILEHARVAPAEVRrrcidslrrvgitspeTRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:TIGR00957 721 FGKAL---NEKYYQQVLEACALLPDLEILPSGDR----------------TEIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 180 IIADEPTTALDVTIQGQI----IAEMQALQRETgtaMIWITHDLGVVAELaDRIAVMYAGDIVEIGATDDVLDR 249
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIfehvIGPEGVLKNKT---RILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-235 |
8.54e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.11 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLrgAWPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRPgeiTRGEVIFKGRDLlalppE 86
Cdd:TIGR01257 927 PGVCVKNLVKIFEPS--GRPAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTGLLPP---TSGTVLVGGKDI-----E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRGSALAMIFQDPLttLNPVLTIgeqmAEAILEHARVAPAEVRRRCIDSLRRVGITSPETRLSQYPHEFSGGMRQR 166
Cdd:TIGR01257 996 TNLDAVRQSLGMCPQHNI--LFHHLTV----AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRK 1069
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 167 VAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMqaLQRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-231 |
9.50e-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: 61.27 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAG-----EVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQd 102
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVL----KPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSS- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 plttlnpvltigeqmaeaileharvapaEVRRRCIDSLRRVGITSP---ETRLSQYPHEFSGGMRQRVAIAIALLNSPDL 179
Cdd:cd03237 85 ----------------------------ITKDFYTHPYFKTEIAKPlqiEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 180 IIADEPTTALDVTiqgQIIAEMQALQR----ETGTAMIwITHDLGVVAELADRIAV 231
Cdd:cd03237 137 YLLDEPSAYLDVE---QRLMASKVIRRfaenNEKTAFV-VEHDIIMIDYLADRLIV 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-273 |
1.36e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 21 LRGAW------PALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKgRDLLA--LPPEAQRRLR 92
Cdd:PRK11147 6 IHGAWlsfsdaPLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNGEVLLDDGRIIYE-QDLIVarLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 93 GS---------------------ALAMIFQDPL-TTLNpvltigeQMAE--AILEHARVAPAEvrRRCIDSLRRVGItSP 148
Cdd:PRK11147 81 GTvydfvaegieeqaeylkryhdISHLVETDPSeKNLN-------ELAKlqEQLDHHNLWQLE--NRINEVLAQLGL-DP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 149 ETRLSqyphEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTiqgqIIAEMQALQRETGTAMIWITHDLGVVAELADR 228
Cdd:PRK11147 151 DAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1208293942 229 iavmyagdIVEigatddvLDrprhpytRGLLNSVPGD-----TARGERLR 273
Cdd:PRK11147 223 --------IVD-------LD-------RGKLVSYPGNydqylLEKEEALR 250
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-247 |
1.69e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 23 GAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLALPP-EAQRRLrgsalAMIFQ 101
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRI-----GLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 102 DPLTTLNpvLTIGEQMAEAILEHArvaPAEVRRRCID------SLRRVGITSPETrlsQYPHEFSGGMRQRVAIAIALLN 175
Cdd:PRK10253 89 NATTPGD--ITVQELVARGRYPHQ---PLFTRWRKEDeeavtkAMQATGITHLAD---QSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 176 SPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-190 |
1.98e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLlalppeAQRRLRGSALAMIFQDP--L 104
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKS----SLLSLIAGARKIQQGRVEVLGGDM------ADARHRRAVCPRIAYMPqgL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 -TTLNPVLTIgeqmAEAILEHARV---APAEVRRRcIDSLRRvgitspETRLSQYPH----EFSGGMRQRVAIAIALLNS 176
Cdd:NF033858 86 gKNLYPTLSV----FENLDFFGRLfgqDAAERRRR-IDELLR------ATGLAPFADrpagKLSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 1208293942 177 PDLIIADEPTTALD 190
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-235 |
2.50e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpGEITRGEVIFKGRDLlalppeAQRRLRGSALamIFQDPLttL 107
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ--GNNFTGTILANNRKP------TKQILKRTGF--VTQDDI--L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 NPVLTIGEQMAE-AILEHARVAPAEVRRRCIDS-LRRVGITSPETRL--SQYPHEFSGGMRQRVAIAIALLNSPDLIIAD 183
