|
Name |
Accession |
Description |
Interval |
E-value |
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-336 |
4.11e-167 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 468.06 E-value: 4.11e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 11 GTREVLLDVNDLVVHFPAGRR--QGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRD 88
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGlfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 89 IASLTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGG 168
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 249 AAEIFAAPRHPYTWSLIAAAapPGPMRDELKRRHLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRLPALDAIGSHHYVA 328
Cdd:COG4608 242 RDELYARPLHPYTQALLSAV--PVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPGHQVA 319
|
....*...
gi 456355960 329 CHRVAELP 336
Cdd:COG4608 320 CHLAEEGS 327
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-334 |
2.70e-161 |
|
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: 452.97 E-value: 2.70e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPA---TSGQIVFGNRDIASL 92
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV-----VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 93 TGRPLREVR-RHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQA--ADLFPHQFSGGQ 169
Cdd:COG0444 76 SEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPErrLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 170 RQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPA 249
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 250 AEIFAAPRHPYTWSLIAAAAPPGPmrdELKRRHLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRLPALDAIGSHHYVAC 329
Cdd:COG0444 236 EELFENPRHPYTRALLSSIPRLDP---DGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVAC 312
|
....*
gi 456355960 330 HRVAE 334
Cdd:COG0444 313 HLYEE 317
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-268 |
1.88e-136 |
|
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: 397.90 E-value: 1.88e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPAGRR--QGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPaTSGQIVFGNRDI 89
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGlfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASLTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIG-TRSERDERVRRLLGDVGLPPQAADLFPHQFSGG 168
Cdd:COG4172 350 DGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
250 260
....*....|....*....|
gi 456355960 249 AAEIFAAPRHPYTWSLIAAA 268
Cdd:COG4172 510 TEQVFDAPQHPYTRALLAAA 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-273 |
5.40e-136 |
|
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: 396.20 E-value: 5.40e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 4 ADAIRGTGTREVLLDVNDLVVHFPAGRRQGkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIV 83
Cdd:COG1123 248 GRAAPAAAAAEPLLEVRNLSKRYPVRGKGG----VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 84 FGNRDIASLTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPH 163
Cdd:COG1123 324 FDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
250 260 270
....*....|....*....|....*....|
gi 456355960 244 VEQAPAAEIFAAPRHPYTWSLIAAAAPPGP 273
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-247 |
2.27e-116 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 335.63 E-value: 2.27e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR 95
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSE-RDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLC 174
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQA 247
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-270 |
1.12e-112 |
|
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: 327.15 E-value: 1.12e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGR 95
Cdd:COG1124 1 MLEVRNLSVSYGQGGRR-----VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGtrsERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCI 175
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
250
....*....|....*
gi 456355960 256 PRHPYTWSLIAAAAP 270
Cdd:COG1124 230 PKHPYTRELLAASLA 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-335 |
1.78e-112 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 329.74 E-value: 1.78e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 13 REVLLDVNDLVVHFP-AGRRQ---GKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRD 88
Cdd:PRK15079 5 KKVLLEVADLKVHFDiKDGKQwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 89 IASLTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPL-----DLlgigTRSERDERVRRLLGDVGLPPQAADLFPH 163
Cdd:PRK15079 85 LLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLrtyhpKL----SRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 244 VEQAPAAEIFAAPRHPYTWSLIAAAAPPGPMRDELKRRHLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRLPALDaiGS 323
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLE--GS 318
|
330
....*....|...
gi 456355960 324 -HHYVACHRVAEL 335
Cdd:PRK15079 319 fRHAVSCLKVDPL 331
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-334 |
9.14e-110 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 322.68 E-value: 9.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRRQGKPS-FVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASL 92
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRGLFKPErLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 93 TGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQR 172
Cdd:PRK11308 83 DPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 173 LCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 253 FAAPRHPYTWSLIAAAapPGPMRDELKRRHLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRLPALDAIGSHHyVACHRV 332
Cdd:PRK11308 243 FNNPRHPYTQALLSAT--PRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRL-VACFAV 319
|
..
gi 456355960 333 AE 334
Cdd:PRK11308 320 EQ 321
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-278 |
1.11e-98 |
|
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: 301.22 E-value: 1.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPA----TSGQIVFGNRDIAS 91
Cdd:COG4172 6 LLSVEDLSVAFGQGGGT-----VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREVR-RHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADL--FPHQFSGG 168
Cdd:COG4172 81 LSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdaYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270
....*....|....*....|....*....|....*
gi 456355960 249 AAEIFAAPRHPYTWSLIAA-----AAPPGPMRDEL 278
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAeprgdPRPVPPDAPPL 275
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-332 |
1.95e-81 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 259.40 E-value: 1.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFP--AGRRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAS 91
Cdd:PRK10261 311 EPILQVRNLVTRFPlrSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQ 171
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 172 RLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAE 251
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 252 IFAAPRHPYTWSLIAAAAPPGPMRDELKRRHLvkgdppspvdpppgcrfAQRCPAAIDKCAQRLPA--LDAIGSHHYVAC 329
Cdd:PRK10261 551 VFENPQHPYTRKLMAAVPVADPSRQRPQRVLL-----------------SDDLPSNIHLRGEEVAAvsLQCVGPGHYVAQ 613
|
...
gi 456355960 330 HRV 332
Cdd:PRK10261 614 PQS 616
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-285 |
4.76e-80 |
|
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: 252.52 E-value: 4.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPAT---SGQIVFGNRDIA 90
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD-------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 SLtgrPLREVRRHLQIVFQDPFSALNPRRrAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQR 170
Cdd:COG1123 75 EL---SEALRGRRIGMVFQDPMTQLNPVT-VGDQIAEALENLGL-SRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 171 QRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAA 250
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 456355960 251 EIFAAPRH----PYTWSLIAAAAPPGPMRDELKR-RHLVK 285
Cdd:COG1123 229 EILAAPQAlaavPRLGAARGRAAPAAAAAEPLLEvRNLSK 268
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-334 |
2.66e-77 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 240.01 E-value: 2.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 5 DAIRGTGTREVLLDVNDLVVHF--PAGRrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPA---TS 79
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 80 GQIVFGNRDIASLTGRPLREVR-RHLQIVFQDPFSALNPRRRAGDQIREPLDL-LGIGTRSERDERVRrLLGDVGLPP-- 155
Cdd:PRK09473 74 GSATFNGREILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVR-MLDAVKMPEar 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 156 QAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEV 235
Cdd:PRK09473 153 KRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 236 AVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAAAappgPMRDElKRRHL--VKGDPPSPVDPPPGCRFAQRCPAAIDKCaQ 313
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV----PRLDA-EGESLltIPGNPPNLLRLPKGCPFQPRCPHAMEIC-S 306
|
330 340
....*....|....*....|.
gi 456355960 314 RLPALDAIGSHHYVACHRVAE 334
Cdd:PRK09473 307 SAPPLEEFGPGRLRACFKPVE 327
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-267 |
1.54e-76 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 235.89 E-value: 1.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrdiasltGR 95
Cdd:COG4167 4 LLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILIN--------GH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PL----REVR-RHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQR 170
Cdd:COG4167 76 KLeygdYKYRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 171 QRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAA 250
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTA 235
|
250
....*....|....*..
gi 456355960 251 EIFAAPRHPYTWSLIAA 267
Cdd:COG4167 236 EVFANPQHEVTKRLIES 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-275 |
1.16e-74 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 230.85 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR 95
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCI 175
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF 241
|
250 260
....*....|....*....|
gi 456355960 256 pRHPYTWSLIAAAAPPGPMR 275
Cdd:TIGR02769 242 -KHPAGRNLQSAVLPEHPVR 260
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-280 |
1.89e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 232.66 E-value: 1.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 19 VNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLR 98
Cdd:COG1135 4 LENLSKTFPTKGGP-----VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 99 EVRRHLQIVFQDpFSALNpRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARA 178
Cdd:COG1135 79 AARRKIGMIFQH-FNLLS-SRTVAENVALPLEIAGV-PKAEIRKRVAELLELVGLSDKA-DAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 179 MAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRH 258
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
250 260
....*....|....*....|..
gi 456355960 259 PYTWSLIAAAAPPGPMRDELKR 280
Cdd:COG1135 235 ELTRRFLPTVLNDELPEELLAR 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-268 |
5.35e-73 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 234.98 E-value: 5.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAgrRQG----KPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPAtSGQIVFGNRDI 89
Cdd:PRK15134 273 SPLLDVEQLQVAFPI--RKGilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASLTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIG-TRSERDERVRRLLGDVGLPPQAADLFPHQFSGG 168
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250 260
....*....|....*....|
gi 456355960 249 AAEIFAAPRHPYTWSLIAAA 268
Cdd:PRK15134 510 CERVFAAPQQEYTRQLLALS 529
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-275 |
1.04e-72 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 226.11 E-value: 1.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR 95
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCI 175
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF 242
|
250 260
....*....|....*....|
gi 456355960 256 pRHPYTWSLIAAAAPPGPMR 275
Cdd:PRK10419 243 -SSPAGRVLQNAVLPAFPVR 261
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-330 |
4.69e-72 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 226.55 E-value: 4.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPagrrQGKPSFvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP----ATSGQIVFGNRDIAS 91
Cdd:PRK11022 3 LLNVDKLSVHFG----DESAPF-RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLRE-VRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAA--DLFPHQFSGG 168
Cdd:PRK11022 78 ISEKERRNlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrlDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 249 AAEIFAAPRHPYTWSLIAAAappgPMRDELKRR-HLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRLPALDAIGSHHyV 327
Cdd:PRK11022 238 AHDIFRAPRHPYTQALLRAL----PEFAQDKARlASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQ-S 312
|
...
gi 456355960 328 ACH 330
Cdd:PRK11022 313 KCH 315
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
32-257 |
1.43e-68 |
|
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: 214.37 E-value: 1.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 32 QGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDp 111
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FSALNpRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:cd03258 91 FNLLS-SRTVFENVALPLEIAGVP-KAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPR 257
Cdd:cd03258 168 TSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
25-268 |
3.49e-65 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 209.27 E-value: 3.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 25 HFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHL 104
Cdd:PRK11153 10 VFPQGGRT-----IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 105 QIVFQDpFSALNpRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPD 184
Cdd:PRK11153 85 GMIFQH-FNLLS-SRTVFDNVALPLELAGT-PKAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 185 LIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSL 264
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....
gi 456355960 265 IAAA 268
Cdd:PRK11153 241 IQST 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-267 |
2.14e-60 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 201.86 E-value: 2.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFpagRRQGKPSFVhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPA-----TSGQIVFGNRDIA 90
Cdd:PRK15134 5 LLAIENLSVAF---RQQQTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 SLTGRPLREVR-RHLQIVFQDPFSALNPRRRAGDQIREPLDL-LGIGTRSERDERVRrLLGDVGLPPQAADL--FPHQFS 166
Cdd:PRK15134 80 HASEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILN-CLDRVGIRQAAKRLtdYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 167 GGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250 260
....*....|....*....|.
gi 456355960 247 APAAEIFAAPRHPYTWSLIAA 267
Cdd:PRK15134 239 NRAATLFSAPTHPYTQKLLNS 259
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-260 |
2.09e-58 |
|
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: 188.26 E-value: 2.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFpaGRRQgkpsfVHavDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAS 91
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRV-----VL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREVRRHLQIVFQDP--FSALNprrragdqIRE----PLDLLGIGTRSERDERVRRLLGDVGLpPQAADLFPHQF 165
Cdd:COG1127 72 LSEKELYELRRRIGMLFQGGalFDSLT--------VFEnvafPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|....*
gi 456355960 246 QAPAAEIFAAPrHPY 260
Cdd:COG1127 223 EGTPEELLASD-DPW 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-281 |
7.90e-58 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 197.00 E-value: 7.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFG-------NRD 88
Cdd:PRK10261 12 VLAVENLNIAFMQEQQK-----IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 89 IASLTGRPLREVRR----HLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADL--FP 162
Cdd:PRK10261 87 VIELSEQSAAQMRHvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILsrYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 163 HQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGK 242
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 456355960 243 IVEQAPAAEIFAAPRHPYTWSLIAAAAPPGPMR-DELKRR 281
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVPQLGAMKgLDYPRR 286
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-330 |
5.04e-56 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 185.11 E-value: 5.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHF--PAGRrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP----ATSGQIVFGNRDI 89
Cdd:COG4170 3 LLDIRNLTIEIdtPQGR-------VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASLTGRPLRE-VRRHLQIVFQDPFSALNPRRRAGDQIRE--PLDLLGiGT----RSERDERVRRLLGDVGLPPQAADL-- 160
Cdd:COG4170 76 LKLSPRERRKiIGREIAMIFQEPSSCLDPSAKIGDQLIEaiPSWTFK-GKwwqrFKWRKKRAIELLHRVGIKDHKDIMns 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 161 FPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYL 240
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 241 GKIVEQAPAAEIFAAPRHPYTWSLIAAAA---PPGPMRDELkrrHLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRlPA 317
Cdd:COG4170 235 GQTVESGPTEQILKSPHHPYTKALLRSMPdfrQPLPHKSRL---NTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PR 310
|
330
....*....|...
gi 456355960 318 LDAIGSHHYvACH 330
Cdd:COG4170 311 LRKIKGHEF-ACH 322
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-257 |
2.68e-55 |
|
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: 179.84 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRP 96
Cdd:COG1122 1 IELENLSFSYPGGTP--------ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPFsalnprrragDQIREPL---DL------LGIgTRSERDERVRRLLGDVGLPPQaADLFPHQFSG 167
Cdd:COG1122 70 LRELRRKVGLVFQNPD----------DQLFAPTveeDVafgpenLGL-PREEIRERVEEALELVGLEHL-ADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 168 GQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQA 247
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
250
....*....|
gi 456355960 248 PAAEIFAAPR 257
Cdd:COG1122 217 TPREVFSDYE 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-260 |
1.94e-54 |
|
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: 178.08 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFpaGRRQgkpsfVHavDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRP 96
Cdd:cd03261 1 IELRGLTKSF--GGRT-----VL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDP--FSALNPRRRAGDQIREPLDLlgigTRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLC 174
Cdd:cd03261 72 LYRLRRRMGMLFQSGalFDSLTVFENVAFPLREHTRL----SEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*.
gi 456355960 255 APrHPY 260
Cdd:cd03261 227 SD-DPL 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-267 |
1.00e-52 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 174.59 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHF--PAG--RRQgkpsFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRdi 89
Cdd:PRK15112 2 ETLLEVRNLSKTFryRTGwfRRQ----TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 aSLTGRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQ 169
Cdd:PRK15112 76 -PLHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 170 RQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPA 249
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*...
gi 456355960 250 AEIFAAPRHPYTWSLIAA 267
Cdd:PRK15112 235 ADVLASPLHELTKRLIAG 252
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
38-247 |
5.94e-52 |
|
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: 170.78 E-value: 5.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLRevRRHLQIVFQDPfsALNP 117
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPE--RRNIGMVFQDY--ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:cd03259 86 HLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 456355960 198 AIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQA 247
Cdd:cd03259 164 KLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-246 |
1.03e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 170.61 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT 93
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE-----VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLREVRR-HLQIVFQDPFsaLNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQR 172
Cdd:COG1136 77 ERELARLRRrHIGFVFQFFN--LLPELTALENVALPLLLAGVS-RKERRERARELLERVGLGDRL-DHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 173 LCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIqKFCDEVAVMYLGKIVEQ 246
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
40-260 |
1.71e-51 |
|
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: 171.67 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRH-LQIVFQDpFsALNPR 118
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQS-F-ALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd03294 117 RTVLENVAFGLEVQGVP-RAEREERAAEALELVGLEGWE-HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 199 IQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPY 260
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-260 |
5.25e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 172.59 E-value: 5.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 13 REVLLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIasl 92
Cdd:COG3842 2 AMPALELENVSKRYGD---------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 93 TGRPLRevRRHLQIVFQDPfsALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQR 172
Cdd:COG3842 70 TGLPPE--KRNVGMVFQDY--ALFPHLTVAENVAFGLRMRGVP-KAEIRARVAELLELVGLEGLA-DRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 173 LCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDlgviQK----FCDEVAVMYLGKIVEQAP 248
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD----QEealaLADRIAVMNDGRIEQVGT 219
|
250
....*....|..
gi 456355960 249 AAEIFAAPRHPY 260
Cdd:COG3842 220 PEEIYERPATRF 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-252 |
1.14e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.70 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR 95
Cdd:COG3638 2 MLELRNLSKRYPGGTP--------ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPfsALNPRRRAGD--------QIREPLDLLGIGTRSERdERVRRLLGDVGLPPQA---ADlfphQ 164
Cdd:COG3638 74 ALRRLRRRIGMIFQQF--NLVPRLSVLTnvlagrlgRTSTWRSLLGLFPPEDR-ERALEALERVGLADKAyqrAD----Q 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
....*...
gi 456355960 245 EQAPAAEI 252
Cdd:COG3638 227 FDGPPAEL 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-330 |
2.32e-50 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 170.37 E-value: 2.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRrqgkpSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP----ATSGQIVFGNRDIAS 91
Cdd:PRK15093 3 LLDIRNLTIEFKTSD-----GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREVRRH-LQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTR-----SERDERVRRLLGDVGL--PPQAADLFPH 163
Cdd:PRK15093 78 LSPRERRKLVGHnVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIkdHKDAMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 244 VEQAPAAEIFAAPRHPYTWSLIAAAAPPGPMRDELKRRHLVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRlPALDAIGS 323
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRLTGAKN 316
|
....*..