Cdd:PLN03211 152 YPHLTVRETLVFcSLLRLPKSLTKQEKILVAESvISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 184 EPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMYAG 235
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-233 |
4.39e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 29 NGLSL----TLHAGEVLGLVGESGSGKSVAgFSIL--------GLVDRPGEITrgEVIfkgrdllalppeaqRRLRGSAL 96
Cdd:COG1245 86 NGFRLyglpVPKKGKVTGILGPNGIGKSTA-LKILsgelkpnlGDYDEEPSWD--EVL--------------KRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 97 amifQDPLT-----TLNPVLTIgeQMAEAIlehARVAPAEVR--------RRCIDSLR-RVGITSpetRLSQYPHEFSGG 162
Cdd:COG1245 149 ----QDYFKklangEIKVAHKP--QYVDLI---PKVFKGTVRellekvdeRGKLDELAeKLGLEN---ILDRDISELSGG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVtiqGQIIAEMQALQR--ETGTAMIWITHDLGVVAELADRIAVMY 233
Cdd:COG1245 217 ELQRVAIAAALLRDADFYFFDEPSSYLDI---YQRLNVARLIRElaEEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-240 |
8.17e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNlqTVFHDLRGAWpALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:PRK10522 323 LELRN--VTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-QP---QSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLrgsaLAMIFQD--PLT-TLNPVltiGEQMAEAI----LEHARVApaevrrrciDSLRRVGITSPETRLSQyphefsg 161
Cdd:PRK10522 396 RKL----FSAVFTDfhLFDqLLGPE---GKPANPALvekwLERLKMA---------HKLELEDGRISNLKLSK------- 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDlGVVAELADRIAVMYAGDIVEI 240
Cdd:PRK10522 453 GQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-233 |
9.26e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 29 NGLSL----TLHAGEVLGLVGESGSGKS-----VAGFSILGLVDRPGEITRGEVIfkgrdllalppeaqRRLRGSALAMI 99
Cdd:PRK13409 86 NGFKLyglpIPKEGKVTGILGPNGIGKTtavkiLSGELIPNLGDYEEEPSWDEVL--------------KRFRGTELQNY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 100 FQDpLT--TLNPVLTIgeQMAEAIleharvaPAEVRRRCIDSLRRV---GITSP-------ETRLSQYPHEFSGGMRQRV 167
Cdd:PRK13409 152 FKK-LYngEIKVVHKP--QYVDLI-------PKVFKGKVRELLKKVderGKLDEvverlglENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 168 AIAIALLNSPDLIIADEPTTALDVtiqGQIIAEMQALQRET-GTAMIWITHDLGVVAELADRIAVMY 233
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDI---RQRLNVARLIRELAeGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-221 |
1.56e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVfhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPE 86
Cdd:PRK13539 1 MMLEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL----PPAAGTIKLDGGDIDDPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 87 AQRRLRGSALAMifqdplttlNPVLTIGEQMA--EAILEHARVAPAEvrrrcidSLRRVGITSPETRLSQYpheFSGGMR 164
Cdd:PRK13539 73 EACHYLGHRNAM---------KPALTVAENLEfwAAFLGGEELDIAA-------ALEAVGLAPLAHLPFGY---LSAGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 165 QRVAIAiALLNSPDLI-IADEPTTALDVTIQGQIIAEMQAlQRETGTAMIWITH-DLGV 221
Cdd:PRK13539 134 RRVALA-RLLVSNRPIwILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-231 |
1.59e-09 |
|
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: 59.03 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 25 WPAL----NGLSLT-----LHAGEVLGLVGESGSGKSVagF-SILGLVDRPGEitrGEVIFKGRdlLA-----LPPEAQR 89
Cdd:COG1245 344 YPDLtksyGGFSLEveggeIREGEVLGIVGPNGIGKTT--FaKILAGVLKPDE---GEVDEDLK--ISykpqyISPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 90 RLRgsalAMIFQdplttlnpvlTIGEQMAEAILEHarvapaEVrrrcidsLRRVGItspETRLSQYPHEFSGGMRQRVAI 169
Cdd:COG1245 417 TVE----EFLRS----------ANTDDFGSSYYKT------EI-------IKPLGL---EKLLDKNVKDLSGGELQRVAI 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 170 AIALLNSPDLIIADEPTTALDVTiqgQIIAEMQALQR---ETGTAMIWITHDLGVVAELADRIAV 231
Cdd:COG1245 467 AACLSRDADLYLLDEPSAHLDVE---QRLAVAKAIRRfaeNRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
158-231 |
2.16e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 2.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTiqgQIIAEMQALQR---ETGTAMIWITHDLGVVAELADRIAV 231
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE---QRLAVAKAIRRiaeEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-204 |
2.41e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVfhdlRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSIL----GLVdRPGEitrGEVIFKGRDLLAL 83