gi 456355960 324 HHYvACH 330
Cdd:PRK15093 317 HLY-ACH 322
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-252 |
6.15e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.39 E-value: 6.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFpagrrqGKpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAsltgRP 96
Cdd:COG1131 1 IEVRGLTKRY------GD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPfsALNPRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLCIA 176
Cdd:COG1131 68 PAEVRRRIGYVPQEP--ALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
41-267 |
6.29e-50 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 167.18 E-value: 6.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPA----TSGQIVfgnrdiasLTGRPL--REVR-RHLQIVFQDPFS 113
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVL--------LDGKPVapCALRgRKIATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNPRRRAGDQIREPLDLLGigtRSERDERVRRLLGDVGL--PPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALG---KPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAA 267
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
38-259 |
6.33e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 166.32 E-value: 6.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaSLTGRPLREVRRHLQIVFQDpFSaLNP 117
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKVGMVFQQ-FN-LFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIRE-PLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:COG1126 91 HLTVLENVTLaPIKVKKM-SKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 197 VAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHP 259
Cdd:COG1126 169 PELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-243 |
1.40e-49 |
|
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: 164.97 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTaqavMRLV----PATSGQIVFGNRDIASL 92
Cdd:cd03255 1 IELKNLSKTYGGGGEK-----VQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILggldRPTSGEVRVDGTDISKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 93 TGRPLREVRR-HLQIVFQdpFSALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQ 171
Cdd:cd03255 72 SEKELAAFRRrHIGFVFQ--SFNLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGLG-DRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 172 RLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIqKFCDEVAVMYLGKI 243
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
39-252 |
3.80e-49 |
|
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: 163.89 E-value: 3.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPA-----TSGQIVFGNRDIASLTGRPLrEVRRHLQIVFQDPfs 113
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVL-ELRRRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 alNP-RRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAAD-LFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDrLHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 192 VSALDVAIQAQILNLLKRLQRErdLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
40-267 |
3.36e-47 |
|
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: 159.39 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDpfSALNPRR 119
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELRRKIGYVIQQ--IGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQA-ADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd03295 91 TVEENIALVPKLLKWP-KEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 199 IQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAA 267
Cdd:cd03295 170 TRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-238 |
1.30e-46 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 157.25 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrdiasltGRP 96
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-----VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD--------GEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPfsALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIA 176
Cdd:cd03293 68 VTGPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVP-KAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVM 238
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
17-242 |
1.21e-44 |
|
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: 150.80 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRp 96
Cdd:cd03229 1 LELKNVSKRYGQ---------KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPfsALNPRRRAGDQIREPLdllgigtrserdervrrllgdvglppqaadlfphqfSGGQRQRLCIA 176
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGK 242
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
16-271 |
5.00e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 151.62 E-value: 5.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFpaGRRQGkpsfvhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRD--IASLT 93
Cdd:PRK11701 6 LLSVRGLTKLY--GPRKG-------CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqLRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLREvRRHLQ-----IVFQDPFSALNPRRRAGDQIREPLdlLGIGTRSERDERVRRL--LGDVGLPPQAADLFPHQFS 166
Cdd:PRK11701 77 ALSEAE-RRRLLrtewgFVHQHPRDGLRMQVSAGGNIGERL--MAVGARHYGDIRATAGdwLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 167 GGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|....*
gi 456355960 247 APAAEIFAAPRHPYTWSLIAAAAPP 271
Cdd:PRK11701 234 GLTDQVLDDPQHPYTQLLVSSVLQV 258
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
17-252 |
8.39e-44 |
|
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: 150.80 E-value: 8.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRrqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRP 96
Cdd:cd03256 1 IEVENLSKTYPNGK--------KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPfsALNPRRRAGDQI------REPL--DLLGIGTRSERdERVRRLLGDVGLPPQA---ADlfphQF 165
Cdd:cd03256 73 LRQLRRQIGMIFQQF--NLIERLSVLENVlsgrlgRRSTwrSLFGLFPKEEK-QRALAALERVGLLDKAyqrAD----QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
....*..
gi 456355960 246 QAPAAEI 252
Cdd:cd03256 226 DGPPAEL 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-242 |
8.85e-44 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 149.54 E-value: 8.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 19 VNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLR 98
Cdd:cd03225 2 LKNLSFSYPDGARP-------ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 99 EVRRHLQIVFQDP---FSALNPRrragDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCI 175
Cdd:cd03225 72 ELRRKVGLVFQNPddqFFGPTVE----EEVAFGLENLGL-PEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdLTYIFISHDLGVIQKFCDEVAVMYLGK 242
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-225 |
1.02e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 148.31 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrdias 91
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGG-----VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 ltGRPLREVRRHLQIVFQDPfsALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQ 171
Cdd:COG1116 72 --GKPVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVP-KAERRERARELLELVGLA-GFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 456355960 172 RLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDL 225
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-265 |
1.57e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 150.30 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPagrrqgkpSFvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAslTGRP 96
Cdd:COG1118 3 IEVRNISKRFG--------SF-TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREvrRHLQIVFQDPfsALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIA 176
Cdd:COG1118 72 PRE--RRVGFVFQHY--ALFPHMTVAENIAFGLRVRPPS-KAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
....*....
gi 456355960 257 RHPYTWSLI 265
Cdd:COG1118 226 ATPFVARFL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-253 |
1.56e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.19 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVhfpagRRQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgr 95
Cdd:COG1120 1 MLEAENLSV-----GYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALN------------PRRRAgdqirepldllgIGTRSERDER-VRRLLGDVGLPPQAADLFp 162
Cdd:COG1120 69 SRRELARRIAYVPQEPPAPFGltvrelvalgryPHLGL------------FGRPSAEDREaVEEALERTGLEHLADRPV- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 163 HQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGK 242
Cdd:COG1120 136 DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
250
....*....|.
gi 456355960 243 IVEQAPAAEIF 253
Cdd:COG1120 216 IVAQGPPEEVL 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
40-260 |
1.21e-40 |
|
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: 151.14 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP--FS---- 113
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRRQIGVVLQDVflFSgtir 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ---ALNpRRRAGD-QIREPLDLLGIgtrserDERVRRL-------LGDVGlppqaadlfpHQFSGGQRQRLCIARAMAPE 182
Cdd:COG2274 567 eniTLG-DPDATDeEIIEAARLAGL------HDFIEALpmgydtvVGEGG----------SNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 183 PDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAAPRHPY 260
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
39-243 |
1.28e-40 |
|
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: 141.51 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaSLTGRPLREVRRHLQIVFQDpFSaLNPR 118
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQ-FN-LFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIRE-PLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:cd03262 91 LTVLENITLaPIKVKGM-SKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 456355960 198 AIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:cd03262 169 ELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-256 |
2.64e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFpagrrQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaS 91
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV--------R 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREVRR-------HLQIVFQDPFSA-------LNPRRRagdqirepldLLGIGTRSERdERVRRLLGDVGLppqa 157
Cdd:COG1121 65 LFGKPPRRARRrigyvpqRAEVDWDFPITVrdvvlmgRYGRRG----------LFRRPSRADR-EAVDEALERVGL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 158 ADLFPHQF---SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDE 234
Cdd:COG1121 130 EDLADRPIgelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDR 208
|
250 260
....*....|....*....|..
gi 456355960 235 VAVMyLGKIVEQAPAAEIFAAP 256
Cdd:COG1121 209 VLLL-NRGLVAHGPPEEVLTPE 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
39-256 |
3.16e-40 |
|
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: 141.22 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAsltgrPLREVRRHLQIVFQDpfSALNPR 118
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRPVNTVFQN--YALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd03300 87 LTVFENIAFGLRLKKLP-KAEIKERVAEALDLVQLEGYA-NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 199 IQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
16-268 |
4.01e-40 |
|
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: 141.51 E-value: 4.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVvHFPAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR 95
Cdd:TIGR02323 3 LLQVSGLS-KSYGGGK--------GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHL------QIVFQDPFSALNPRRRAGDQIREplDLLGIGTRSERDER--VRRLLGDVGLPPQAADLFPHQFSG 167
Cdd:TIGR02323 74 QLSEAERRRlmrtewGFVHQNPRDGLRMRVSAGANIGE--RLMAIGARHYGNIRatAQDWLEEVEIDPTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 168 GQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQA 247
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 456355960 248 PAAEIFAAPRHPYTWSLIAAA 268
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
38-251 |
5.91e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 5.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDpFSALnP 117
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-FRLL-P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:COG2884 93 DRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLSDKA-KALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 198 AIQAQILNLLKRLQRERdlTYIFI-SHDLGVIQKFCDEVAVMYLGKIVEQAPAAE 251
Cdd:COG2884 171 ETSWEIMELLEEINRRG--TTVLIaTHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-242 |
1.59e-39 |
|
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: 137.13 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrP 96
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-------VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL---D 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDP--FSalnprrragDQIREPLdllgigtrserdervrrllgdvglppqaadlfphqFSGGQRQRLC 174
Cdd:cd03228 71 LESLRKNIAYVPQDPflFS---------GTIRENI-----------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGK 242
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-257 |
4.95e-39 |
|
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: 137.95 E-value: 4.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFpAGrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRP 96
Cdd:cd03219 1 LEVRGLTKRF-GG--------LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRhLQIV--FQDP--FSALNPRR--RAGDQIREPLDLLGIGTRSERD---ERVRRLLGDVGLPP----QAADLfph 163
Cdd:cd03219 69 PHEIAR-LGIGrtFQIPrlFPELTVLEnvMVAAQARTGSGLLLARARREERearERAEELLERVGLADladrPAGEL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 qfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:cd03219 145 --SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
250
....*....|....
gi 456355960 244 VEQAPAAEIFAAPR 257
Cdd:cd03219 222 IAEGTPDEVRNNPR 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-261 |
6.16e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 138.25 E-value: 6.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFpaGRRqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMR-------LVP--ATSGQI 82
Cdd:COG1117 7 TLEPKIEVRNLNVYY--GDK-------QALKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPgaRVEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 83 VFGNRDIASlTGRPLREVRRHLQIVFQDP----FSalnprrragdqIRE----PLDLLGIGTRSERDERVRRLLGDVGLP 154
Cdd:COG1117 74 LLDGEDIYD-PDVDVVELRRRVGMVFQKPnpfpKS-----------IYDnvayGLRLHGIKSKSELDEIVEESLRKAALW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 155 P--------QAADLfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQreRDLTYIFISHDLG 226
Cdd:COG1117 142 DevkdrlkkSALGL-----SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQ 214
|
250 260 270
....*....|....*....|....*....|....*
gi 456355960 227 VIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYT 261
Cdd:COG1117 215 QAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-191 |
7.62e-39 |
|
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: 134.70 E-value: 7.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLREVRRHLQIVFQDPFsaLNPRRR 120
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 121 AGDQIREPLDLLGIGTR--SERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:pfam00005 76 VRENLRLGLLLKGLSKRekDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
43-261 |
1.94e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 136.80 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrDIASLTGRPL-------REVRRHLQIVFQDpFSaL 115
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSLsqqkgliRQLRQHVGFVFQN-FN-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 NPRRRAGDQIRE-PLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSA 194
Cdd:PRK11264 97 FPHRTVLENIIEgPVIVKGE-PKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 195 LDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYT 261
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
39-242 |
5.40e-38 |
|
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: 132.75 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQdpfsalnpr 118
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL---PLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 rragdqirepldllgigtrserdervrrllgdvglppqaadlfphqFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 456355960 199 IQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGK 242
Cdd:cd00267 115 SRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
35-254 |
6.31e-38 |
|
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: 136.02 E-value: 6.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGnrdIASLTGRPLREVRRHLQIVFQDPfs 113
Cdd:TIGR04520 12 ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtVDG---LDTLDEENLWEIRKKVGMVFQNP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 alnprrraGDQI-----REplDL------LGIgTRSERDERVRRLLGDVGLPPQaADLFPHQFSGGQRQRLCIARAMAPE 182
Cdd:TIGR04520 87 --------DNQFvgatvED--DVafglenLGV-PREEMRKRVDEALKLVGMEDF-RDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 183 PDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLG-VIQkfCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
40-252 |
1.29e-37 |
|
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: 134.03 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQ-IVFGNrDIAsltgRPLREVRRHLQIVFQDPfsALNPR 118
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGH-DVV----REPREVRRRIGIVFQDL--SVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd03265 88 LTGWENLYIHARLYGVP-GAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 456355960 199 IQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-246 |
2.06e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 132.17 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQdpfsalnprrr 120
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL---SPKELARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 agdqirePLDLLGIGTRSERDerVRRLlgdvglppqaadlfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQ 200
Cdd:cd03214 81 -------ALELLGLAHLADRP--FNEL------------------SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 456355960 201 AQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
40-246 |
2.31e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 140.69 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDPF----SAL 115
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTFlfsgTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 N----PRRRAGD-QIREPLDLLGIgtrserDERVRRL-------LGDVGlppqaadlfpHQFSGGQRQRLCIARAMAPEP 183
Cdd:COG1132 432 EniryGRPDATDeEVEEAAKAAQA------HEFIEALpdgydtvVGERG----------VNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 184 DLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
40-246 |
2.37e-37 |
|
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: 133.00 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP--FSAlnp 117
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSRISIIPQDPvlFSG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 rrragdQIREPLDLLGIGTrserDERVRRLLGDVGLPPQAADLFPH----------QFSGGQRQRLCIARAMAPEPDLIV 187
Cdd:cd03244 93 ------TIRSNLDPFGEYS----DEELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 188 CDEAVSALDVAIQAQILNLLKRlqRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:cd03244 163 LDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEF 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-252 |
3.48e-37 |
|
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: 133.44 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFpagrrqGKpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAsltgR 95
Cdd:COG4555 1 MIEVENLSKKY------GK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFsaLNPRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAADLFpHQFSGGQRQRLCI 175
Cdd:COG4555 68 EPREARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
42-243 |
3.66e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.25 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP--FSAlnprr 119
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWRRQVAYVPQEPalWGG----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLLGigtRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:COG4619 89 TVRDNLPFPFQLRE---RKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 456355960 200 QAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:COG4619 166 TRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
38-258 |
6.09e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.59 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTaqavMRLV----PATSGQIVFGNRDIaslTGRPLREvrRHLQIVFQDPfs 113
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagleDPTSGEILIGGRDV---TDLPPKD--RNIAMVFQSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNPRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVS 193
Cdd:COG3839 85 ALYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLEDLL-DRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 194 ALDVAIQAQILNLLKRLQRERDLTYIFISHD------LGviqkfcDEVAVMYLGKIVEQAPAAEIFAAPRH 258
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveamtLA------DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-243 |
9.26e-37 |
|
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: 130.21 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGrrqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIasltGRP 96
Cdd:cd03230 1 IEVRNLSKRYGKK---------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPfsALNPRRRAGDQIRepldllgigtrserdervrrllgdvglppqaadlfphqFSGGQRQRLCIA 176
Cdd:cd03230 68 PEEVKRRIGYLPEEP--SLYENLTVRENLK--------------------------------------LSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-254 |
1.67e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.83 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrdiaslt 93
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATY-------ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLRE-----VRRHLQIVFQDP---FSALNPRrragDQIREPLDLLGIgTRSERDERVRRLLGDVGLPpQAADLFPHQF 165
Cdd:PRK13635 68 GMVLSEetvwdVRRQVGMVFQNPdnqFVGATVQ----DDVAFGLENIGV-PREEMVERVDQALRQVGME-DFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVE 245
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
....*....
gi 456355960 246 QAPAAEIFA 254
Cdd:PRK13635 221 EGTPEEIFK 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-238 |
1.01e-35 |
|
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: 128.81 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 19 VNDLVVHFpaGRRqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLR 98
Cdd:cd03235 2 VEDLTVSY--GGH-------PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI--------RVFGKPLE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 99 EVRRHLQIVFQ----DP--------FSALNPRRRAGdqirepldLLGIGTRSERdERVRRLLGDVGLppqaADLFPHQF- 165
Cdd:cd03235 65 KERKRIGYVPQrrsiDRdfpisvrdVVLMGLYGHKG--------LFRRLSKADK-AKVDEALERVGL----SELADRQIg 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 166 --SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVM 238
Cdd:cd03235 132 elSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-255 |
1.11e-35 |
|
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: 135.66 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 10 TGTREVLLDVNDLVVHFPAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDI 89
Cdd:COG4988 330 PAAGPPSIELEDVSFSYPGGRP--------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASLtgrPLREVRRHLQIVFQDP--FSalnprrragDQIREPLDLlgiGTRSERDERVRRLLGDVGLPPQAADLfPHQF-- 165
Cdd:COG4988 402 SDL---DPASWRRQIAWVPQNPylFA---------GTIRENLRL---GRPDASDEELEAALEAAGLDEFVAAL-PDGLdt 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 ---------SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIqKFCDEVA 236
Cdd:COG4988 466 plgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRIL 542
|
250
....*....|....*....
gi 456355960 237 VMYLGKIVEQAPAAEIFAA 255
Cdd:COG4988 543 VLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-260 |
1.37e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 135.66 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrP 96
Cdd:COG4987 334 LELEDVSFRYPGAGRP-------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL---D 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDP--FSAlnprrragdQIREPLdLLGIGTRSerDERVRRLLGDVGLPPQAADLfPH----------- 163
Cdd:COG4987 404 EDDLRRRIAVVPQRPhlFDT---------TLRENL-RLARPDAT--DEELWAALERVGLGDWLAAL-PDgldtwlgeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKFcDEVAVMYLGKI 243
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRI 547
|
250
....*....|....*..
gi 456355960 244 VEQAPAAEIFAAPRHPY 260
Cdd:COG4987 548 VEQGTHEELLAQNGRYR 564
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
34-244 |
1.54e-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: 128.39 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 34 KPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASltgrPLREVRRHLQIVFQDP-- 111
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQSLGYCPQFDal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FSALNPRrragDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQaADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:cd03263 87 FDELTVR----EHLRFYARLKGL-PKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-253 |
2.12e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.49 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 32 QGKPSFvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLREVRRHLQIVFQDP 111
Cdd:PRK13648 18 QSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FSALnprrrAGDQIRepLDL-LGIGTRS----ERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLI 186
Cdd:PRK13648 93 DNQF-----VGSIVK--YDVaFGLENHAvpydEMHRRVSEALKQVDMLERA-DYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 187 VCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
35-267 |
3.30e-35 |
|
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: 128.23 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLREvrRHLQIVFQDpfSA 114
Cdd:cd03296 13 GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQE--RNVGFVFQH--YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRRRAGDQIREPLDLLGIGTRSERDE---RVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSERPPEAEiraKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAA 267
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
56-265 |
1.60e-34 |
|
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: 128.77 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 56 IVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLRevRRHLQIVFQDpfSALNPRRRAGDQIREPLDLLGIG 135
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV---TNVPPH--LRHINMVFQS--YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 136 tRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERD 215
Cdd:TIGR01187 74 -RAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 456355960 216 LTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLI 265
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
38-245 |
1.98e-34 |
|
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: 125.44 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLREvrRHLQIVFQDpfSALNP 117
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKD--RDIAMVFQN--YALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDLLGIGtRSERDERVR---RLLGDVGLppqaADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSA 194
Cdd:cd03301 86 HMTVYDNIAFGLKLRKVP-KDEIDERVRevaELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 456355960 195 LDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
39-254 |
2.25e-34 |
|
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: 125.80 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP--FSaln 116
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI---SRKSLRSMIGVVLQDTflFS--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 prrragDQIREPLDLlgiGTRSERDERVRRLLGDVG-------LP--------PQAADLfphqfSGGQRQRLCIARAMAP 181
Cdd:cd03254 91 ------GTIMENIRL---GRPNATDEEVIEAAKEAGahdfimkLPngydtvlgENGGNL-----SQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 182 EPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIqKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLA 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-251 |
2.45e-34 |
|
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: 125.62 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLV----PATSGQIVFGNR 87
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGE-----LTILKGISLEVEAGESVAIVGASGSGKST----LLGLLagldRPTSGTVRLAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 88 DIASLTGRPLREVR-RHLQIVFQDpfSALNPRRRAGDQIREPLDLLGigtRSERDERVRRLLGDVGLPpQAADLFPHQFS 166
Cdd:COG4181 75 DLFALDEDARARLRaRHVGFVFQS--FQLLPTLTALENVMLPLELAG---RRDARARARALLERVGLG-HRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 167 GGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
....*
gi 456355960 247 APAAE 251
Cdd:COG4181 228 TAATA 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
32-253 |
4.14e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.70 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 32 QGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASlTGRPLREVRRHLQIVFQDP 111
Cdd:PRK13637 14 EGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 ----FS-------ALNPRRragdqirepldlLGIgTRSERDERVRRLLGDVGLPPQA-ADLFPHQFSGGQRQRLCIARAM 179
Cdd:PRK13637 93 eyqlFEetiekdiAFGPIN------------LGL-SEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 180 APEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
42-254 |
2.96e-33 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 123.03 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP--FSAlnprr 119
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQIGLVSQEPvlFDG----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 ragdQIREPLdLLGI--GTRSERDERVRR----------------LLGDVGLppqaadlfphQFSGGQRQRLCIARAMAP 181
Cdd:cd03249 92 ----TIAENI-RYGKpdATDEEVEEAAKKanihdfimslpdgydtLVGERGS----------QLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 182 EPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-264 |
3.23e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 124.12 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 31 RQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT-GRPLREVRRHLQIVFQ 109
Cdd:PRK13646 13 QKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 110 DPFSALNPRRRAGDQIREP----LDLlgigtrSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDL 185
Cdd:PRK13646 93 FPESQLFEDTVEREIIFGPknfkMNL------DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 186 IVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSL 264
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHI 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
40-260 |
3.36e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 126.69 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRH-LQIVFQDpfSALNPR 118
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIGTrSERDERVRRLLGDVGLPPQAADlFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:PRK10070 121 MTVLDNTAFGMELAGINA-EERREKALDALRQVGLENYAHS-YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 199 IQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPY 260
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
39-247 |
7.04e-33 |
|
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: 121.17 E-value: 7.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASltgrpLREVRRHLQIVFQDPfsALNPR 118
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALRRIGALIEAP--GFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIgtrseRDERVRRLLGDVGLpPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd03268 87 LTARENLRLLARLLGI-----RKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 456355960 199 IQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQA 247
Cdd:cd03268 161 GIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
51-256 |
1.92e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.05 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 51 GTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT-GRPLREVRRHLQIVFQDPFSALNPRRRAGDQIREPL 129
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKPLRKKVGIVFQFPEHQLFEETVEKDICFGPM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 130 DLlGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKR 209
Cdd:PRK13634 113 NF-GV-SEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 456355960 210 LQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK13634 191 LHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-261 |
2.52e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.10 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLV-----PATSGQIVFGNRDIASLTGRPLrEVRRHLQIVFQ--DP 111
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDPI-EVRREVGMVFQypNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FsalnPRRRAGDQIREPLDLLG-IGTRSERDERVRRLLGDVGLPPQAADL---FPHQFSGGQRQRLCIARAMAPEPDLIV 187
Cdd:PRK14267 97 F----PHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 188 CDEAVSALDVAIQAQILNLLKRLQreRDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYT 261
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-261 |
2.62e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 120.79 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 31 RQGKPSF--VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLV-----PATSGQIVFGNRDIASLtgrPLREVRRH 103
Cdd:PRK14247 7 RDLKVSFgqVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKM---DVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 104 LQIVFQDPFSALNPRRRAGDQIREPLDLLgIGTRSERDERVRRLLGDVGLPPQAADLF---PHQFSGGQRQRLCIARAMA 180
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRL-VKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQILNLLkrLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPY 260
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
.
gi 456355960 261 T 261
Cdd:PRK14247 241 T 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
43-259 |
2.79e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTG----------RPLREVRRHLQIVFQDpF 112
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRTRLTMVFQH-F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SALNPRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:PRK10619 102 NLWSHMTVLENVMEAPIQVLGL-SKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 193 SALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHP 259
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
40-255 |
2.80e-32 |
|
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: 120.41 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDPFsALNprr 119
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQDVF-LFN--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 ragDQIREPLdllGIGTRSERDERVRRLLgdvglppQAADLfpHQF-------------------SGGQRQRLCIARAMA 180
Cdd:cd03251 90 ---DTVAENI---AYGRPGATREEVEEAA-------RAANA--HEFimelpegydtvigergvklSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-255 |
3.63e-32 |
|
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: 125.98 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 10 TGTREV-----LLDVNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVF 84
Cdd:TIGR02203 319 TGTRAIerargDVEFRNVTFRYPGRDRP-------ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 85 GNRDIASLTgrpLREVRRHLQIVFQDPF-----SALNPRRRAGDQIRepldllgigtrserDERVRRLLGDVGLPpQAAD 159
Cdd:TIGR02203 392 DGHDLADYT---LASLRRQVALVSQDVVlfndtIANNIAYGRTEQAD--------------RAEIERALAAAYAQ-DFVD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 160 LFPHQF-----------SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVI 228
Cdd:TIGR02203 454 KLPLGLdtpigengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTI 531
|
250 260
....*....|....*....|....*..
gi 456355960 229 QKfCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:TIGR02203 532 EK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
41-256 |
4.19e-32 |
|
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: 119.75 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAsltgrPLREVRRHLQIVFQDpfSALNPRRR 120
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRDISYVPQN--YALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 AGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQ 200
Cdd:cd03299 88 VYKNIAYGLKKRKV-DKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 201 AQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-254 |
4.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.11 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaSLTGR 95
Cdd:PRK13636 5 ILKVEELNYNYSDG--------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLCI 175
Cdd:PRK13636 76 GLMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNL-KL-PEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-244 |
4.62e-32 |
|
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: 117.53 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAsltgrp 96
Cdd:cd03216 1 LELRGITKRFGG---------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lrevrrhlqivFQDPFSALNprrragdqirepldlLGIGTrserdervrrllgdVglppqaadlfpHQFSGGQRQRLCIA 176
Cdd:cd03216 66 -----------FASPRDARR---------------AGIAM--------------V-----------YQLSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-245 |
4.95e-32 |
|
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: 118.67 E-value: 4.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFpagrrqgKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrP 96
Cdd:cd03369 7 IEVENLSVRY-------APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDP--FSAlnprrragdQIREPLDLLGIGTrserDERVRRLL--GDVGLppqaadlfphQFSGGQRQR 172
Cdd:cd03369 77 LEDLRSSLTIIPQDPtlFSG---------TIRSNLDPFDEYS----DEEIYGALrvSEGGL----------NLSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 173 LCIARAMAPEPDLIVCDEAVSALDVAIQAqilnLLKRLQRE--RDLTYIFISHDLGVIQKfCDEVAVMYLGKIVE 245
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDA----LIQKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGEVKE 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-252 |
5.44e-32 |
|
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: 119.08 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFpagrrqGKpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgRP 96
Cdd:cd03224 1 LEVENLNAGY------GK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDP--FSALNprrragdqIREPLDL-LGIGTRSERDERVRRLLgdvglppqaaDLFP----------H 163
Cdd:cd03224 70 HERARAGIGYVPEGRriFPELT--------VEENLLLgAYARRRAKRKARLERVY----------ELFPrlkerrkqlaG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:cd03224 132 TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
....*....
gi 456355960 244 VEQAPAAEI 252
Cdd:cd03224 211 VLEGTAAEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
55-256 |
6.42e-32 |
|
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: 122.13 E-value: 6.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 55 GIVGESGSGKSTTAQAVMRLVPATSGQIVFGNR---DIASLTGRPLRevRRHLQIVFQDP--FSALN------------P 117
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIFLPPH--RRRIGYVFQEArlFPHLSvrgnllygrkraP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDLLGIGTrserdervrrLLgdvglppqaaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:COG4148 107 RAERRISFDEVVELLGIGH----------LL----------DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 198 AIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-256 |
6.45e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.01 E-value: 6.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 33 GKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTG-RPLREVRRHLQIVFQDP 111
Cdd:PRK13641 15 GTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FSALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:PRK13641 95 EAQLFENTVLKDVEFGPKNF-GF-SEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
44-259 |
8.70e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT--GRPLrevrrhlQIVFQDP--FSALNPRR 119
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpaERPV-------SMLFQENnlFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLlgigTRSERdERVRRLLGDVGLppqaADL---FPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:COG3840 91 NIGLGLRPGLKL----TAEQR-AQVEQALERVGL----AGLldrLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 197 VAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHP 259
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-256 |
9.38e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.49 E-value: 9.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaSLTGR 95
Cdd:PRK13639 1 ILETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCI 175
Cdd:PRK13639 72 SLLEVRKTVGIVFQNPDDQLFAPTVEEDVAFGPLNL-GL-SKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
.
gi 456355960 256 P 256
Cdd:PRK13639 228 I 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
40-256 |
1.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDP---FSALN 116
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 prrrAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK13640 102 ----VGDDVAFGLENRAV-PRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 197 VAIQAQILNLLKRLQRERDLTYIFISHDLGViQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
41-244 |
1.81e-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: 114.66 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIasltgrPLREVRRHLQIVFQDPFSALnprrr 120
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRKSIGYVMQDVDYQL----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 AGDQIREPLdLLGIGTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQ 200
Cdd:cd03226 85 FTDSVREEL-LLGLKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 456355960 201 AQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:cd03226 163 ERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-254 |
1.85e-30 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 115.41 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 24 VHFpaGRRQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRH 103
Cdd:cd03253 6 VTF--AYDPGRP----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 104 LQIVFQDP--FSalnprrragDQIREPLdllGIGTRSERDERVRRllgdvglPPQAADL------FPHQF---------- 165
Cdd:cd03253 77 IGVVPQDTvlFN---------DTIGYNI---RYGRPDATDEEVIE-------AAKAAQIhdkimrFPDGYdtivgerglk 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 -SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIV 244
Cdd:cd03253 138 lSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
250
....*....|
gi 456355960 245 EQAPAAEIFA 254
Cdd:cd03253 215 ERGTHEELLA 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
44-247 |
4.20e-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: 113.93 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFrVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrdiasltGRPLREVR---------RHLQIVFQDpfSA 114
Cdd:cd03297 17 IDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN--------GTVLFDSRkkinlppqqRKIGLVFQQ--YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRRragdQIREPLDL-LGIGTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVS 193
Cdd:cd03297 86 LFPHL----NVRENLAFgLKRKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 456355960 194 ALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQA 247
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-224 |
4.45e-30 |
|
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: 114.04 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDpfSA 114
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRRRAGDQIREPLDLLGIGTRsERDERVRRLLGDVGLPPQaADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSA 194
Cdd:cd03292 89 LLPDRNVYENVAFALEVTGVPPR-EIRKRVPAALELVGLSHK-HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190
....*....|....*....|....*....|
gi 456355960 195 LDVAIQAQILNLLKRLQReRDLTYIFISHD 224
Cdd:cd03292 167 LDPDTTWEIMNLLKKINK-AGTTVVVATHA 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-257 |
1.49e-29 |
|
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: 113.15 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLt 93
Cdd:COG0410 1 MPMLEVENLHAGYGG---------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 gRPLREVRRHLQIVFQDP--FSALNprrragdqIREPLdLLGIGTRSERDERVRRLlgdvglpPQAADLFP------HQF 165
Cdd:COG0410 71 -PPHRIARLGIGYVPEGRriFPSLT--------VEENL-LLGAYARRDRAEVRADL-------ERVYELFPrlkerrRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 ----SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLG 241
Cdd:COG0410 134 agtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 456355960 242 KIVEQAPAAEIFAAPR 257
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
34-255 |
8.70e-29 |
|
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: 111.04 E-value: 8.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 34 KPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLrevRRHLQIVFQDpfS 113
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE--N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNPRrragdQIREPLDLLGIGTRSERDERVRRLLG------------DVGLPPQAADLfphqfSGGQRQRLCIARAMAP 181
Cdd:cd03252 86 VLFNR-----SIRDNIALADPGMSMERVIEAAKLAGahdfiselpegyDTIVGEQGAGL-----SGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 182 EPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIqKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
41-254 |
9.33e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.13 E-value: 9.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFgnrDIASLTGRPLREVRRHLQIVFQDP---FSALNp 117
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEENVWDIRHKIGMVFQNPdnqFVGAT- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 rrrAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:PRK13650 99 ---VEDDVAFGLENKGI-PHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 198 AIQAQILNLLKRLQRERDLTYIFISHDLGVIqKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-224 |
1.14e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRp 96
Cdd:COG4525 4 LTVRHVSVRYPGGGQP-----QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lREVrrhlqiVFQDpfSALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIA 176
Cdd:COG4525 78 -RGV------VFQK--DALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHD 224
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-261 |
1.54e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.91 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP------ATSGQIVFGNRDIASLTGRPLRevrRHLQIVFQ--DPFsal 115
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLR---KEVGMVFQqpNPF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 nPRRRAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLF---PHQFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:PRK14246 103 -PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 193 SALDVAIQAQILNLLKRLQRErdLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYT 261
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
42-256 |
4.84e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASlTGRPLREVRRHLQIVFQDpFSaLNPRRRA 121
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEAGMVFQQ-FY-LFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 122 GDQIR-EPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQ 200
Cdd:PRK09493 95 LENVMfGPLRVRGAS-KEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 201 AQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK09493 173 HEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
14-238 |
6.00e-28 |
|
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: 108.68 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRRQGKPsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVF----GNRDI 89
Cdd:COG4778 2 TTLLEVENLSKTFTLHLQGGKR--LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASLTGRPLREVRRH--------LQIVfqdpfsalnPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAADLF 161
Cdd:COG4778 80 AQASPREILALRRRtigyvsqfLRVI---------PRVSALDVVAEPLLERGVD-REEARARARELLARLNLPERLWDLP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 162 PHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQReRDLTYIFISHDLGVIQKFCDEVAVM 238
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
41-256 |
6.22e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 111.35 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLVPA----TSGQIVFGNRDIaslTGRPLREvrRHLQIVFQDpfSALN 116
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAGlekpTEGQIFIDGEDV---THRSIQQ--RDICMVFQS--YALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 PRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK11432 91 PHMSLGENVGYGLKMLGVP-KEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 197 VAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-253 |
1.04e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.92 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPagrrqgkPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGNrDIA 90
Cdd:PRK13632 3 NKSVMIKVENVSFSYP-------NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGI-TIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 SLTgrpLREVRRHLQIVFQDP--------------FSALN---PRRRAGDQIREPLDLLGIGTRSERDervrrllgdvgl 153
Cdd:PRK13632 75 KEN---LKEIRKKIGIIFQNPdnqfigatveddiaFGLENkkvPPKKMKDIIDDLAKKVGMEDYLDKE------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 154 ppqaadlfPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCD 233
Cdd:PRK13632 140 --------PQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-AD 210
|
250 260
....*....|....*....|
gi 456355960 234 EVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13632 211 KVIVFSEGKLIAQGKPKEIL 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
44-256 |
1.14e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDI---ASLTGRPLREVRRHLQIVFQDpfSALNPRRR 120
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 AGDQIRE-PLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:COG4161 99 VMENLIEaPCKVLGL-SKEQAREKAMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 200 QAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQApAAEIFAAP 256
Cdd:COG4161 177 TAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
44-254 |
3.69e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNR--DIASLTG-RPLREVRRHLQIVFQDpfSALNPRRR 120
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdKAIRELRRNVGMVFQQ--YNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 AGDQIRE-PLDLLGIgTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:PRK11124 99 VQQNLIEaPCRVLGL-SKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 200 QAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ-------APAAEIFA 254
Cdd:PRK11124 177 TAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQgdascftQPQTEAFK 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-252 |
5.67e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.50 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPL-REVRRHL------------ 104
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV--------LWDGEPLdPEDRRRIgylpeerglypk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 105 -----QIVFqdpFSALN--PRRRAGDQIREPLDLLGIGTRseRDERVRRLlgdvglppqaadlfphqfSGGQRQRLCIAR 177
Cdd:COG4152 86 mkvgeQLVY---LARLKglSKAEAKRRADEWLERLGLGDR--ANKKVEEL------------------SKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 178 AMAPEPDLIVCDEAVSALD-VAIQAqILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDpVNVEL-LKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
38-254 |
6.46e-27 |
|
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: 110.66 E-value: 6.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVF--GNRDIASLTGRPLREVR--RHLQIVFQDpfS 113
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDMTKPGPDGRGRakRYIGILHQE--Y 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNPRRRAGDQIREPLDLlgigtrSERDERVRR----LLGDVGLPPQAA----DLFPHQFSGGQRQRLCIARAMAPEPDL 185
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGL------ELPDELARMkaviTLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 186 IVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-246 |
7.38e-27 |
|
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: 105.35 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRrqgkpsfvhAVDGISFRVCRGTtFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIasltGRP 96
Cdd:cd03264 1 LQLENLTKRYGKKR---------ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPfsALNPRRRAgdqiREPLDLLGIGTR---SERDERVRRLLGDVGLPPQAADLfPHQFSGGQRQRL 173
Cdd:cd03264 67 PQKLRRRIGYLPQEF--GVYPNFTV----REFLDYIAWLKGipsKEVKARVDEVLELVNLGDRAKKK-IGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 174 CIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
40-265 |
3.80e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLVP----ATSGQIVFGNRDIASLTGRplrevRRHLQIVFQDpfSAL 115
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetPDSGRIMLDGQDITHVPAE-----NRHVNTVFQS--YAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 NPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSAL 195
Cdd:PRK09452 98 FPHMTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 196 DVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLI 265
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-246 |
2.69e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 28 AGRRQGkpsfvhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIV 107
Cdd:PRK13657 345 DNSRQG-------VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 108 FQDPFsALNprRRAGDQIRepldllgIGTRSERDERVRRLLGDVglppQAADLFP--------------HQFSGGQRQRL 173
Cdd:PRK13657 415 FQDAG-LFN--RSIEDNIR-------VGRPDATDEEMRAAAERA----QAHDFIErkpdgydtvvgergRQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 174 CIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
44-225 |
2.95e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.43 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVR-RHLQIVFQdpFSALNPRRRAG 122
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 DQIREPLdLLGIGTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQ 202
Cdd:PRK11629 106 ENVAMPL-LIGKKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|...