Cdd:PRK13538 1 MLEARNLACE----RDERILFSGLSFTLNAGELVQIEGPNGAGKT----SLLrilaGLA-RPDA---GEVLWQGEPIRRQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 84 PPEAQRrlrgsalAMIFQDPLTTLNPVLTIGEQMAEAilehARVAPAEVRRRCIDSLRRVGIT----SPETRLSQyphef 159
Cdd:PRK13538 69 RDEYHQ-------DLLYLGHQPGIKTELTALENLRFY----QRLHGPGDDEALWEALAQVGLAgfedVPVRQLSA----- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1208293942 160 sgGMRQRVAIAIALLNSPDLIIADEPTTALDVtiQGqiIAEMQAL 204
Cdd:PRK13538 133 --GQQRRVALARLWLTRAPLWILDEPFTAIDK--QG--VARLEAL 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-240 |
2.56e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQtvfhDLRGawPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGeitrGEVIFKGRDL------- 80
Cdd:PRK10982 250 ILEVRNLT----SLRQ--PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA----GTITLHGKKInnhnane 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 -----LALPPEaQRRLRG--SALAMIFQDPLTTLNPVLT-IGeqmaeaILEHARVAPAEvrRRCIDSLRrVGITSPETRL 152
Cdd:PRK10982 320 ainhgFALVTE-ERRSTGiyAYLDIGFNSLISNIRNYKNkVG------LLDNSRMKSDT--QWVIDSMR-VKTPGHRTQI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 153 SQypheFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVM 232
Cdd:PRK10982 390 GS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM 464
|
....*...
gi 1208293942 233 YAGDIVEI 240
Cdd:PRK10982 465 SNGLVAGI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-239 |
2.76e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.15 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 7 PVLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSvagfsilglvdrpgeiTrgevIFKgrdLLA--LP 84
Cdd:COG0488 314 KVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKS----------------T----LLK---LLAgeLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLRGSALAMIF--QDpLTTLNPVLTIgeqmaeaiLEH-ARVAPAEVRRRCIDSLRRVGItSPEtRLSQYPHEFSG 161
Cdd:COG0488 367 PDSGTVKLGETVKIGYfdQH-QEELDPDKTV--------LDElRDGAPGGTEQEVRGYLGRFLF-SGD-DAFKPVGVLSG 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDV-TIQgqiiAEMQALQRETGTAMIwITHDLGVVAELADRIAVMYAGDIVE 239
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLE----ALEEALDDFPGTVLL-VSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
131-246 |
5.76e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 131 EVRRRCIDSLRRVGITSPETRLSQyphEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGT 210
Cdd:NF000106 120 DARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90 100 110
....*....|....*....|....*....|....*.
gi 1208293942 211 AMIwITHDLGVVAELADRIAVMYAGDIVEIGATDDV 246
Cdd:NF000106 197 VLL-TTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-227 |
1.05e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 25 WPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVifkgrdllalppeaqrrlrgsalamifqdpl 104
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV------------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 ttlnPVLTIGEQmaEAILEH--ARVAPAEVRRRcidsLRRVGITSPETRLSQYpHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:COG2401 92 ----PDNQFGRE--ASLIDAigRKGDFKDAVEL----LNAVGLSDAVLWLRRF-KELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELAD 227
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQP 205
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-235 |
1.28e-08 |
|
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: 54.64 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEVIFKGRDLLALPPEAQRRLRGSALAMIFQDPL- 104
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 --TTLNPVLTIG----EQMAEAILEHARVAPAevrrrcIDSLRRvgitSPETRLSQYPHEFSGGMRQRVAIAIALLNSPD 178
Cdd:cd03290 91 lnATVEENITFGspfnKQRYKAVTDACSLQPD------IDLLPF----GDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 179 LIIADEPTTALDVTIQGQIIAE--MQALQRETGTaMIWITHDLGVVAElADRIAVMYAG 235
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRT-LVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
155-217 |
1.40e-08 |
|
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: 53.31 E-value: 1.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 155 YP--HEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIiaeMQALQREtGTAMIWITH 217
Cdd:cd03223 86 YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL---YQLLKEL-GITVISVGH 146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-248 |
1.55e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 27 ALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlVDRPGEitrGEVIFKGR-DLLALPPEAQRRLRGsalamIFQDPLT 105