gi 456355960 203 ILNLLKRLQRERDLTYIFISHDL 225
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDL 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-252 |
3.05e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.87 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMR----LVPATSGQIVFGNRDI 89
Cdd:COG1129 2 EPLLEMRGISKSFGG---------VKALDGVSLELRPGEVHALLGENGAGKST----LMKilsgVYQPDSGEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASLTgrPlREVRRH-LQIVFQDPfsALNPRRRAGDQI---REPLDLLGIGTRSERdERVRRLLGDVGL--PPQA--ADLf 161
Cdd:COG1129 69 RFRS--P-RDAQAAgIAIIHQEL--NLVPNLSVAENIflgREPRRGGLIDWRAMR-RRARELLARLGLdiDPDTpvGDL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 162 phqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLG 241
Cdd:COG1129 142 ----SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDG 216
|
250
....*....|.
gi 456355960 242 KIVEQAPAAEI 252
Cdd:COG1129 217 RLVGTGPVAEL 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
55-260 |
3.88e-25 |
|
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: 103.65 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 55 GIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIA-SLTGRPLREVRRHLQIVFQDpfSALNPRRRAGDQIREPLDLLG 133
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVRGNLRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 134 IGTRSERDERVRRLLGDVGLppqaADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRE 213
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHL----LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 456355960 214 RDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPY 260
Cdd:TIGR02142 181 FGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
35-254 |
4.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.39 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDI-ASLTG-RPLREVRRHLQIVFQDPF 112
Cdd:PRK13645 21 PFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SALNPRRRAGDQIREPLDLLGigTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:PRK13645 101 YQLFQETIEKDIAFGPVNLGE--NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 193 SALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
38-246 |
5.32e-25 |
|
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: 100.05 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRP---LREVRrhlqivfqdpfsA 114
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEER------------G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPQaADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSA 194
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGL-KKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 456355960 195 LDVaIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:cd03269 159 LDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-254 |
7.18e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.71 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPagrrqgKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGNRdiasLTG 94
Cdd:PRK13642 4 ILEVENLVFKYE------KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkIDGEL----LTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 95 RPLREVRRHLQIVFQDPFSALnprrrAGDQIReplDLLGIGTRSE---RDERVRRLlGDVGLPPQAADLF---PHQFSGG 168
Cdd:PRK13642 74 ENVWNLRRKIGMVFQNPDNQF-----VGATVE---DDVAFGMENQgipREEMIKRV-DEALLAVNMLDFKtrePARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAP 248
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA 223
|
....*.
gi 456355960 249 AAEIFA 254
Cdd:PRK13642 224 PSELFA 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-256 |
7.85e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.42 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRPLREVRRHLQIVFQDPFSALNP 117
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDL-LGIGTRSERDERVRRLLGDVGLppqaADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK13652 94 PTVEQDIAFGPINLgLDEETVAHRVSSALHMLGLEEL----RDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 197 VAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-255 |
1.32e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.16 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 29 GRRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRdIASL-----------TGRpl 97
Cdd:COG1134 30 RRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALlelgagfhpelTGR-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 98 revrrhlQIVFqdpFSALnprrragdqirepldLLGIgTRSERDERVRRL-----LGDvglppqAADLfP-HQFSGGQRQ 171
Cdd:COG1134 107 -------ENIY---LNGR---------------LLGL-SRKEIDEKFDEIvefaeLGD------FIDQ-PvKTYSSGMRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 172 RLCIARAMAPEPD-LIVcDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAA 250
Cdd:COG1134 154 RLAFAVATAVDPDiLLV-DEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
....*
gi 456355960 251 EIFAA 255
Cdd:COG1134 232 EVIAA 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
30-244 |
2.32e-24 |
|
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: 98.59 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 30 RRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASltgRPlREVRRHLQIVFQ 109
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EP-AEARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 110 DpfSALNPRRRAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCD 189
Cdd:cd03266 86 S--TGLYDRLTARENLEYFAGLYGL-KGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 190 EAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
44-247 |
2.96e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.31 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRplrevRRHLQIVFQDpfSALNPRRRAGD 123
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR-----DRKVGFVFQH--YALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 124 QIREPLDLLgigTRSER------DERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:PRK10851 94 NIAFGLTVL---PRRERpnaaaiKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 456355960 198 AIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIvEQA 247
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI-EQA 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-257 |
3.07e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGrp 96
Cdd:PRK09536 4 IDVSDLSVEFGD---------TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLLGIGTRSERDER-VRRLLGDVGLpPQAADLFPHQFSGGQRQRLCI 175
Cdd:PRK09536 73 -RAASRRVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAaVERAMERTGV-AQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
..
gi 456355960 256 PR 257
Cdd:PRK09536 230 DT 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-249 |
4.26e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.88 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR 95
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQ-----VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRR-HLQIVFQDpfSALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLC 174
Cdd:PRK10535 79 ALAQLRReHFGFIFQR--YHLLSHLTAAQNVEVPAVYAGLE-RKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPA 249
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-252 |
7.96e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 97.60 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGrrqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgRP 96
Cdd:TIGR03410 1 LEVSNLNVYYGQS---------HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQ--DPFSALNprrragdqIREPLdLLGIGTRSERDERVrrllgdvglPPQAADLFP--HQF------- 165
Cdd:TIGR03410 70 HERARAGIAYVPQgrEIFPRLT--------VEENL-LTGLAALPRRSRKI---------PDEIYELFPvlKEMlgrrggd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 -SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:TIGR03410 132 lSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVV 211
|
....*...
gi 456355960 245 EQAPAAEI 252
Cdd:TIGR03410 212 ASGAGDEL 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
34-244 |
8.57e-24 |
|
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: 97.28 E-value: 8.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 34 KPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP-- 111
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLRRNIGYVPQDVtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FSAlnprrragdQIREPLDLlgiGTRSERDERVRRLLGDVGLPPQAADLfPHQF-----------SGGQRQRLCIARAMA 180
Cdd:cd03245 90 FYG---------TLRDNITL---GAPLADDERILRAAELAGVTDFVNKH-PNGLdlqigergrglSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQkFCDEVAVMYLGKIV 244
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-253 |
8.73e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 97.85 E-value: 8.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVhfpagRRQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQ--IVFGNRdias 91
Cdd:COG1119 1 DPLLELRNVTV-----RRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGER---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREVRRHLQIVFqdpfSALNPRRRAGDQIREPL-----DLLGIGTR-SERD-ERVRRLLGDVGLPPQAADLFpHQ 164
Cdd:COG1119 68 RGGEDVWELRKRIGLVS----PALQLRFPRDETVLDVVlsgffDSIGLYREpTDEQrERARELLELLGLAHLADRPF-GT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
....*....
gi 456355960 245 EQAPAAEIF 253
Cdd:COG1119 223 AAGPKEEVL 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
40-256 |
9.54e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.32 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGT-------TF------GIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPL-REVRRHLQ 105
Cdd:PRK10575 13 ALRNVSFRVPGRTllhplslTFpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 106 ivfQDPFSAlnprrraGDQIREpldLLGIGT----------RSERDERVRRLLGDVGLPPQAADLFpHQFSGGQRQRLCI 175
Cdd:PRK10575 93 ---QLPAAE-------GMTVRE---LVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLV-DSLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
.
gi 456355960 256 P 256
Cdd:PRK10575 239 E 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
39-268 |
1.94e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrplrEVRRHLQIVFQDpfSALNPR 118
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----PYQRPINMMFQS--YALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPL--DLLgigTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK11607 106 MTVEQNIAFGLkqDKL---PKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 197 VAI----QAQILNLLKRLqrerDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAAA 268
Cdd:PRK11607 182 KKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-251 |
2.07e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 15 VLLDVNDLVVhfpagRRQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTaqavMRL----VPATSGQIVFGNRDIA 90
Cdd:PRK13548 1 AMLEARNLSV-----RLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTL----LRAlsgeLSPDSGEVRLNGRPLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 SLTGRPL---REV-RRHLQIVFqdPFSALnprrragDQIRepldlLGIGTRSERDERVRRL----LGDVGLPPQAADLFP 162
Cdd:PRK13548 68 DWSPAELarrRAVlPQHSSLSF--PFTVE-------EVVA-----MGRAPHGLSRAEDDALvaaaLAQVDLAHLAGRDYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 163 hQFSGGQRQRLCIARAMA------PEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVA 236
Cdd:PRK13548 134 -QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
250
....*....|....*
gi 456355960 237 VMYLGKIVEQAPAAE 251
Cdd:PRK13548 213 LLHQGRLVADGTPAE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-252 |
2.76e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT 93
Cdd:COG3845 255 EVVLEVENLSVRDDRG--------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLREVR-------RH---------------LQIVFQDPFSA---LNP---RRRAGDQIREpldlLGIGTRSErDERVR 145
Cdd:COG3845 327 PRERRRLGvayipedRLgrglvpdmsvaenliLGRYRRPPFSRggfLDRkaiRAFAEELIEE----FDVRTPGP-DTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 146 RLlgdvglppqaadlfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDL 225
Cdd:COG3845 402 SL------------------SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDL 462
|
250 260
....*....|....*....|....*..
gi 456355960 226 GVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:COG3845 463 DEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
41-243 |
5.86e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 93.82 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDpfsalnprrr 120
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDHVGYLPQD---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 agdqireplDLLGIGTRSErdervrrllgdvglppqaadlfpHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQ 200
Cdd:cd03246 85 ---------DELFSGSIAE-----------------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 456355960 201 AQILNLLKRLqRERDLTYIFISHDLGVIQKfCDEVAVMYLGKI 243
Cdd:cd03246 133 RALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
39-230 |
6.88e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.94 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDPFSALNpr 118
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIGTRSERdERVRRLLGDVGLPPQAADlFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIR-RRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190
....*....|....*....|....*....|..
gi 456355960 199 IQAQILNLLKRLQRErDLTYIFISHDLGVIQK 230
Cdd:PRK10908 172 LSEGILRLFEEFNRV-GVTVLMATHDIGLISR 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-224 |
7.65e-23 |
|
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: 94.08 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVhfpagRRQGKPSFvhavDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAsltgR 95
Cdd:COG4133 2 MLEAENLSC-----RRGERLLF----SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDPfsALNPRRRAgdqiREPLDLL-GIGTRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLC 174
Cdd:COG4133 69 AREDYRRRLAYLGHAD--GLKPELTV----RENLRFWaALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRlQRERDLTYIFISHD 224
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-256 |
7.81e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 24 VHFPAGRRQGKPSFvhavDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVfgnrdiasLTGRPLRE---- 99
Cdd:TIGR00958 484 VSFSYPNRPDVPVL----KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL--------LDGVPLVQydhh 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 100 -VRRHLQIVFQDP--FSalnprrragdqiREPLDLLGIGTRSERDERVRrllgDVGLPPQAADL---FPH---------- 163
Cdd:TIGR00958 552 yLHRQVALVGQEPvlFS------------GSVRENIAYGLTDTPDEEIM----AAAKAANAHDFimeFPNgydtevgekg 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 164 -QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAqilnLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGK 242
Cdd:TIGR00958 616 sQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
250
....*....|....
gi 456355960 243 IVEQAPAAEIFAAP 256
Cdd:TIGR00958 691 VVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-243 |
9.02e-23 |
|
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: 93.27 E-value: 9.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHfpagrrqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslT 93
Cdd:cd03215 2 EPVLEVRGLSVK-------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV---T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLREVRRHlqivfqdpfsalnprrragdqirepldllGIGTRSErdERVRRLLgdvgLPPQA-AD--LFPHQFSGGQR 170
Cdd:cd03215 66 RRSPRDAIRA-----------------------------GIAYVPE--DRKREGL----VLDLSvAEniALSSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 171 QRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
41-256 |
1.12e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 98.86 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDPFsalnprrR 120
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI---PREVLANSVAMVDQDIF-------L 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 AGDQIREPLDLLgigTRSERDERVRRLLGD-------VGLPPQ-AADLFP--HQFSGGQRQRLCIARAMAPEPDLIVCDE 190
Cdd:TIGR03796 565 FEGTVRDNLTLW---DPTIPDADLVRACKDaaihdviTSRPGGyDAELAEggANLSGGQRQRLEIARALVRNPSILILDE 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 191 AVSALDVAIQAQILNLLKRlqreRDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:TIGR03796 642 ATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
56-276 |
1.42e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.16 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 56 IVGESGSGKSTTAQAVMRLVPATSG-----QIVFGNRDIASLtgRPLREVRRHLQIVFQDPfsalNPRRRA-GDQIREPL 129
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY--RDVLEFRRRVGMLFQRP----NPFPMSiMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 130 DLLGIGTRSERDERVRRLLGDVGLPPQAADLF---PHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNL 206
Cdd:PRK14271 126 RAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 207 LKRLQRErdLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAAAAppGPMRD 276
Cdd:PRK14271 206 IRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLS--GDVKD 271
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
40-253 |
1.65e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.15 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGrpLREVRRHLQIVFQDPFSALNPRR 119
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LWDIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLlGIGTRSERdERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:PRK13633 103 VEEDVAFGPENL-GIPPEEIR-ERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 200 QAQILNLLKRLQRERDLTYIFISHDLG-VIQkfCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEeAVE--ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-225 |
1.86e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.38 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPagrrqGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGR 95
Cdd:PRK11248 1 MLQISHLYADYG-----GKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI--------TLDGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 PLREVRRHLQIVFQDpfSALNPRRRAGDQIREPLDLLGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCI 175
Cdd:PRK11248 64 PVEGPGAERGVVFQN--EGLLPWRNVQDNVAFGLQLAGVE-KMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDL 225
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-246 |
2.06e-22 |
|
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: 93.33 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 48 VCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrplrEVRRHLQIVFQDP--FSALNPRRRAGDQI 125
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENnlFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 126 REPLDLlgigtRSERDERVRRLLGDVGLPPQAADLfPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILN 205
Cdd:cd03298 96 SPGLKL-----TAEDRQAIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 456355960 206 LLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
40-246 |
9.46e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.96 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDPFSAlnprr 119
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFINYLPQEPYIF----- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 rAGdQIREPLdLLGIGTRSERDE-----RVRRLLGDVGLPPQA--ADLFPHQF--SGGQRQRLCIARAMAPEPDLIVCDE 190
Cdd:TIGR01193 561 -SG-SILENL-LLGAKENVSQDEiwaacEIAEIKDDIENMPLGyqTELSEEGSsiSGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 191 AVSALDVAIQAQILNLLKRLQrerDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQ 689
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
42-246 |
1.25e-21 |
|
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: 95.66 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDP--FS---ALN 116
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRAAIGIVPQDTvlFNdtiAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 PRR-RAG---DQIREPLDLLGIgtrserDERVRRL-------LGDVGLppqaadlfphQFSGGQRQRLCIARAMAPEPDL 185
Cdd:COG5265 452 IAYgRPDaseEEVEAAARAAQI------HDFIESLpdgydtrVGERGL----------KLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 186 IVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
41-254 |
1.45e-21 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 95.58 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLRevrRHLQIVFQDpfSALNPRrr 120
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLR---RQMGVVLQE--NVLFSR-- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 agdQIREPLDLLGIGTRSERDERVRRLLGD----VGLP--------PQAADLfphqfSGGQRQRLCIARAMAPEPDLIVC 188
Cdd:TIGR01846 546 ---SIRDNIALCNPGAPFEHVIHAAKLAGAhdfiSELPqgyntevgEKGANL-----SGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 189 DEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIqKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICRGR--TVIIIAHRLSTV-RACDRIIVLEKGQIAESGRHEELLA 680
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
42-256 |
1.95e-21 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 95.02 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTtaqaVMRL-----VPAtSGQIVFGNRDIASLTgrpLREVRRHLQIVFQD--PFSA 114
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKST----LLRLllgfeTPE-SGSVFYDGQDLAGLD---VQAVRRQLGVVLQNgrLMSG 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRRRAG------DQIREPLDLLGIgtrserDERVRRLlgDVGLppqaadlfpH--------QFSGGQRQRLCIARAMA 180
Cdd:TIGR03797 542 SIFENIAGgapltlDEAWEAARMAGL------AEDIRAM--PMGM---------HtvisegggTLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQILNLLKRLQrerdLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
41-252 |
2.65e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.30 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDPfsALNPRRR 120
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT---PSRELAKRLAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 agdqIREpldLLGIGtR--------SERDER-VRRLLGDVGLPPqAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:COG4604 92 ----VRE---LVAFG-RfpyskgrlTAEDREiIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-246 |
3.94e-21 |
|
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: 88.91 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPagrrqgkPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGrp 96
Cdd:cd03247 1 LSINNVSFSYP-------EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lrEVRRHLQIVFQDP--FSalnprrragDQIREpldllGIGTRserdervrrllgdvglppqaadlfphqFSGGQRQRLC 174
Cdd:cd03247 72 --ALSSLISVLNQRPylFD---------TTLRN-----NLGRR---------------------------FSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLkrLQRERDLTYIFISHDLGVIQKFcDEVAVMYLGKIVEQ 246
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
14-261 |
4.31e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFpaGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMR---LVP--ATSGQIVFGNRD 88
Cdd:PRK14239 3 EPILQVSDLSVYY--NKKK-------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPevTITGSIVYNGHN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 89 IASLTGRPLrEVRRHLQIVFQDPfsalNPRRRA-GDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFpHQ--- 164
Cdd:PRK14239 74 IYSPRTDTV-DLRKEIGMVFQQP----NPFPMSiYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-HDsal 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 -FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQreRDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:PRK14239 148 gLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|....*...