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG-VTMPNK---GTVDIKGSaALIAISSGLNGQLTG-----IENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVLTiGEQMAE---AILEHARVAPAevrrrcidslrrvgitspetrLSQYPHEFSGGMRQRVAIAIALLNSPDLIIA 182
Cdd:PRK13545 110 GLMMGLT-KEKIKEiipEIIEFADIGKF---------------------IYQPVKTYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 183 DEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVLD 248
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-247 |
1.81e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 32 SLTLHAGEVLGLVGESGSGKSVAGFSIlglvdrPGEIT--RGEVIFKGRDLLALPPEAQRRLrgsaLAMIFQDPLTTLnp 109
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL------AGELPllSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNTDM-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 110 vLTIGEQ-----MAEAILEHARvAPAevrrRCIDSLRRVGITSPETRLSQYpheFSGGMRQRVAIAIALLNSPDLIIADE 184
Cdd:PRK10938 91 -LSPGEDdtgrtTAEIIQDEVK-DPA----RCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 185 PTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-255 |
2.28e-08 |
|
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: 54.14 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeITRGEVIFKGRDLLALPPEAQRrlrgSALAMIFQDPLT 105
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTLR----SRLSIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 -------TLNPVLTIGEQMAEAILEharvapaevrrrcIDSLRRVGITSP---ETRLSQYPHEFSGGMRQRVAIAIALLN 175
Cdd:cd03288 107 fsgsirfNLDPECKCTDDRLWEALE-------------IAQLKNMVKSLPgglDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 176 SPDLIIADEPTTALDvtiqgqiIAEMQALQRETGTA-----MIWITHDLGVVAElADRIAVMYAGDIVEIGATDDVLDRP 250
Cdd:cd03288 174 KSSILIMDEATASID-------MATENILQKVVMTAfadrtVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
....*
gi 1208293942 251 RHPYT 255
Cdd:cd03288 246 DGVFA 250
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-232 |
9.47e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQtvFH-DLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDRPGEITRGEVIFKGRDLLAlppEA 87
Cdd:PTZ00265 383 IQFKNVR--FHyDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIINDSHNLK---DI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLRGSALAMIFQDPLTTLNPV----------LTIGEQMAEAILEHARVA------PAEVRRRCIDSLRRVGITSPETR 151
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIknnikyslysLKDLEALSNYYNEDGNDSqenknkRNSCRAKCAGDLNDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 152 LSQYP--------------------HEF-------------------SGGMRQRVAIAIALLNSPDLIIADEPTTALDVT 192
Cdd:PTZ00265 534 LIEMRknyqtikdsevvdvskkvliHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1208293942 193 IQGQIIAEMQALQRETGTAMIWITHDLGVVaELADRIAVM 232
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-218 |
1.39e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRP--GE------ITRG---------------EVIFKGrdlLALP 84
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTL-LRIMAGVDKDfnGEarpqpgIKVGylpqepqldptktvrENVEEG---VAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 85 PEAQRRLrgSALAMIFQDPLTTLNPVLtigEQMAE--AILEHARVAPAEVR-RRCIDSLRRVGITSPETRLSqyphefsG 161
Cdd:TIGR03719 97 KDALDRF--NEISAKYAEPDADFDKLA---AEQAElqEIIDAADAWDLDSQlEIAMDALRCPPWDADVTKLS-------G 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 162 GMRQRVAIAIALLNSPDLIIADEPTTALDvtiqgqiiAEM-----QALQRETGTaMIWITHD 218
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD--------AESvawleRHLQEYPGT-VVAVTHD 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-238 |
1.96e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 4 DRAP-----VLEVRNLqTVFHDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGlvdRP-GEITRGEVIFKG 77
Cdd:NF040905 248 ERTPkigevVFEVKNW-TVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSyGRNISGTVFKDG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 78 RDL-LALPPEAQRrlrgSALAMIFQDPLTT-LNPVLTIGEQMAEAIL----------EHARVAPAEVRRRcidSLRrvgI 145
Cdd:NF040905 324 KEVdVSTVSDAID----AGLAYVTEDRKGYgLNLIDDIKRNITLANLgkvsrrgvidENEEIKVAEEYRK---KMN---I 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 146 TSPEtrLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQREtGTAMIWITHDLGVVAEL 225
Cdd:NF040905 394 KTPS--VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGM 470
|
250
....*....|...
gi 1208293942 226 ADRIAVMYAGDIV 238
Cdd:NF040905 471 CDRIYVMNEGRIT 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-217 |
2.39e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDlrgaWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdRPgeiTRGEVIFKGRDLLALPPEA 87
Cdd:PRK13540 1 MLDVIELDFDYHD----QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL-NP---EKGEILFERQSIKKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 88 QRRLrgsalamIFQDPLTTLNPVLTIGEQMAEAIleHARVAPAEVRRRCidSLRRVGitspetRLSQYP-HEFSGGMRQR 166
Cdd:PRK13540 73 QKQL-------CFVGHRSGINPYLTLRENCLYDI--HFSPGAVGITELC--RLFSLE------HLIDYPcGLLSSGQKRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1208293942 167 VAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQAlQRETGTAMIWITH 217
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
160-233 |
2.99e-07 |
|
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: 49.67 E-value: 2.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 160 SGGMRQRVAIAIAL----LNSPDLIIADEPTTALDvTIQGQIIAEMQALQRETGTAMIWITHDLGvVAELADRIAVMY 233
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLD-PRDGQALAEAILEHLVKGAQVIVITHLPE-LAELADKLIHIK 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-229 |
3.23e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 17 VFHDL---RGAWPALNGLSLTLHAGEVLGLVGESGSGKSvagfSILGLVDrpGEITR--GEVIFKGRDLLALPPEAQRRL 91
Cdd:PRK10636 3 VFSSLqirRGVRVLLDNATATINPGQKVGLVGKNGCGKS----TLLALLK--NEISAdgGSYTFPGNWQLAWVNQETPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 92 RGSALAMI------FQDPLTTLNPVLTIGEQMAEAILeHAR---VAPAEVRRRCIDSLRRVGITSPEtrLSQYPHEFSGG 162
Cdd:PRK10636 77 PQPALEYVidgdreYRQLEAQLHDANERNDGHAIATI-HGKldaIDAWTIRSRAASLLHGLGFSNEQ--LERPVSDFSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1208293942 163 MRQRVAIAIALLNSPDLIIADEPTTALDVTiqgQIIAEMQALQRETGTaMIWITHDLGVVAELADRI 229
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGT-LILISHDRDFLDPIVDKI 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-230 |
3.71e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 8 VLEVRNLQTVFHDLrgawPALNGLSLTLHAGEVLGLVGESGSGKSVAgFSILGLVDRP--GEITRGEVIfkgrdllalpp 85
Cdd:TIGR03719 322 VIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTL-FRMITGQEQPdsGTIEIGETV----------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 eaqrrlrgsALAMIFQDPlTTLNPVLTIGEQMAEAiLEHARVAPAEVRRRCI---------DSLRRVGitspetrlsqyp 156
Cdd:TIGR03719 386 ---------KLAYVDQSR-DALDPNKTVWEEISGG-LDIIKLGKREIPSRAYvgrfnfkgsDQQKKVG------------ 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 157 hEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDV-TIQgqiiAEMQALQRETGTAMIwITHD---LgvvaelaDRIA 230
Cdd:TIGR03719 443 -QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLR----ALEEALLNFAGCAVV-ISHDrwfL-------DRIA 507
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
124-235 |
4.01e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 124 HAR---VAPAEVRRRCIDSLRRVGitspetrLSQYPHEFSG----GMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQ 196
Cdd:NF033858 363 HARlfhLPAAEIAARVAEMLERFD-------LADVADALPDslplGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1208293942 197 IIAEMQALQRETG-TamIWI-THDLGvVAELADRIAVMYAG 235
Cdd:NF033858 436 FWRLLIELSREDGvT--IFIsTHFMN-EAERCDRISLMHAG 473
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
158-233 |
4.34e-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: 49.49 E-value: 4.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIWITHDLGVVAELADRIAVMY 233
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-231 |
1.23e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 131 EVRRRC----IDSLRRVGITSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQR 206