gi 456355960 244 VEQAPAAEIFAAPRHPYT 261
Cdd:PRK14239 226 IEYNDTKQMFMNPKHKET 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-252 |
7.59e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 7.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFpaGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrP 96
Cdd:COG1137 4 LEAENLVKSY--GKRT-------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL---P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREvRRHLQIVF--QDP--FSALNprrrAGDQIREPLDLLGIgTRSERDERVRRLLGDVGLPP---QAADlfphQFSGGQ 169
Cdd:COG1137 72 MHK-RARLGIGYlpQEAsiFRKLT----VEDNILAVLELRKL-SKKEREERLEELLEEFGITHlrkSKAY----SLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 170 RQRLCIARAMAPEPDLIVCDEAVSALD---VA-IQAQILNLlkrlqRERDLTyIFIS-HD----LGViqkfCDEVAVMYL 240
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIG-VLITdHNvretLGI----CDRAYIISE 211
|
250
....*....|..
gi 456355960 241 GKIVEQAPAAEI 252
Cdd:COG1137 212 GKVLAEGTPEEI 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
40-254 |
9.55e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 9.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIV------FQDPFs 113
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQVALVsqnvhlFNDTI- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNPRRRAGDQI-REPLdllgigtrsERDERVRRLLGDVGLPPQAADLFPHQ----FSGGQRQRLCIARAMAPEPDLIVC 188
Cdd:PRK11176 434 ANNIAYARTEQYsREQI---------EEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 189 DEAVSALDV----AIQAQilnlLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK11176 505 DEATSALDTeserAIQAA----LDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-256 |
1.19e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATS-----GQIVFGNRDIASLTGRpLREVRRHLQIVFQDPfsAL 115
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVN-LNRLRRQVSMVHPKP--NL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 NPRRrAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFPH---QFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:PRK14258 100 FPMS-VYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 193 SALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMY-----LGKIVEQAPAAEIFAAP 256
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSP 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-258 |
1.27e-20 |
|
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: 88.68 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLREVRRHLQIVFQDpfSALNPRRR 120
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV--------ILEGKQITEPGPDRMVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 AGDQIREPLD-LLGIGTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:TIGR01184 71 VRENIALAVDrVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 200 QAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGkiveqaPAAEI-------FAAPRH 258
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG------PAANIgqilevpFPRPRD 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
41-253 |
1.58e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRplrEVRRHLQIVFQDPfsaLNPRrr 120
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLARRLALLPQHH---LTPE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 aGDQIRE-------P-LDLLGigTRSERDE-RVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:PRK11231 90 -GITVRElvaygrsPwLSLWG--RLSAEDNaRVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
40-238 |
1.62e-20 |
|
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: 91.96 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLrevRRHLQIVFQDPFS------ 113
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFLfagtia 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ---ALNPRRRAGDQIREPLDLLGIGTR-SERDERVRRLLGDVGlppqaadlfpHQFSGGQRQRLCIARAMAPEPDLIVCD 189
Cdd:TIGR02857 414 eniRLARPDASDAEIREALERAGLDEFvAALPQGLDTPIGEGG----------AGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 456355960 190 EAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVM 238
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
38-244 |
1.72e-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: 88.54 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGNRdiasltgrPLREVRRHLQ---IVF----- 108
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLV--------PWKRRKKFLRrigVVFgqktq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 109 -------QDPFSALN-----PRRRAGDQIREPLDLLGIGtrSERDERVRRLlgdvglppqaadlfphqfSGGQRQRLCIA 176
Cdd:cd03267 106 lwwdlpvIDSFYLLAaiydlPPARFKKRLDELSELLDLE--ELLDTPVRQL------------------SLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-243 |
1.75e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 11 GTREVLldvNDLVVHFPAGRrqgkpsFVhavdgisfrvcrgttfGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRdia 90
Cdd:PRK11247 23 GERTVL---NQLDLHIPAGQ------FV----------------AVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 sltgrPLREVRRHLQIVFQDpfSALNPRRRAgdqirepLDLLGIGTRSERDERVRRLLGDVGLPPQAADlFPHQFSGGQR 170
Cdd:PRK11247 75 -----PLAEAREDTRLMFQD--ARLLPWKKV-------IDNVGLGLKGQWRDAALQALAAVGLADRANE-WPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 171 QRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-245 |
2.69e-20 |
|
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: 87.59 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 20 NDLVVHFPAGRRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVfGNRDIASLTGrplre 99
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-VRGRVSSLLG----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 100 vrrhLQIVFQDPFSAL-NPRRRAGdqirepldLLGIgTRSERDERVRRLLGDVGLpPQAADLFPHQFSGGQRQRLCIARA 178
Cdd:cd03220 91 ----LGGGFNPELTGReNIYLNGR--------LLGL-SRKEIDEKIDEIIEFSEL-GDFIDLPVKTYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 179 MAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-254 |
2.85e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.96 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 31 RQGKPSFVHavdGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQD 110
Cdd:PLN03232 1245 RPGLPPVLH---GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 111 P--FSA-----LNPRRRAGDQireplDLLGIGTRSERDERVRRllGDVGLPPQAADlFPHQFSGGQRQRLCIARAMAPEP 183
Cdd:PLN03232 1319 PvlFSGtvrfnIDPFSEHNDA-----DLWEALERAHIKDVIDR--NPFGLDAEVSE-GGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 184 DLIVCDEAVSALDVAIQAqilnLLKRLQRE--RDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PLN03232 1391 KILVLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-256 |
3.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDiaslTGRP--LREVRRHLQIVFQDPF 112
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID----TGDFskLQGIRKLVGIVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SALNPRRRAGDQIREPLDLLGIGTrsERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:PRK13644 88 TQFVGRTVEEDLAFGPENLCLPPI--EIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 193 SALDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
33-253 |
3.36e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 33 GKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT-GRPLREVRRHLQIVFQDP 111
Cdd:PRK13649 15 GTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 FSALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:PRK13649 95 ESQLFEETVLKDVAFGPQNF-GV-SQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 192 VSALDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-225 |
3.58e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGrrqgKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRP 96
Cdd:COG1101 2 LELKNLSKTFNPG----TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lrEVRRHLQI--VFQDPFS--------------ALNPRRRAGdqirepldlLGIG-TRSERD---ERVRRL-LG------ 149
Cdd:COG1101 75 --EYKRAKYIgrVFQDPMMgtapsmtieenlalAYRRGKRRG---------LRRGlTKKRRElfrELLATLgLGlenrld 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 150 -DVGLppqaadlfphqFSGGQRQrlCIARAMAP--EPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDL 225
Cdd:COG1101 144 tKVGL-----------LSGGQRQ--ALSLLMATltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-253 |
4.65e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKST----------TAQAVMRLVPATSGQIVFGNRDIASLTGRPLR---EVRRHL 104
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTlvthfnglikSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKnfkELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 105 QIVFQDPFSALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPD 184
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDIMFGPVAL-GV-KKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 185 LIVCDEAVSALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-254 |
4.72e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 32 QGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT--------------GRP- 96
Cdd:PRK13651 14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkekekvleklviQKTr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 ------LREVRRHLQIVFQDPFSALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQR 170
Cdd:PRK13651 94 fkkikkIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSM-GV-SKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 171 QRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAA 250
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
....
gi 456355960 251 EIFA 254
Cdd:PRK13651 251 DILS 254
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-252 |
5.32e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 45 SFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrplrEVRRHLQIVFQDP--FSALNPRRRAG 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PSRRPVSMLFQENnlFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 dqirepldlLGI--GTR--SERDERVRRLLGDVGLPPQAADLfPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:PRK10771 94 ---------LGLnpGLKlnAAQREKLHAIARQMGIEDLLARL-PGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 456355960 199 IQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
40-261 |
5.48e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMR---LVPA--TSGQIVFGNRDIASLTGRPLrEVRRHLQIVFQDPfsa 114
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDPV-EVRRRIGMVFQKP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 lNPRRRA-------GDQIRepldllgiGTRSERDERVRRLLGDVGLPPQAADLFPHQ---FSGGQRQRLCIARAMAPEPD 184
Cdd:PRK14243 101 -NPFPKSiydniayGARIN--------GYKGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 185 LIVCDEAVSALDVAIQAQILNLLKRLQreRDLTYIFISHDLGVIQKFCDEVAVM---------YLGKIVEQAPAAEIFAA 255
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNS 249
|
....*.
gi 456355960 256 PRHPYT 261
Cdd:PRK14243 250 PQQQAT 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-251 |
5.67e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGNR-DI 89
Cdd:COG3845 1 MMPPALELRGITKRFGG---------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlIDGKPvRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 90 ASltgrPlREVRRhLQI--VFQ-----DPFSALnprrragDQI---REPLDLLGIGTRSERdERVRRLLGDVGLP--PQA 157
Cdd:COG3845 72 RS----P-RDAIA-LGIgmVHQhfmlvPNLTVA-------ENIvlgLEPTKGGRLDRKAAR-ARIRELSERYGLDvdPDA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 158 --ADLfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEV 235
Cdd:COG3845 138 kvEDL-----SVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRV 211
|
250
....*....|....*.
gi 456355960 236 AVMYLGKIVEQAPAAE 251
Cdd:COG3845 212 TVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
39-246 |
6.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGNrdiaSLTGRPLREVRRHLQIVFQDPFSALNP 117
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGR----EVNAENEKWVRSKVGLVFQDPDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDLlGIGtRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:PRK13647 95 STVWDDVAFGPVNM-GLD-KDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 456355960 198 AIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:PRK13647 172 RGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-255 |
9.27e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 89.81 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrp 96
Cdd:COG4618 331 LSVENLTVVPPGSKR-------PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lREVR-RHLQIVFQDP-------------FSALNPR------RRAG--DQIrepLDL-LGIGTRserdervrrlLGDVGL 153
Cdd:COG4618 401 -REELgRHIGYLPQDVelfdgtiaeniarFGDADPEkvvaaaKLAGvhEMI---LRLpDGYDTR----------IGEGGA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 154 PpqaadlfphqFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKfCD 233
Cdd:COG4618 467 R----------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VD 534
|
250 260
....*....|....*....|..
gi 456355960 234 EVAVMYLGKIVEQAPAAEIFAA 255
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLAR 556
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
45-246 |
1.18e-19 |
|
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: 85.68 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 45 SFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrplrEVRRHLQIVFQDP--FSALNPRRRAG 122
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQENnlFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 DQIREPLDLlgigtRSERDERVRRLLGDVGLPPQAADLfPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQ 202
Cdd:TIGR01277 93 LGLHPGLKL-----NAEQQEKVVDAAQQVGIADYLDRL-PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 456355960 203 ILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQ 246
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
39-256 |
2.38e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.29 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREvRRHLQIVF--QDP--FSA 114
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHK-RARLGIGYlpQEAsiFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRrragDQIREPLDLLGIgTRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSA 194
Cdd:cd03218 90 LTVE----ENILAVLEIRGL-SKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 195 LD-VAIQaQILNLLKRLqRERDLTyIFIS-HDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:cd03218 164 VDpIAVQ-DIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-244 |
2.96e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTaqavMR-----LVPaTSGQIVFGNRDiasltgrPLREVRRHL-QI--VF- 108
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTT----IKmltgiLVP-TSGEVRVLGYV-------PFKRRKEFArRIgvVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 109 -----------QDPFsALN------PRRRAGDQIREPLDLLGIGtrSERDERVRRLlgdvglppqaadlfphqfSGGQRQ 171
Cdd:COG4586 103 qrsqlwwdlpaIDSF-RLLkaiyriPDAEYKKRLDELVELLDLG--ELLDTPVRQL------------------SLGQRM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 172 RLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:COG4586 162 RCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-265 |
2.99e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPAGRRqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAS 91
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQ-------PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LTGRPLREvrrHLQIVFQ--DPFSAL--------NPrrRAGD-QIREPLDLLGIGTRSERDERVRRLLGDVGlppqaadl 160
Cdd:PRK11160 407 YSEAALRQ---AISVVSQrvHLFSATlrdnlllaAP--NASDeALIEVLQQVGLEKLLEDDKGLNAWLGEGG-------- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 161 fpHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLkrLQRERDLTYIFISHDLGVIQKFcDEVAVMYL 240
Cdd:PRK11160 474 --RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQF-DRICVMDN 548
|
250 260
....*....|....*....|....*
gi 456355960 241 GKIVEQAPAAEIFAapRHPYTWSLI 265
Cdd:PRK11160 549 GQIIEQGTHQELLA--QQGRYYQLK 571
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
35-253 |
4.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTG-RPLREVRRHLQIVFQDPFS 113
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNPRRRAGDQIREPLDLlGIgTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVS 193
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNF-GI-PKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 194 ALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-247 |
4.22e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRRQgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLT 93
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHE-----LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEV--------SLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPL----REVR-----RHLQIVFQDpfSALNPRRRAGDQIREPLDLLGIGTRSERdERVRRLLGDVGLPpQAADLFPHQ 164
Cdd:PRK10584 71 GQPLhqmdEEARaklraKHVGFVFQS--FMLIPTLNALENVELPALLRGESSRQSR-NGAKALLEQLGLG-KRLDHLPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIV 244
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
...
gi 456355960 245 EQA 247
Cdd:PRK10584 226 EEA 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-245 |
6.15e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.17 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 35 PSFVHavdGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDP--F 112
Cdd:PLN03130 1252 PPVLH---GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPvlF 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SA-----LNPRRRAGD-QIREPLDllgigtRSERDERVRRllGDVGLPPQAADLfPHQFSGGQRQRLCIARAMAPEPDLI 186
Cdd:PLN03130 1326 SGtvrfnLDPFNEHNDaDLWESLE------RAHLKDVIRR--NSLGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 187 VCDEAVSALDVAIQAqilnLLKRLQRE--RDLTYIFISHDLGVIQKfCDEVAVMYLGKIVE 245
Cdd:PLN03130 1397 VLDEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
242-330 |
7.59e-18 |
|
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: 77.02 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 242 KIVEQAPAAEIFAAPRHPYTWSLIAAAAPPGPMRDELKRrhlVKGDPPSPVDPPPGCRFAQRCPAAIDKCAQRLPALDAI 321
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLIS---IPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEI 77
|
....*....
gi 456355960 322 GSHHYVACH 330
Cdd:TIGR01727 78 AEGHRVACH 86
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
51-261 |
7.73e-18 |
|
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: 81.88 E-value: 7.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 51 GTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLREVRRHLQIVFQDP--FSA-----LNPRRRAGD 123
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPilFSGsirfnLDPECKCTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 124 -QIREPLDLlgigtrSERDERVRRLLGdvGLPPQAADlFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQaq 202
Cdd:cd03288 124 dRLWEALEI------AQLKNMVKSLPG--GLDAVVTE-GGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-- 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 203 ilNLLKR--LQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAAPRHPYT 261
Cdd:cd03288 193 --NILQKvvMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
42-275 |
9.30e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDP--FSALNPRR 119
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGalFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLLGIGTRSErderVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHST----VMMKLEAVGLR-GAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 200 QAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPRHPYTWSLIAAAAPPGPMR 275
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFR 254
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-277 |
1.00e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.99 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgr 95
Cdd:PRK10789 313 ELDVNIRQFTYPQTDHP-------ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ-- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 pLREVRRHLQIVFQDPFsalnprrRAGDQIREPLDLLGIGTRSERDERVRRLLG---DVGLPPQAADLFPHQ----FSGG 168
Cdd:PRK10789 384 -LDSWRSRLAVVSQTPF-------LFSDTVANNIALGRPDATQQEIEHVARLASvhdDILRLPQGYDTEVGErgvmLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAP 248
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
250 260 270
....*....|....*....|....*....|..