Cdd:PTZ00265 1327 DVKRACkfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
90 100
....*....|....*....|....*
gi 1208293942 207 ETGTAMIWITHDLGVVAElADRIAV 231
Cdd:PTZ00265 1407 KADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-238 |
1.33e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 3 RDRAPV-LEVRNLQTvfhdlrgawPALNG-LSLTLHAGEVLGLVGESGSGKSVAGFSILGLvDRPgeiTRGEVIFKGRDL 80
Cdd:PRK11288 251 RPLGEVrLRLDGLKG---------PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGA-TRR---TAGQVYLDGKPI 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 81 -LALPPEAQRRlrGSAL--------AMIfqdplttlnPVLTIGEQMAEAILEHARVA--------PAEVRRRCIDSLRrV 143
Cdd:PRK11288 318 dIRSPRDAIRA--GIMLcpedrkaeGII---------PVHSVADNINISARRHHLRAgclinnrwEAENADRFIRSLN-I 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 144 GITSPETRLSQypheFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAEMQALQrETGTAMIWITHDLGVVA 223
Cdd:PRK11288 386 KTPSREQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVL 460
|
250
....*....|....*
gi 1208293942 224 ELADRIAVMYAGDIV 238
Cdd:PRK11288 461 GVADRIVVMREGRIA 475
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
105-241 |
1.57e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 TTLnpVLTIGEQMAEAILEHARVAPAEVRRRCIDSLRR---VGITSpeTRLSQYPHEFSGGMRQRVAIA--IALLNSPDL 179
Cdd:cd03238 35 STL--VNEGLYASGKARLISFLPKFSRNKLIFIDQLQFlidVGLGY--LTLGQKLSTLSGGELQRVKLAseLFSEPPGTL 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALqRETGTAMIWITHDLGVVaELADRIAVM------YAGDIVEIG 241
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-235 |
2.86e-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: 47.46 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 26 PALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDRpgeiTRGEVIFKGRDLLAlppeAQrrlrgsaLAMIFQdplT 105
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK----LSGSVSVPGSIAYV----SQ-------EPWIQN---G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 106 TLNPVLTIGEQMAEAILEharvapaEVRRRCidSLRRvgitspetRLSQYPH-------E----FSGGMRQRVAIAIALL 174
Cdd:cd03250 81 TIRENILFGKPFDEERYE-------KVIKAC--ALEP--------DLEILPDgdlteigEkginLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 175 NSPDLIIADEPTTALDVTIQGQIIAE--MQALQRetGTAMIWITHDLGVVAElADRIAVMYAG 235
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENciLGLLLN--NKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
160-218 |
3.74e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 3.74e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDvtiqgqiiAEM-----QALQRETGTAMIwITHD 218
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD--------AESvawleQFLHDYPGTVVA-VTHD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-247 |
6.12e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 35 LHAGEVLGLVGESGSGKSVAGFSILGLVDRPGEITRGEVIFKGRDllalPPEAQRRLRGSalaMIFQDPLTTLNPVLTIG 114
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGIT----PEEIKKHYRGD---VVYNAETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 115 EQMAEAilehARV-APA--------EVRRRCIDSL--RRVGITspETRLSQYPHEF----SGGMRQRVAIAIALLNSPDL 179
Cdd:TIGR00956 157 ETLDFA----ARCkTPQnrpdgvsrEEYAKHIADVymATYGLS--HTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 180 IIADEPTTALDVTIQGQIIAEMQALQRET-GTAMIWITHDLGVVAELADRIAVMYAGDIVEIGATDDVL 247
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILdTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAK 299
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
159-191 |
6.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 6.18e-05
10 20 30
....*....|....*....|....*....|...