gi 456355960 249 AAEIFAAP---RHPYTWSLIAAAAPPGPMRDE 277
Cdd:PRK10789 533 HDQLAQQSgwyRDMYRYQQLEAALDDAPEIRE 564
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-225 |
2.25e-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: 82.79 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRp 96
Cdd:TIGR02868 335 LELRDLSAGYPGAPP--------VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 lrEVRRHLQIVFQDP--FSAlnprrragdQIREPLdLLGIGTRSerDERVRRLLGDVGLPPQAADLfPH----------- 163
Cdd:TIGR02868 406 --EVRRRVSVCAQDAhlFDT---------TVRENL-RLARPDAT--DEELWAALERVGLADWLRAL-PDgldtvlgegga 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLkrLQRERDLTYIFISHDL 225
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-223 |
3.55e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.16 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfvhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVF-GNRDIASLTGR 95
Cdd:COG4178 363 LALEDLTLRTPDGRPL--------LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 96 P------LREvrrhlQIVFqdPFSAlnprrragdqirEPLDllgigtrserDERVRRLLGDVGLPPQAADL-----FPHQ 164
Cdd:COG4178 435 PylplgtLRE-----ALLY--PATA------------EAFS----------DAELREALEAVGLGHLAERLdeeadWDQV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 165 FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKrlQRERDLTYIFISH 223
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
49-256 |
6.62e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 49 CRGTTfGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNR---DIASltGRPLREVRRHLQIVFQDpfSALNPRRR-AG-- 122
Cdd:PRK11144 23 AQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLPPEKRRIGYVFQD--ARLFPHYKvRGnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 ------------DQIrepLDLLGIGTrserdervrrLLgdvglppqaaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDE 190
Cdd:PRK11144 98 rygmaksmvaqfDKI---VALLGIEP----------LL----------DRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 191 AVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-244 |
8.18e-17 |
|
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: 78.08 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 31 RQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP---ATSGQIVFgnrdiaslTGRPLR--EVRRHLQ 105
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILF--------NGQPRKpdQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 106 IVFQD-------------PFSALNPRRRAGDQirepldllgiGTRSERDERVRrlLGDVGLPPQAADLFPhQFSGGQRQR 172
Cdd:cd03234 85 YVRQDdillpgltvretlTYTAILRLPRKSSD----------AIRKKRVEDVL--LRDLALTRIGGNLVK-GISGGERRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 173 LCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-255 |
8.42e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 36 SFVhAVDGISFRVCRGTTFGIVGESGSGKSTTaqavMR----LVPATSGQivfgnrdiASLTGRPLrevrrhlqivfqDP 111
Cdd:NF033858 278 DFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTT----MKmltgLLPASEGE--------AWLFGQPV------------DA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 fSALNPRRRAG--DQ---------IREPLDL----LGIGtRSERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLCIA 176
Cdd:NF033858 333 -GDIATRRRVGymSQafslygeltVRQNLELharlFHLP-AAEIAARVAEMLERFDLAD-VADALPDSLPLGIRQRLSLA 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTyIFIS-HdlgviqkF------CDEVAVMYLGKIVEQAPA 249
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIStH-------FmneaerCDRISLMHAGRVLASDTP 481
|
....*.
gi 456355960 250 AEIFAA 255
Cdd:NF033858 482 AALVAA 487
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
43-245 |
9.54e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 81.36 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDPF-------SAL 115
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVlfdgtvrQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 NPRRRAGD-QIREPLDLLGIGTR--SER---DERVrrLLGdvGLppqaadlfphQFSGGQRQRLCIARAMAPE-PDLIVC 188
Cdd:PTZ00243 1405 DPFLEASSaEVWAALELVGLRERvaSESegiDSRV--LEG--GS----------NYSVGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 189 DEAVS----ALDVAIQAQILNLLKrlqrerDLTYIFISHDLGVIQKfCDEVAVMYLGKIVE 245
Cdd:PTZ00243 1471 DEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQ-YDKIIVMDHGAVAE 1524
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-249 |
1.22e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.18 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRL--VPATSGQIVFGNRDIASLTgrPLREVRRHLQIVFQdpfsalnpr 118
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP--PEERARLGIFLAFQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 rragdqirEPLDLLGIgtrserdeRVRRLLGDVGLppqaadlfphQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVA 198
Cdd:cd03217 85 --------YPPEIPGV--------KNADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 456355960 199 IQAQILNLLKRLqRERDLTYIFISHdLGVIQKFC--DEVAVMYLGKIVEQAPA 249
Cdd:cd03217 139 ALRLVAEVINKL-REEGKSVLIITH-YQRLLDYIkpDRVHVLYDGRIVKSGDK 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-252 |
1.62e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHfpagrrqgkpsfvHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRD----- 88
Cdd:COG1129 254 EVVLEVEGLSVG-------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirs 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 89 --------IASLTG-R------PLREVRRHLQIVFQDPFSA---LNPRR---RAGDQIREpldlLGIGTRSeRDERVRRL 147
Cdd:COG1129 321 prdairagIAYVPEdRkgeglvLDLSIRENITLASLDRLSRgglLDRRReraLAEEYIKR----LRIKTPS-PEQPVGNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 148 lgdvglppqaadlfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGV 227
Cdd:COG1129 396 ------------------SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPE 456
|
250 260
....*....|....*....|....*
gi 456355960 228 IQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:COG1129 457 LLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
40-255 |
2.64e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLRE-VRRHL-------------- 104
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI--------SILGQPTRQaLQKNLvayvpqseevdwsf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 105 -----QIVFQDPFSALNPRRRAGDQIREPLDllGIGTRSERDERVRRLLGDVglppqaadlfphqfSGGQRQRLCIARAM 179
Cdd:PRK15056 94 pvlveDVVMMGRYGHMGWLRRAKKRDRQIVT--AALARVDMVEFRHRQIGEL--------------SGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 180 APEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDeVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTA 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
57-244 |
3.48e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 57 VGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrplrEVRRHLQIVFQDpfSALNPRRRAGDQIREPLDLLGIGt 136
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-----PAERGVGMVFQS--YALYPHLSVAENMSFGLKLAGAK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 137 RSERDERVRrllgdvglppQAADLF---------PHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQ----I 203
Cdd:PRK11000 107 KEEINQRVN----------QVAEVLqlahlldrkPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQmrieI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 456355960 204 LNLLKRLQRerdlTYIFISHdlgviqkfcDEVAVMYLG-KIV 244
Cdd:PRK11000 177 SRLHKRLGR----TMIYVTH---------DQVEAMTLAdKIV 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-257 |
4.75e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.57 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 16 LLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTG- 94
Cdd:PRK11300 5 LLSVSGLMMRFGG---------LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 95 --------RPLREVR----------------RHLQIVFqdpFSAL--NPRRRagdqirepldllgigtRSERD--ERVRR 146
Cdd:PRK11300 76 qiarmgvvRTFQHVRlfremtvienllvaqhQQLKTGL---FSGLlkTPAFR----------------RAESEalDRAAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 147 LLGDVGLPP----QAADLfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFIS 222
Cdd:PRK11300 137 WLERVGLLEhanrQAGNL-----AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIE 211
|
250 260 270
....*....|....*....|....*....|....*
gi 456355960 223 HDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPR 257
Cdd:PRK11300 212 HDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
41-252 |
5.50e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.15 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPL----REVRRHLQIVFQdpFSALN 116
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI--------SLCGEPVpsraRHARQRVGVVPQ--FDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 PRRRAGDQIREPLDLLGIGTRSERdERVRRLLGDVGLpPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK13537 93 PDFTVRENLLVFGRYFGLSAAAAR-ALVPPLLEFAKL-ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 197 VAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLG-KIVEQAPAAEI 252
Cdd:PRK13537 171 PQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHALI 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-252 |
6.58e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLVPAT------SGQIVFgnr 87
Cdd:PRK13549 3 EYLLEMKNITKTFGG---------VKALDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSGVyphgtyEGEIIF--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 88 DIASLTGRPLREV-RRHLQIVFQDpfSALNPRRRAGDQI---REPLDllgiGTRSERDE---RVRRLLGDVGLppqaaDL 160
Cdd:PRK13549 67 EGEELQASNIRDTeRAGIAIIHQE--LALVKELSVLENIflgNEITP----GGIMDYDAmylRAQKLLAQLKL-----DI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 161 FPH----QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQReRDLTYIFISHDLGVIQKFCDEVA 236
Cdd:PRK13549 136 NPAtpvgNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTIC 214
|
250
....*....|....*.
gi 456355960 237 VMYLGKIVEQAPAAEI 252
Cdd:PRK13549 215 VIRDGRHIGTRPAAGM 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
43-243 |
7.91e-16 |
|
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: 75.59 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVfgnrdiasLTGRPL-----REVRRHLQIVFQDP--FSal 115
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL--------LDGKPIsqyehKYLHSKVSLVGQEPvlFA-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 nprrragdqiREPLDLLGIGTRSERDERVRRLlgdvglpPQAAD------LFPH-----------QFSGGQRQRLCIARA 178
Cdd:cd03248 102 ----------RSLQDNIAYGLQSCSFECVKEA-------AQKAHahsfisELASgydtevgekgsQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 179 MAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKfCDEVAVMYLGKI 243
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
41-252 |
9.86e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPL----REVRRHLQIVFQdpFSALN 116
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI--------TVLGVPVparaRLARARIGVVPQ--FDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 PRRragdQIREPLDLLG--IGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSA 194
Cdd:PRK13536 127 LEF----TVRENLLVFGryFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 195 LDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLG-KIVEQAPAAEI 252
Cdd:PRK13536 203 LDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALI 260
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
56-255 |
1.06e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 56 IVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRplrEVRRHLQIVFQDpfsALNPRRRAGDQI----REPLDL 131
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLLAQN---ATTPGDITVQELvargRYPHQP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 132 LGIGTRSERDERVRRLLGDVG---LPPQAADlfphQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLK 208
Cdd:PRK10253 112 LFTRWRKEDEEAVTKAMQATGithLADQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 456355960 209 RLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK10253 188 ELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
44-252 |
2.09e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRplreVRRHLQIVF--QDpfsalnpRRRA 121
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA----QRLARGLVYlpED-------RQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 122 GDQIREPL---------DLLGIGTRSERD----ERVRRLLG-DVGLPPQAAdlfpHQFSGGQRQRLCIARAMAPEPDLIV 187
Cdd:PRK15439 351 GLYLDAPLawnvcalthNRRGFWIKPAREnavlERYRRALNiKFNHAEQAA----RTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 188 CDEAVSALDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-250 |
2.33e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.79 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP--ATSGQIVFgnrDIASLTGRPLREV-RRHLQIVFQDpfSA 114
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYW---SGSPLKASNIRDTeRAGIVIIHQE--LT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 115 LNPRRRAGDQIREPLDLLGIGTRSERDERVRR---LLGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:TIGR02633 89 LVPELSVAENIFLGNEITLPGGRMAYNAMYLRaknLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 192 VSALDVAIQAQILNLLKRLQReRDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAA 250
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMS 226
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
244-311 |
2.33e-15 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 69.74 E-value: 2.33e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 244 VEQAPAAEIFAAPRHPYTWSLIAAAAPPGPMRDELkrrHLVKGDPPSPVDPPPGCRFAQRCPAAIDKC 311
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPL---YTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-245 |
2.72e-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: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 26 FPAGRRQGKP---------SF--VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrdiasltg 94
Cdd:COG0488 305 FPPPERLGKKvleleglskSYgdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG--------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 95 rplrevrRHLQIVF--QDpFSALNPRRRAGDQIREpldllgiGTRSERDERVRRLLGDVGLPPQAADLFPHQFSGGQRQR 172
Cdd:COG0488 376 -------ETVKIGYfdQH-QEELDPDKTVLDELRD-------GAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 173 LCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKrlqrerdlTY----IFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD--------DFpgtvLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-254 |
3.15e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.66 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 30 RRQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaSLTGRPLREVRRHLQIVFQ 109
Cdd:PRK13638 10 RYQDEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 110 DPFSALNPRRRAGDqIREPLDLLGIGtrseRDERVRRLlgDVGLPPQAADLFPHQ----FSGGQRQRLCIARAMAPEPDL 185
Cdd:PRK13638 85 DPEQQIFYTDIDSD-IAFSLRNLGVP----EAEITRRV--DEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 186 IVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIfISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
41-254 |
5.20e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLtgrPLRE-VRRHLQIVFQDPfsALNPRR 119
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHArARRGIGYLPQEA--SIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLLGIGTRSERDERVRRLLGDVGLpPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAI 199
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 200 QAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK10895 173 VIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
44-254 |
6.54e-15 |
|
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: 75.22 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAV--MRLVPATSGQIVF--------GNRDIASLTGRPL---------------- 97
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYhvalcekcGYVERPSKVGEPCpvcggtlepeevdfwn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 98 ------REVRRHLQIVFQDPFsALNPRRRAGDQIREPLDLLGIgtrsERDERVRR---LLGDVGLPPQ----AADLfphq 164
Cdd:TIGR03269 99 lsdklrRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEALEEIGY----EGKEAVGRavdLIEMVQLSHRithiARDL---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 fSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:TIGR03269 170 -SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
250
....*....|
gi 456355960 245 EQAPAAEIFA 254
Cdd:TIGR03269 249 EEGTPDEVVA 258
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
41-255 |
6.91e-15 |
|
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: 75.46 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFgnrDIASLTGRPLREVRRHLQIVFQD----PFSALN 116
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL---DGADLKQWDRETFGKHIGYLPQDvelfPGTVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 PRRRAGDQIrEPLDLLGIGTRSERDERVRRL-------LGDVGLPpqaadlfphqFSGGQRQRLCIARAMAPEPDLIVCD 189
Cdd:TIGR01842 411 NIARFGENA-DPEKIIEAAKLAGVHELILRLpdgydtvIGPGGAT----------LSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 190 EAVSALDVAIQAQILNLLKRLQReRDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGC-VDKILVLQDGRIARFGERDEVLAK 543
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
38-256 |
7.84e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.49 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRplrevRRHLQIVFQDpfSALNP 117
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-----DRDIAMVFQN--YALYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREPLDLLGIGtRSERDERVRrllgdvglppQAADLF---------PHQFSGGQRQRLCIARAMAPEPDLIVC 188
Cdd:PRK11650 90 HMSVRENMAYGLKIRGMP-KAEIEERVA----------EAARILeleplldrkPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 189 DEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHD------LGviqkfcDEVAVMYLGKIvEQ--APaAEIFAAP 256
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqveamtLA------DRVVVMNGGVA-EQigTP-VEVYEKP 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-235 |
3.63e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDlvVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIAS 91
Cdd:PRK10247 3 ENSPLLQLQN--VGYLAGDAK-------ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LtgrPLREVRRHLQIVFQDPfsALnprrrAGDQIREPLdLLGIGTRSERDE--RVRRLLGDVGLPPQAADLFPHQFSGGQ 169
Cdd:PRK10247 74 L---KPEIYRQQVSYCAQTP--TL-----FGDTVYDNL-IFPWQIRNQQPDpaIFLDDLERFALPDTILTKNIAELSGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 170 RQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKfCDEV 235
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
40-228 |
4.64e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 40 AVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQI-VFGNRDIASLTGRplREVRRHLQIVFQDPFSALNPR 118
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAYVPQR--SEVPDSLPLTVRDLVAMGRWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAgdqirepldLLGIGTRSERdERVRRLLGDVGLppqaADLFPHQF---SGGQRQRLCIARAMAPEPDLIVCDEAVSAL 195
Cdd:NF040873 85 RRG---------LWRRLTRDDR-AAVDDALERVGL----ADLAGRQLgelSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|...
gi 456355960 196 DVAIQAQILNLLKRLqRERDLTYIFISHDLGVI 228
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELV 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
44-255 |
6.24e-14 |
|
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: 73.06 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDP--FSAlnprrra 121
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPvlFSG------- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 122 gdQIREPLDLLGigtrSERDERV------RRLLGDVGLPPQAADlfpHQ-------FSGGQRQRLCIARAMAPEPDLIVC 188
Cdd:TIGR00957 1375 --SLRMNLDPFS----QYSDEEVwwalelAHLKTFVSALPDKLD---HEcaeggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 189 DEAVSALDVA----IQAQIlnllkRLQRErDLTYIFISHDLGVIQKFCdEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:TIGR00957 1446 DEATAAVDLEtdnlIQSTI-----RTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
56-255 |
7.31e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 56 IVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLrevRRHLQIVFQDPFSalnprrrAGDQIREPLDLlgig 135
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDPVV-------LADTFLANVTL---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 136 TRSERDERVRRLLGDVGLPPQAADLfP-----------HQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQIL 204
Cdd:PRK10790 438 GRDISEEQVWQALETVQLAELARSL-PdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 456355960 205 NLLkRLQRERDlTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFAA 255
Cdd:PRK10790 517 QAL-AAVREHT-TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-256 |
9.20e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQGKPsfvhavdgISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATsgqivfgnrdiASLT--G 94
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGP--------LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-----------GSLKinG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 95 RPLREV-----RRHLQIVFQDP--FSA------LNPRRRAGD-QIREPLDLLGIgtrserDERVRRL-------LGDvgl 153
Cdd:PRK11174 411 IELRELdpeswRKHLSWVGQNPqlPHGtlrdnvLLGNPDASDeQLQQALENAWV------SEFLPLLpqgldtpIGD--- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 154 ppQAADLfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQreRDLTYIFISHDLGVIQKfCD 233
Cdd:PRK11174 482 --QAAGL-----SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQ-WD 551
|
250 260
....*....|....*....|...