gi 1208293942 159 FSGGMRQRVAIAIALLNSPDLIIADEPTTALDV 191
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-218 |
7.78e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKS-----VAGfsilGLVDRPGEITrgevifkgrdlLAlppeaqrrlRGSALAMIFQD 102
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKStliklLAG----ELAPVSGEIG-----------LA---------KGIKLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 PLTTLNPvltigeqmAEAILEH-ARVAPAEVRRRCIDSLRRVG-----ITSPETRlsqypheFSGGMRQRVAIAIALLNS 176
Cdd:PRK10636 384 QLEFLRA--------DESPLQHlARLAPQELEQKLRDYLGGFGfqgdkVTEETRR-------FSGGEKARLVLALIVWQR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1208293942 177 PDLIIADEPTTALDVTIQgQIIAEmqALQRETGtAMIWITHD 218
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMR-QALTE--ALIDFEG-ALVVVSHD 486
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-290 |
9.63e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVdrpgEITRGEViFKGRDLLALPPEA---QRRLRGSALamiFQDPL 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF----EISEGRV-WAERSIAYVPQQAwimNATVRGNIL---FFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 105 TTlnpvltigEQMAEAIlehaRVAPAEVrrrcidSLRRVGiTSPETRLSQYPHEFSGGMRQRVAIAIALLNSPDLIIADE 184
Cdd:PTZ00243 748 DA--------ARLADAV----RVSQLEA------DLAQLG-GGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 185 PTTALDVTIqGQIIAEMQALQRETGTAMIWITHDLGVVAeLADRIAVMYAGDIVEIGATDDVLDRPRHPYTRGLL----- 259
Cdd:PTZ00243 809 PLSALDAHV-GERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTSLYATLAAELkenkd 886
|
250 260 270
....*....|....*....|....*....|....
gi 1208293942 260 ---NSVPGDTARGERLRQIEGTAPPLSARPVGCA 290
Cdd:PTZ00243 887 skeGDADAEVAEVDAAPGGAVDHEPPVAKQEGNA 920
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-194 |
1.14e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.30 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 9 LEVRNLQTVFHDlrGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrpgeiTRGEVIFKGRDLLALPPEAQ 88
Cdd:cd03289 3 MTVKDLTAKYTE--GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-----TEGDIQIDGVSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 89 RRLRG--SALAMIFQDPL-TTLNPVltiGEQMAEAILehaRVApaevrrrcidslRRVGItspETRLSQYPHE------- 158
Cdd:cd03289 76 RKAFGviPQKVFIFSGTFrKNLDPY---GKWSDEEIW---KVA------------EEVGL---KSVIEQFPGQldfvlvd 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1208293942 159 ----FSGGMRQRVAIAIALLNSPDLIIADEPTTALD-VTIQ 194
Cdd:cd03289 135 ggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
160-245 |
2.99e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAemQALQRE-TGTAMIWITHDLGVVAELaDRIAVMYAGDIV 238
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIK 818
|
....*..
gi 1208293942 239 EIGATDD 245
Cdd:PLN03130 819 EEGTYEE 825
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-190 |
3.89e-04 |
|
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: 40.69 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 28 LNGLSLTLHAGEVLGLVGESGSGKSV-----AGFSILGLVdrpgeitRGEVIFKGRdllALPPEAQRRlrgSALAMifQD 102
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGVI-------TGEILINGR---PLDKNFQRS---TGYVE--QQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 103 PLttLNPVLTIgeqmAEAILEHArvapaevrrrcidSLRrvGITspetrLSQyphefsggmRQRVAIAIALLNSPDLIIA 182
Cdd:cd03232 88 DV--HSPNLTV----REALRFSA-------------LLR--GLS-----VEQ---------RKRLTIGVELAAKPSILFL 132
|
....*...
gi 1208293942 183 DEPTTALD 190
Cdd:cd03232 133 DEPTSGLD 140
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-241 |
6.99e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 6 APVLEVRNLQTVFhDLRGAWPALNGLSLTLHAGEVLGLVGESGSGKSVAGFSILGLVDrPGEITrgEVIFKGRdlLALPP 85
Cdd:PLN03232 612 APAISIKNGYFSW-DSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-HAETS--SVVIRGS--VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 86 EaqrrlrgsaLAMIFQDPLTtlnpvltigeqmaEAILEHARVAPaEVRRRCIDslrrvgITSPETRLSQYPHE------- 158
Cdd:PLN03232 686 Q---------VSWIFNATVR-------------ENILFGSDFES-ERYWRAID------VTALQHDLDLLPGRdlteige 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 159 ----FSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQIIAE--MQALQretGTAMIWITHDLGVVAeLADRIAVM 232
Cdd:PLN03232 737 rgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScmKDELK---GKTRVLVTNQLHFLP-LMDRIILV 812
|
....*....