gi 456355960 234 EVAVMYLGKIVEQAPAAEIFAAP 256
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-223 |
1.83e-13 |
|
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: 67.18 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 19 VNDLVVHFPAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiasltGRPLR 98
Cdd:cd03223 3 LENLSLATPDGRV--------LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 99 EvrrHLQIVFQDP-FSALNPRrragDQIREPLDllgigtrserdervrrllgdvglppqaadlfpHQFSGGQRQRLCIAR 177
Cdd:cd03223 64 E---DLLFLPQRPyLPLGTLR----EQLIYPWD--------------------------------DVLSGGEQQRLAFAR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 456355960 178 AMAPEPDLIVCDEAVSALDVAIQAQILNLLKrlqrERDLTYIFISH 223
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
41-244 |
4.65e-13 |
|
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: 66.81 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVM--RLVPATSGQIVFGNRDiasltgRPLREVRRHLQIVFQDpfsalnpr 118
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRP------LDKRSFRKIIGYVPQD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 rragDQ------IREPLDLlgigtrserdervrrllgdvglppqAADLfpHQFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:cd03213 91 ----DIlhptltVRETLMF-------------------------AAKL--RGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 456355960 193 SALDVAIQAQILNLLKRL-QRERdlTYIFISHDL-GVIQKFCDEVAVMYLGKIV 244
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLaDTGR--TIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-238 |
6.26e-13 |
|
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: 66.72 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRdIA------ 90
Cdd:cd03250 1 ISVEDASFTWDSGEQETSF----TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAyvsqep 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 ---SLTgrpLREVrrhlqIVFQDPFsalNPRR-----RAGdQIREPLDLLGIGTRSERDERvrrllGdVGLppqaadlfp 162
Cdd:cd03250 76 wiqNGT---IREN-----ILFGKPF---DEERyekviKAC-ALEPDLEILPDGDLTEIGEK-----G-INL--------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 163 hqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILN--LLKRLQRERdlTYIFISHDLGVIQKfCDEVAVM 238
Cdd:cd03250 129 ---SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVL 200
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
44-225 |
2.26e-12 |
|
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: 65.43 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREVRRHL-----------------QI 106
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvayaaqkpwllnatveeNI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 107 VFQDPFSalNPRRRA---GDQIREPLDLLGIGTRSERDERvrrllgdvGLppqaadlfphQFSGGQRQRLCIARAMAPEP 183
Cdd:cd03290 100 TFGSPFN--KQRYKAvtdACSLQPDIDLLPFGDQTEIGER--------GI----------NLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 456355960 184 DLIVCDEAVSALDVAI-----QAQILNLLKRLQRerdlTYIFISHDL 225
Cdd:cd03290 160 NIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-245 |
2.91e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNR-DIASLTgrplrevrrhlQIVFQDP--------F 112
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlRIGYLP-----------QEPPLDDdltvldtvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SALNPRRRAGDQIRE--------PLDLLGIGTRSER---------DERVRRLLGDVGLPPQAADLFPHQFSGGQRQRLCI 175
Cdd:COG0488 84 DGDAELRALEAELEEleaklaepDEDLERLAELQEEfealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVAL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 176 ARAMAPEPDLIVCDEAVSALDV-AIQ--AQILnllkrlqRERDLTYIFISHDlgviQKFCDEVAvmylGKIVE 245
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLeSIEwlEEFL-------KNYPGTVLVVSHD----RYFLDRVA----TRILE 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
163-238 |
1.67e-11 |
|
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: 61.31 E-value: 1.67e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 163 HQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRerdlTYIFISHDLGVIQKFCDEVAVM 238
Cdd:cd03221 69 EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
44-229 |
1.82e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGnrDIASLTGRPLREVRRHLQIVFQDP------------ 111
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPllfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 112 -----------------------FSALNPRRRAGDQIREPLDLLGIGTRSERDERVRR-----------------LLGDV 151
Cdd:PTZ00265 482 yslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKnyqtikdsevvdvskkvLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 152 --GLPPQAADLF---PHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLG 226
Cdd:PTZ00265 562 vsALPDKYETLVgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
...
gi 456355960 227 VIQ 229
Cdd:PTZ00265 642 TIR 644
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
15-260 |
2.03e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 15 VLLDVNDLVVHFpagrrqGKpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASL-T 93
Cdd:PRK11614 4 VMLSFDKVSAHY------GK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLREVrrhlqivfqdpfSALNPRRR---AGDQIREPLDLLGI-GTRSERDERVRRLLgdvglppqaaDLFPHQF---- 165
Cdd:PRK11614 75 AKIMREA------------VAIVPEGRrvfSRMTVEENLAMGGFfAERDQFQERIKWVY----------ELFPRLHerri 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 ------SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMY 239
Cdd:PRK11614 133 qragtmSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLE 211
|
250 260
....*....|....*....|...
gi 456355960 240 LGKIVEQAPAAEIFA--APRHPY 260
Cdd:PRK11614 212 NGHVVLEDTGDALLAneAVRSAY 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-245 |
2.52e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 9 GTGTREVLLDVNDLVvhfpaGRRQGKpsfvhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRD 88
Cdd:PRK09700 258 SNLAHETVFEVRNVT-----SRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 89 IASLTgrPLREVRRHLQIVFQDpfsalnpRRRAGD----QIREPLDLL----------GIGTRSERDER-----VRRLLG 149
Cdd:PRK09700 327 ISPRS--PLDAVKKGMAYITES-------RRDNGFfpnfSIAQNMAISrslkdggykgAMGLFHEVDEQrtaenQRELLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 150 dvgLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQ 229
Cdd:PRK09700 398 ---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEII 473
|
250
....*....|....*.
gi 456355960 230 KFCDEVAVMYLGKIVE 245
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQ 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-245 |
3.54e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLV----PATS--GQIVF-GN----RDIASltgrplREvRRHLQI 106
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKST----LMKVLsgvyPHGSyeGEILFdGEvcrfKDIRD------SE-ALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 107 VFQDpfSAL-------------NPRRRAGdqirepldllgIGTRSERDERVRRLLGDVGL--PPQA--ADLfphqfsG-G 168
Cdd:NF040905 83 IHQE--LALipylsiaeniflgNERAKRG-----------VIDWNETNRRARELLAKVGLdeSPDTlvTDI------GvG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
43-245 |
6.01e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQaVMRLVPA---TSGQIVFGNRDIASLTGrplrEVRRHLQI--VFQDPFS---- 113
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSK-VIAGHPAykiLEGDILFKGESILDLEP----EERAHLGIflAFQYPIEipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 --------ALNPRRRA-GDQIREPLDLLGIgtrserderVRRLLGDVGLPPQaadlFPHQ-----FSGGQRQRLCIARAM 179
Cdd:CHL00131 100 snadflrlAYNSKRKFqGLPELDPLEFLEI---------INEKLKLVGMDPS----FLSRnvnegFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 180 APEPDLIVCDEAVSALDV-AIQ--AQILNLLKRLQRerdlTYIFISHD---LGVIQKfcDEVAVMYLGKIVE 245
Cdd:CHL00131 167 LLDSELAILDETDSGLDIdALKiiAEGINKLMTSEN----SIILITHYqrlLDYIKP--DYVHVMQNGKIIK 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-243 |
7.61e-11 |
|
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: 62.92 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 12 TREVLLDVNDLVVHFPAGRRQGKpsfvhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP-ATSGQIVFGNRDIA 90
Cdd:TIGR02633 253 IGDVILEARNLTCWDVINPHRKR------VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 SLTgrPLREVRRHLQIVFQDpfsalnpRRRAGdqirePLDLLGIG------------TRSERDER-----VRRLLGDVGL 153
Cdd:TIGR02633 327 IRN--PAQAIRAGIAMVPED-------RKRHG-----IVPILGVGknitlsvlksfcFKMRIDAAaelqiIGSAIQRLKV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 154 PPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCD 233
Cdd:TIGR02633 393 KTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSD 471
|
250
....*....|
gi 456355960 234 EVAVMYLGKI 243
Cdd:TIGR02633 472 RVLVIGEGKL 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
39-245 |
1.07e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.37 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGqivfgnrdiasltgrplrEVRRHLQIVFQDPFSALNPR 118
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG------------------KVDRNGEVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLGIgTRSERDErvrrllgdvgLPPQAADL-----FPHQ----FSGGQRQRLCIARAMAPEPDLIVCD 189
Cdd:PRK13546 100 LTGIENIEFKMLCMGF-KRKEIKA----------MTPKIIEFselgeFIYQpvkkYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 190 EAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-252 |
1.18e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 30 RRQGKPSFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrDI---ASLTGRPlrevrrhlqi 106
Cdd:PRK13545 29 FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIkgsAALIAIS---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 107 vfqdpfSALNPRRRAGDQIREPLDLLGIgTRSERDERVRRLL--GDVGLppqaadlFPHQ----FSGGQRQRLCIARAMA 180
Cdd:PRK13545 94 ------SGLNGQLTGIENIELKGLMMGL-TKEKIKEIIPEIIefADIGK-------FIYQpvktYSSGMKSRLGFAISVH 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:PRK13545 160 INPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
38-244 |
1.68e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrPLREVRRHLQIVFQ-----DPF 112
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD--HKLAAQLGIGIIYQelsviDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SALN-------PRRR---------AGDQIREPLDLLGIGTRSERDERVRRLlgdvglppqaadlfphqfSGGQRQRLCIA 176
Cdd:PRK09700 96 TVLEnlyigrhLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANL------------------SISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 456355960 177 RAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDlTYIFISHDLGVIQKFCDEVAVMYLGKIV 244
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-223 |
5.11e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 25 HFPAGRRQGKpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLREvrrhl 104
Cdd:COG2401 33 AFGVELRVVE---RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLID----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 105 QIVFQDPFSAlnprrragdqirepldllgigtrserderVRRLLGDVGLppQAADLF---PHQFSGGQRQRLCIARAMAP 181
Cdd:COG2401 105 AIGRKGDFKD-----------------------------AVELLNAVGL--SDAVLWlrrFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 456355960 182 EPDLIVCDEAVSALDVAiQAQILNL-LKRLQRERDLTYIFISH 223
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-237 |
6.44e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 54 FGIVGESGSGKSTTaqavmrlVPATSGQIVFGNRDIASLTgrpLREVRRHLQIVFQDP--FSAL---NPRRRAGDQIREp 128
Cdd:PTZ00265 1258 FSLTKEGGSGEDST-------VFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPmlFNMSiyeNIKFGKEDATRE- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 129 lDLLGIGTRSERDERVRRLLG--DVGLPPQAADLfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNL 206
Cdd:PTZ00265 1327 -DVKRACKFAAIDEFIESLPNkyDTNVGPYGKSL-----SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
170 180 190
....*....|....*....|....*....|.
gi 456355960 207 LKRLQRERDLTYIFISHDLGVIQKfCDEVAV 237
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
38-243 |
6.75e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.87 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDgisFRVCRGTTFGIVGESGSGKSTTAQAVMRLV-----PATSGQIVFGNRDIASLTGRPLREVRRHLQIVFQDpF 112
Cdd:PRK09984 20 LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSHIELLGRTVQREGRLARDIRKSRANTGYIFQQ-F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 SALNPRrragdQIREPLDLLGIGT-----------RSERDERVRRLLGDVGLPPqaadlFPHQ----FSGGQRQRLCIAR 177
Cdd:PRK09984 96 NLVNRL-----SVLENVLIGALGStpfwrtcfswfTREQKQRALQALTRVGMVH-----FAHQrvstLSGGQQQRVAIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 178 AMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
44-235 |
1.15e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVfgnrdiasltgrplREVRRHLQIVFQ----DPFSALNPRR 119
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRIGYVPQklylDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 ----RAGDQIREPLDLLgigtrserdERVrrllgdvglppQAADL--FPHQ-FSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:PRK09544 89 flrlRPGTKKEDILPAL---------KRV-----------QAGHLidAPMQkLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 456355960 193 SALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEV 235
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
47-230 |
1.19e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 47 RVCrgttfgIVGESGSGKSTTAQAVMRLVPATSGQIVFgNRD--IASLTGRPLREV--------------------RRH- 103
Cdd:PRK11147 31 RVC------LVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDliVARLQQDPPRNVegtvydfvaegieeqaeylkRYHd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 104 -LQIVFQDPfSALNPRRRAgdQIREPLDLLGIGtrsERDERVRRLLGDVGLPPQA--ADLfphqfSGGQRQRLCIARAMA 180
Cdd:PRK11147 104 iSHLVETDP-SEKNLNELA--KLQEQLDHHNLW---QLENRINEVLAQLGLDPDAalSSL-----SGGWLRKAALGRALV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQILNLLKRLQRerdlTYIFISHDLGVIQK 230
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRN 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-230 |
2.52e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 50 RGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNrdiasltgrplrevrrhlqivfqdpfsalnprrraGDQIREPL 129
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------------------------------GEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 130 DLLGIGTRSERDervrrllgdvglppqaadlfPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQIL----- 204
Cdd:smart00382 46 LDQLLLIIVGGK--------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180
....*....|....*....|....*.
gi 456355960 205 NLLKRLQRERDLTYIFISHDLGVIQK 230
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
51-210 |
3.05e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 51 GTTFGIVGESGSGKSTTAQAVMRLVPAtsGQIVFGNRdiaSLTGRPL--REVRRHLQIVFQDP-------------FSAl 115
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSV---LLNGMPIdaKEMRAISAYVQQDDlfiptltvrehlmFQA- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 npRRRAGDQIrepldllgigTRSERDERVRRLLGDVGLPPqAADLF---PHQ---FSGGQRQRLCIARAMAPEPDLIVCD 189
Cdd:TIGR00955 125 --HLRMPRRV----------TKKEKRERVDEVLQALGLRK-CANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180
....*....|....*....|.
gi 456355960 190 EAVSALDVAIQAQILNLLKRL 210
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGL 212
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
39-243 |
3.50e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.79 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 39 HAV-DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVpATSGQIVFgnrDIASLTGRPLREVRRHLQIVFQDPFSALNP 117
Cdd:cd03289 17 NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQI---DGVSWNSVPLQKWRKAFGVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 rrragdqIREPLDLLGigtrSERDERVRRLLGDVGLpPQAADLFPHQ-----------FSGGQRQRLCIARAMAPEPDLI 186
Cdd:cd03289 93 -------FRKNLDPYG----KWSDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 187 VCDEAVSALDVAIQAQILNLLKrlQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKI 243
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-207 |
4.16e-09 |
|
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: 55.44 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLRevrrhlQIVFQDPFSALNPRRRAg 122
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLGHLPGLKPELSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 dqiREPLDLLGIGTRSErDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQ 202
Cdd:TIGR01189 91 ---LENLHFWAAIHGGA-QRTIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
....*
gi 456355960 203 ILNLL 207
Cdd:TIGR01189 166 LAGLL 170
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
43-245 |
4.28e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQ--AVMRLVPATSGQIVFGNRDIASLTgrPLREVRRHLQIVFQDPF-------- 112
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSAtlAGREDYEVTGGTVEFKGKDLLELS--PEDRAGEGIFMAFQYPVeipgvsnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 ----SALNPRRRAGDQirEPLDLLGIGTRSErdERVRRLlgdvGLPpqaADLFPHQ----FSGGQRQRLCIARAMAPEPD 184
Cdd:PRK09580 97 fflqTALNAVRSYRGQ--EPLDRFDFQDLME--EKIALL----KMP---EDLLTRSvnvgFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 456355960 185 LIVCDEAVSALDV---AIQAQILNLLKRLQRerdlTYIFISHD---LGVIQKfcDEVAVMYLGKIVE 245
Cdd:PRK09580 166 LCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYqriLDYIKP--DYVHVLYQGRIVK 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-245 |
5.67e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLRevrrhlqivFQDPFSALNp 117
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI--------LIDGQEMR---------FASTTAALA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 rrrAGDQI-------------REPLDL------LGIGTRSERDERVRRLLGDVGLppqaaDLFPHQ----FSGGQRQRLC 174
Cdd:PRK11288 79 ---AGVAIiyqelhlvpemtvAENLYLgqlphkGGIVNRRLLNYEAREQLEHLGV-----DIDPDTplkyLSIGQRQMVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 456355960 175 IARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVE 245
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-243 |
7.94e-09 |
|
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: 57.33 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 19 VNDLVVHF-PAGRRqgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASltgrPL 97
Cdd:TIGR01257 931 VKNLVKIFePSGRP--------AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 98 REVRRHLQIVFQDpfSALNPRRRAGDQIREPLDLLGiGTRSERDERVRRLLGDVGL----PPQAADLfphqfSGGQRQRL 173
Cdd:TIGR01257 999 DAVRQSLGMCPQH--NILFHHLTVAEHILFYAQLKG-RSWEEAQLEMEAMLEDTGLhhkrNEEAQDL-----SGGMQRKL 1070
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 174 CIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-209 |
1.28e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 28 AGRRQGKPSFVhavdGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLREVRRHLQIV 107
Cdd:PRK13539 9 ACVRGGRVLFS----GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI--------KLDGGDIDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 108 FQDPFSALNPRRRAGDQIREPLDLLGigtrsERDERVRRLLGDVGLPPqAADLFPHQFSGGQRQRLCIARAMAPEPDLIV 187
Cdd:PRK13539 77 YLGHRNAMKPALTVAENLEFWAAFLG-----GEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|..
gi 456355960 188 CDEAVSALDVAIQAQILNLLKR 209
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRA 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-257 |
2.05e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.17 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPAtSGQIVFGNRDIASLTGRPLREVRRHL--QI--VFQDP-FSALNPR 118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLsqQQtpPFAMPvFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RRAGDQIREPLDLLgigtrserDERVRRLlgdvglppQAADLFP---HQFSGGQRQR-------LCIARAMAPEPDLIVC 188
Cdd:PRK03695 94 QPDKTRTEAVASAL--------NEVAEAL--------GLDDKLGrsvNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 189 DEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFAAPR 257
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-254 |
2.25e-08 |
|
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: 55.72 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 32 QGKPSFVHavdGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNR-----DIASLTGRPLREvrrhlQI 106
Cdd:TIGR00957 648 RDLPPTLN---GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpQQAWIQNDSLRE-----NI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 107 VFQDPfsaLNPRRRagDQIREP------LDLLGIGTRSErdervrrlLGDVGLppqaadlfphQFSGGQRQRLCIARAMA 180
Cdd:TIGR00957 720 LFGKA---LNEKYY--QQVLEAcallpdLEILPSGDRTE--------IGEKGV----------NLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 456355960 181 PEPDLIVCDEAVSALDVAIQAQIL-NLLKRLQRERDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
36-255 |
2.26e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 36 SFVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrPLREVRRHLQIVFQDP--FS 113
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQLGIYLVPQEPllFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 114 ALNprrragdqIREPLdLLGIGTRSERDERVRRLLGDVG----LPPQAADLfphqfSGGQRQRLCIARAMAPEPDLIVCD 189
Cdd:PRK15439 100 NLS--------VKENI-LFGLPKRQASMQKMKQLLAALGcqldLDSSAGSL-----EVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 190 EAVSALdvaIQAQILNLLKRLQ--RERDLTYIFISHDLGVIQKFCDEVAVMYLGKIV-----EQAPAAEIFAA 255
Cdd:PRK15439 166 EPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAlsgktADLSTDDIIQA 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-243 |
2.32e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAGRRQGKpsfvhaVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP-ATSGQIVFGNRDIAsl 92
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHIKR------VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVK-- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 93 TGRPLREVRRHLQIVFQDpfsalnpRRRAGdqIrepLDLLGIG---TRSERDERVRRLLGDVGLPPQAADLF-------- 161
Cdd:PRK13549 329 IRNPQQAIAQGIAMVPED-------RKRDG--I---VPVMGVGkniTLAALDRFTGGSRIDDAAELKTILESiqrlkvkt 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 162 PHQF------SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEV 235
Cdd:PRK13549 397 ASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRV 475
|
....*...