gi 1208293942 233 YAGDIVEIG 241
Cdd:PLN03232 813 SEGMIKEEG 821
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
166-233 |
7.99e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 7.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208293942 166 RVAIAIALLNSPDLIIADEPTTALDV-TIQGQIIAEMQALQRETGTAMIWITHDlgvvAELADRIAVMY 233
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD----EELVDAADHIY 193
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-229 |
2.22e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 134 RRCIDSLRRVGITSpeTRLSQYPHEFSGGMRQRVAIAIALL---NSPDLIIADEPTTALDVTiqgQIIAEMQALQR--ET 208
Cdd:TIGR00630 807 SRKLQTLCDVGLGY--IRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFD---DIKKLLEVLQRlvDK 881
|
90 100
....*....|....*....|.
gi 1208293942 209 GTAMIWITHDLGVVaELADRI 229
Cdd:TIGR00630 882 GNTVVVIEHNLDVI-KTADYI 901
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
160-229 |
2.74e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208293942 160 SGGMRQRVAIAIALLNS---PDLIIADEPTTALDVTIQGQIIAEMQALQRETGTAMIwITHDLGVVaELADRI 229
Cdd:PRK00635 811 SGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-IEHNMHVV-KVADYV 881
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
160-218 |
3.81e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.78 E-value: 3.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDV-TIQ--GQIIAEMQalqretGTAMIwITHD 218
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVeTLEllEELLDSYQ------GTVLL-VSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
160-230 |
5.56e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 5.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 160 SGGMRQRVAIAIALLNSPDLIIADEPTTALDV-TIQgqiiAEMQALQRETGTAMIwITHD---LgvvaelaDRIA 230
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLR----ALEEALLEFPGCAVV-ISHDrwfL-------DRIA 509
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
31-225 |
6.27e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 37.66 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 31 LSLTLHAGeVLGLVGESGSGKS----------------VAGFSILGLVDRPGEITRGEVIFKGRDL---LALPPEAQRRL 91
Cdd:cd03242 15 LELEFEPG-VTVLVGENAQGKTnlleaisllatgkshrTSRDKELIRWGAEEAKISAVLERQGGELaleLTIRSGGGRKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 92 RGSALAMIFQDPLT-TLNPVLtigeqMAEAILEHARVAPAEvRRRCIDSLrrVGITSPE--TRLSQYPHefsgGMRQRVa 168
Cdd:cd03242 94 RLNGIKVRRLSDLLgVLNAVW-----FAPEDLELVKGSPAD-RRRFLDRL--LGQLEPAyaHVLSEYQK----ALRQRN- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1208293942 169 iaiALLNSP---DLIIADEPTTALDVTIQGQ--------IIAEMQALQRETGTAMIWITHDlgVVAEL 225
Cdd:cd03242 161 ---ALLKGPhrdDLLFFLNDKPAADFGSQGQqrtlalalKLAEIQLIKEVSGEYPVLLLDD--VLAEL 223
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
158-217 |
6.71e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 38.19 E-value: 6.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 158 EFSGGMRQRVAIAIALLNSPDLIIADEPTTALDVTIQGQiiaeMQALQRETGTAMIWITH 217
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY----MYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
151-229 |
7.91e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 151 RLSQYPHEFSGGMRQRVAIAIALLN---SPDLIIADEPTTAL---DVTiqgQIIAEMQALqRETGTAMIWITHDLGVVAe 224
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLhfhDVK---KLLEVLQRL-VDKGNTVVVIEHNLDVIK- 236
|
....*
gi 1208293942 225 LADRI 229
Cdd:cd03271 237 CADWI 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-240 |
8.49e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 37.86 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 31 LSLTLHAGEVLGLVGESGSGKSVagFS--ILGLVdRPgeiTRGEVIFKGRDLLALPPEAQRRLrgsaLAMIFQDP-LTTl 107
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKST--LAklLTGLY-RP---ESGEILLDGQPVTADNREAYRQL----FSAVFSDFhLFD- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208293942 108 npvltigeqmaEAILEHARVAPAEVRRRcidsLRRVGI---TSPE------TRLSQyphefsgGMRQRVAIAIALLNSPD 178
Cdd:COG4615 420 -----------RLLGLDGEADPARAREL----LERLELdhkVSVEdgrfstTDLSQ-------GQRKRLALLVALLEDRP 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1208293942 179 LIIADEptTALDvtiQ---------GQIIAEMQALqretGTAMIWITHDlgvvaE----LADRIAVMYAGDIVEI 240
Cdd:COG4615 478 ILVFDE--WAAD---QdpefrrvfyTELLPELKAR----GKTVIAISHD-----DryfdLADRVLKMDYGKLVEL 538
|
|
| |