gi 456355960 236 AVMYLGKI 243
Cdd:PRK13549 476 LVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
45-254 |
2.73e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 45 SFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTgrplrevRRHLQIVFQDPFsalnpRRRAGDQ 124
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-------FEQLQKLVSDEW-----QRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 125 IREPLDLLGIGTR------SERDERVRRLLGDVGLppqaADLFPHQF---SGGQRQRLCIARAMAPEPDLIVCDEAVSAL 195
Cdd:PRK10938 91 LSPGEDDTGRTTAeiiqdeVKDPARCEQLAQQFGI----TALLDRRFkylSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 196 DVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEIFA 254
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-241 |
4.24e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 11 GTREVLLDVNDLVVHFPAgrrQGKPsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIa 90
Cdd:TIGR01257 1932 GNKTDILRLNELTKVYSG---TSSP----AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI- 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 91 sLTGrpLREVRRHLQIVFQdpFSALNPRRRAgdqiREPLDLLG--IGTRSERDERVRRL-LGDVGLpPQAADLFPHQFSG 167
Cdd:TIGR01257 2004 -LTN--ISDVHQNMGYCPQ--FDAIDDLLTG----REHLYLYArlRGVPAEEIEKVANWsIQSLGL-SLYADRLAGTYSG 2073
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 168 GQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLG 241
Cdd:TIGR01257 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-252 |
4.36e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 14 EVLLDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT 93
Cdd:PRK10762 2 QALLQLKGIDKAFPG---------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 94 GRPLREVrrHLQIVFQDpfsaLN--PRRRAGDQI---REPLDLLGIGTRSERDERVRRLLGDVGLPPQAADLFpHQFSGG 168
Cdd:PRK10762 73 PKSSQEA--GIGIIHQE----LNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLV-GELSIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE 224
|
....
gi 456355960 249 AAEI 252
Cdd:PRK10762 225 VADL 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
41-210 |
7.24e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATS--GQIVFGNRdiasltgRPLREVRRHLQIVFQDPFsaLNPR 118
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR-------KPTKQILKRTGFVTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 119 RragdQIREPL---DLLGIGTRSERDERVR---RLLGDVGLPPQAADLFPHQF----SGGQRQRLCIARAMAPEPDLIVC 188
Cdd:PLN03211 155 L----TVRETLvfcSLLRLPKSLTKQEKILvaeSVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLIL 230
|
170 180
....*....|....*....|..
gi 456355960 189 DEAVSALDVAIQAQILNLLKRL 210
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSL 252
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
43-207 |
1.18e-07 |
|
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: 51.34 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 43 GISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLREVRRHLQIVFQdpFSALNPRRRAG 122
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--------LLNGGPLDFQRDSIARGLL--YLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 DQIREPLDLLgigTRSERDERVRRLLGDVGLPpQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQ 202
Cdd:cd03231 88 LSVLENLRFW---HADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
....*
gi 456355960 203 ILNLL 207
Cdd:cd03231 164 FAEAM 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-223 |
2.08e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAGRRQgkpsfvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVpATSGQIVFGNRDIASLTgrp 96
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA-------VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVT--- 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPFSALNPRRRAGDQIREpldllgigtrsERDERVRRLLGDVGLpPQAADLFPHQ-----------F 165
Cdd:TIGR01271 1287 LQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQ-----------WSDEEIWKVAEEVGL-KSVIEQFPDKldfvlvdggyvL 1354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDvAIQAQIL-NLLKrlQRERDLTYIFISH 223
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIrKTLK--QSFSNCTVILSEH 1410
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-246 |
4.63e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLT------GRPLREvrrhlQIVFQDPFsalNP 117
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPqvswifNATVRD-----NILFGSPF---DP 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RR--RAGD--QIREPLDLLGIGTRSERDERvrrllgdvGLppqaadlfphQFSGGQRQRLCIARAMAPEPDLIVCDEAVS 193
Cdd:PLN03130 708 ERyeRAIDvtALQHDLDLLPGGDLTEIGER--------GV----------NISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 456355960 194 ALDVAIQAQILNllKRLQRE-RDLTYIFISHDLGVIQKfCDEVAVMYLGKIVEQ 246
Cdd:PLN03130 770 ALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQ-VDRIILVHEGMIKEE 820
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
38-229 |
4.82e-07 |
|
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: 49.24 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMrlvpATSGQivfgNRDIASLTGRPlrevrrHLQIVFQDPFSALnp 117
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGK----ARLISFLPKFS------RNKLIFIDQLQFL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 rrragdqirepldlLGIGtrserdervrrlLGDVGLPPQAADLfphqfSGGQRQRLCIARAMA--PEPDLIVCDEAVSAL 195
Cdd:cd03238 72 --------------IDVG------------LGYLTLGQKLSTL-----SGGELQRVKLASELFsePPGTLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 456355960 196 DVAIQAQILNLLKRLqreRDL--TYIFISHDLGVIQ 229
Cdd:cd03238 121 HQQDINQLLEVIKGL---IDLgnTVILIEHNLDVLS 153
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-252 |
7.16e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRPLRE-----VRRHLQIVFQdpf 112
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEngismVHQELNLVLQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 salnprRRAGDQI---REPLDLLGIG-------TRSERDErvrrLLGDVGLPPQAADLfphqfSGGQRQRLCIARAMAPE 182
Cdd:PRK10982 88 ------RSVMDNMwlgRYPTKGMFVDqdkmyrdTKAIFDE----LDIDIDPRAKVATL-----SVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 183 PDLIVCDEAVSALDVAIQAQILNLLKRLqRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-224 |
8.72e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 24 VHFpagrRQGKPSFvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFgnrDIASLTGRPLREVRRH 103
Cdd:PRK10522 328 VTF----AYQDNGF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 104 LQIVFQD--PFS-ALNPRRRAGD--QIREPLDLLGIGTR-SERDERVRRLlgdvglppqaadlfphQFSGGQRQRLCIAR 177
Cdd:PRK10522 399 FSAVFTDfhLFDqLLGPEGKPANpaLVEKWLERLKMAHKlELEDGRISNL----------------KLSKGQKKRLALLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 456355960 178 AMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHD 224
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-237 |
8.75e-07 |
|
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: 49.33 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 36 SFVHAVDGISFRvcRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASltgRPlREVRRHLQIVFQDPFSAL 115
Cdd:cd03237 12 EFTLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY---KP-QYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 NPRRRAGDQ----IREPLDLLGIgtrseRDERVRRLlgdvglppqaadlfphqfSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:cd03237 86 TKDFYTHPYfkteIAKPLQIEQI-----LDREVPEL------------------SGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAV 237
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
17-252 |
1.06e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPAgrrqgkpsfVHAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQ-----IVFGNRDIAS 91
Cdd:NF000106 14 VEVRGLVKHFGE---------VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRpwrf*TWCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 92 LT---GRPLREVRRhlqivfqDPFSAlnprRRAGDQIREPLDLLGIGTRSERDERVRRLLgdvglPPQAADLFPHQFSGG 168
Cdd:NF000106 85 RTig*HRPVR*GRR-------ESFSG----RENLYMIGR*LDLSRKDARARADELLERFS-----LTEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 169 QRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAP 248
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
....
gi 456355960 249 AAEI 252
Cdd:NF000106 228 VDEL 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
44-251 |
2.62e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGR--------------------PLREVRRH 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagimlcpedrkaegiiPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 104 LQIVFQDPFSA----LNPRRRAgDQIREPLDLLGIGTRSeRDERVRRLlgdvglppqaadlfphqfSGGQRQRLCIARAM 179
Cdd:PRK11288 352 INISARRHHLRagclINNRWEA-ENADRFIRSLNIKTPS-REQLIMNL------------------SGGNQQKAILGRWL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 456355960 180 APEPDLIVCDEAVSALDVAIQAQILNLLKRLQrERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAE 251
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-251 |
3.48e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIASLTGRP--------LREVRRH----LQIVF 108
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 109 QDPFS--ALNPRRRAGDQIREP---------LDLLGIGTRSeRDERVRRLlgdvglppqaadlfphqfSGGQRQRLCIAR 177
Cdd:PRK10762 348 KENMSltALRYFSRAGGSLKHAdeqqavsdfIRLFNIKTPS-MEQAIGLL------------------SGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 456355960 178 AMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAE 251
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
41-252 |
6.04e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVP---ATSGQIVFGnrDIAsLTGRPLREVrrhlqivfqdPFSALNP 117
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTG--DVT-LNGEPLAAI----------DAPRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RRRAGDQIREP--------LDLLGIGTRSERDERVRRLLGDV---GLPPQAADLFPHQ----FSGGQRQRLCIARAMA-- 180
Cdd:PRK13547 84 LRAVLPQAAQPafafsareIVLLGRYPHARRAGALTHRDGEIawqALALAGATALVGRdvttLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 456355960 181 -------PEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDEVAVMYLGKIVEQAPAAEI 252
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
166-228 |
7.20e-06 |
|
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: 47.47 E-value: 7.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVI 228
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
166-228 |
1.16e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVI 228
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-254 |
1.71e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 38 VHAVDGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLVPAT----SGQI-VFGNrDIASltgrplrevRRHlqivfqdpf 112
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAGArkiqQGRVeVLGG-DMAD---------ARH--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 113 salnpRRRAGDQI-----------------REPLD----LLGIGtRSERDERVRRLLGDVGLPP----QAADLfphqfSG 167
Cdd:NF033858 71 -----RRAVCPRIaympqglgknlyptlsvFENLDffgrLFGQD-AAERRRRIDELLRATGLAPfadrPAGKL-----SG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 168 GQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDltyifishDLGVI---------QKFcDEVAVM 238
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERP--------GMSVLvataymeeaERF-DWLVAM 210
|
250
....*....|....*.
gi 456355960 239 YLGKIVEQAPAAEIFA 254
Cdd:NF033858 211 DAGRVLATGTPAELLA 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-253 |
1.94e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVM-RLVPATSGQIVFGNR-----DIASLTGRPLREvrrhlQIVFQDPFSalnP 117
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLgELSHAETSSVVIRGSvayvpQVSWIFNATVRE-----NILFGSDFE---S 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 118 RR--RAGD--QIREPLDLLGIGTRSERDERvrrllgdvGLppqaadlfphQFSGGQRQRLCIARAMAPEPDLIVCDEAVS 193
Cdd:PLN03232 708 ERywRAIDvtALQHDLDLLPGRDLTEIGER--------GV----------NISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 194 ALDVAIQAQILNLLKRlQRERDLTYIFISHDLGVIQKFcDEVAVMYLGKIVEQAPAAEIF 253
Cdd:PLN03232 770 ALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
42-207 |
2.06e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.79 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIvfgnrdiaSLTGRPLREVRRHLQivfQDPF-----SALN 116
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV--------LWQGEPIRRQRDEYH---QDLLylghqPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 117 PRRRAgdqiREPLDLLGIGTRSERDERVRRLLGDVGLPPQAaDLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK13538 87 TELTA----LENLRFYQRLHGPGDDEALWEALAQVGLAGFE-DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170
....*....|.
gi 456355960 197 VAIQAQILNLL 207
Cdd:PRK13538 162 KQGVARLEALL 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
41-224 |
2.24e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNrdiasltgrplrevrrHLQIVFQDPFSA-LNPRR 119
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT----------------KLEVAYFDQHRAeLDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 120 RAGDQIREPLDLLGIGTRSerdervRRLLG---DVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAVSALD 196
Cdd:PRK11147 399 TVMDNLAEGKQEVMVNGRP------RHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180
....*....|....*....|....*...
gi 456355960 197 VaiqaQILNLLKRLQRERDLTYIFISHD 224
Cdd:PRK11147 473 V----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-223 |
2.92e-05 |
|
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: 45.90 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 41 VDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPatsgqiVFGnrdiasltGRPLREVRRHLQIVFQDPFSALNPRRr 120
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP------VYG--------GRLTKPAKGKLFYVPQRPYMTLGTLR- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 121 agDQIREPLDLLGIGTRSERDERVRRLLGDVGLPP--------QAADLFPHQFSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:TIGR00954 533 --DQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 456355960 193 SALDVAIQAQILNLLKRLqrerDLTYIFISH 223
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
165-244 |
3.49e-05 |
|
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: 44.18 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIF-ISHDLGVIQKFCDEVAVMYLGKI 243
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
.
gi 456355960 244 V 244
Cdd:cd03233 199 I 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-223 |
4.61e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 42 DGISFRVCRGTTFGIVGESGSGKSTtaqaVMRLVPATSGQ------IVFGNRdiaSLTGRPLREVRRHLQIVFqdpfSAL 115
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKST----LLSLITGDHPQgysndlTLFGRR---RGSGETIWDIKKHIGYVS----SSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 116 NPRRRAGDQIREPLdLLG----IGTRSERDERVRRL----LGDVGLPPQAADLFPHQFSGGQRQRLCIARAMAPEPDLIV 187
Cdd:PRK10938 346 HLDYRVSTSVRNVI-LSGffdsIGIYQAVSDRQQKLaqqwLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190
....*....|....*....|....*....|....*.
gi 456355960 188 CDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISH 223
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-239 |
6.17e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 155 PQAADLfphqfSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLTYIFISHDLGVIQKFCDE 234
Cdd:cd03222 67 PQYIDL-----SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDR 141
|
....*
gi 456355960 235 VAVMY 239
Cdd:cd03222 142 IHVFE 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
50-239 |
7.46e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 50 RGTTFGIVGESGSGKSTTAQAVmrlvpatSGQIV--FGNRDIASLTGRPLREVRRHlqiVFQDPFSAL-NPRRRAG---- 122
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDYEEEPSWDEVLKRFRGT---ELQNYFKKLyNGEIKVVhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 --DQIREPL-----DLL-GIGTRSERDERVRRLlgdvGLPP---QAADlfphQFSGGQRQRLCIARAMAPEPDLIVCDEA 191
Cdd:PRK13409 168 yvDLIPKVFkgkvrELLkKVDERGKLDEVVERL----GLENildRDIS----ELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 456355960 192 VSALDVAIQAQILNLLKRLQRERdlTYIFISHDLGVIQKFCDEVAVMY 239
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
44-203 |
1.58e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.92 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 44 ISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRdiasltgrplrevrrhlqIVFQDPFSALNPrrragD 123
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------------ISFSSQFSWIMP-----G 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 124 QIREPLdLLGIgtrSERDERVRRLLGDVGLPPQAADlFPHQ-----------FSGGQRQRLCIARAMAPEPDLIVCDEAV 192
Cdd:cd03291 113 TIKENI-IFGV---SYDEYRYKSVVKACQLEEDITK-FPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|.
gi 456355960 193 SALDVAIQAQI 203
Cdd:cd03291 188 GYLDVFTEKEI 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
50-239 |
1.86e-04 |
|
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: 43.23 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 50 RGTTFGIVGESGSGKSTTAQAVmrlvpatSGQIV--FGNRDiasltgRPL--REVRRHLQ-IVFQDPFSAL-NPRRRAG- 122
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIL-------SGELKpnLGDYD------EEPswDEVLKRFRgTELQDYFKKLaNGEIKVAh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 123 -----DQIREPLDllgiGTRSE----RDER--VRRLLGDVGLPP----QAADLfphqfSGGQRQRLCIARAMAPEPDLIV 187
Cdd:COG1245 165 kpqyvDLIPKVFK----GTVREllekVDERgkLDELAEKLGLENildrDISEL-----SGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 456355960 188 CDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMY 239
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
164-239 |
2.34e-04 |
|
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: 41.97 E-value: 2.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRErDLTYIFISHDLGVIQKFCDEVAVMY 239
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
166-249 |
4.24e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQRERDLT-YIFI---SHDlgvIQKFCDEVAVMYLG 241
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTpLVAIyqcSQD---AYELFDKVIVLYEG 287
|
....*...
gi 456355960 242 KIVEQAPA 249
Cdd:TIGR00956 288 YQIYFGPA 295
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
164-197 |
1.05e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|....
gi 456355960 164 QFSGGQRQRLCIARAMAPEPDLIVCDEAVSALDV 197
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
166-247 |
1.19e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 166 SGGQRQRLCIARAMAPEPDLIVCDEAVSALDVAIQAQILNLLKRLQReRDLTYIFISHDLGVIQKFCDEVAVMYLGK--- 242
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLvag 471
|
....*
gi 456355960 243 IVEQA 247
Cdd:PRK10982 472 IVDTK 476
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
17-224 |
1.33e-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: 40.55 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 17 LDVNDLVVHFPagRRQGKPSFvhAVDGISFRVCRGTTFGIVGESGSGKSTTAQAVMRLVPATSGQIVFGNRDIaslTGRP 96
Cdd:COG4615 328 LELRGVTYRYP--GEDGDEGF--TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 97 LREVRRHLQIVFQDPF---SALNPRRRAGD-QIREPLDLLGIGTR-SERDERVRRLlgdvglppqaadlfphQFSGGQRQ 171
Cdd:COG4615 401 REAYRQLFSAVFSDFHlfdRLLGLDGEADPaRARELLERLELDHKvSVEDGRFSTT----------------DLSQGQRK 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 456355960 172 RLCIARAMAPEPDLIVCDE-AvsaldvAIQ---------AQILNLLKRlqreRDLTYIFISHD 224
Cdd:COG4615 465 RLALLVALLEDRPILVFDEwA------ADQdpefrrvfyTELLPELKA----RGKTVIAISHD 517
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
165-224 |
8.82e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.84 E-value: 8.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 456355960 165 FSGGQRQRLCIARAMAPEPDLIVCDEAVSALDvaIQAQIlnLLKRLQRERDLTYIFISHD 224
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI--WLEKWLKSYQGTLILISHD 205
|
|
| |
