|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-529 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 1048.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHGSSLLH 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQLSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 241 AAALLNAPQHPYTQRLLDSEPAGDPVPLQRDSAPLLNVEGLSVSFPIRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGE 320
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 321 SGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQ 400
Cdd:PRK15134 321 SGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 401 RENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYI 480
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502863011 481 FISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSAD 529
Cdd:PRK15134 481 FISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-528 |
0e+00 |
|
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: 953.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPvSYPQGDILFHGSSLLH 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPA-AHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQLSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 241 AAALLNAPQHPYTQRLLDSEPAGDPVPLQRDSAPLLNVEGLSVSFPIRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGE 320
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 321 SGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQ 400
Cdd:COG4172 321 SGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 401 RENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYI 480
Cdd:COG4172 401 RRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502863011 481 FISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:COG4172 481 FISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-528 |
0e+00 |
|
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: 615.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSkqGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvSYPQGDILFHGSSLLHAD 82
Cdd:COG1123 2 TPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG--GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQtlrgVRGNKIAMIFQEPMVSLNPLhTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGER 162
Cdd:COG1123 78 EA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAA 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 243 ALLNAPQHPYTQRLLDSePAGDPVPLQRDSAPLLNVEGLSVSFPIRKGILRRVVDqnavlkNIRFSLRPGESLGLVGESG 322
Cdd:COG1123 229 EILAAPQALAAVPRLGA-ARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVD------DVSLTLRRGETLGLVGESG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 323 SGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQpTLTALQR 401
Cdd:COG1123 302 SGKSTLARLLLGLLrPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHG-LLSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 402 ENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIF 481
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 502863011 482 ISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAA 507
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-528 |
6.65e-159 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 466.25 E-value: 6.65e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHGSS--LL 79
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HADEQT---LRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQ 156
Cdd:PRK10261 89 ELSEQSaaqMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 237 EQNTAAALLNAPQHPYTQRLLDSEP-----AGDPVPLQ---------------------RDSAPLLNVEGLSVSFPIRKG 290
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPqlgamKGLDYPRRfplislehpakqeppieqdtvVDGEPILQVRNLVTRFPLRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 291 ILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWNRRQMLPVRPRMQVVFQ 369
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSLNPRLSILQIIEEGLRVHQptltALQRENEVRRV---MAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVHG----LLPGKAAAARVawlLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 447 IILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLL 526
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
..
gi 502863011 527 SA 528
Cdd:PRK10261 565 AA 566
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-265 |
5.28e-132 |
|
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: 386.33 E-value: 5.28e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSypQGDILFHGSSLLHADEQ 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQLSGGERQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAAL 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 502863011 245 LNAPQHPYTQRLLDSEPAGDP 265
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
271-528 |
1.03e-118 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 352.88 E-value: 1.03e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFPIRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPL 349
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGG 429
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHG-LASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250
....*....|....*....
gi 502863011 510 CQRVFTAPTQSYTRQLLSA 528
Cdd:COG4608 242 RDELYARPLHPYTQALLSA 260
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-528 |
6.23e-108 |
|
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: 324.70 E-value: 6.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKGILRrVVDqnavlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA----SQGEILFDGMPLH 350
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-AVD------GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMLPVRPR-MQVVFQDPNSSLNPRLSILQIIEEGLRVHQPtLTALQRENEVRRVMAEVGL-DPETR-HRYPAEFS 427
Cdd:COG0444 74 KLSEKELRKIRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLpDPERRlDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260
....*....|....*....|.
gi 502863011 508 GECQRVFTAPTQSYTRQLLSA 528
Cdd:COG0444 233 GPVEELFENPRHPYTRALLSS 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-508 |
1.57e-104 |
|
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: 312.52 E-value: 1.57e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVK-------ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 RRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 434 IAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-239 |
1.15e-102 |
|
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: 307.90 E-value: 1.15e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQ 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK--PTS---GSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRgVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILdCLDRTGIRNAAKRLSDFPHQLSGGERQR 164
Cdd:cd03257 76 LRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-528 |
5.00e-98 |
|
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: 296.71 E-value: 5.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKST----LLRALAglerpWSGEVTFDGRPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRQMlpvRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHqptlTALQRENEVRRVMAEVGLDPETRHRYPAEFSGG 429
Cdd:COG1124 70 TRRRRKAF---RRRVQMVFQDPYASLHPRHTVDRILAEPLRIH----GLPDREERIAELLEQVGLPPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 502863011 510 CQRVFTAPTQSYTRQLLSA 528
Cdd:COG1124 223 VADLLAGPKHPYTRELLAA 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-265 |
1.28e-94 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 297.20 E-value: 1.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAF-SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR--PTS---GSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HADEQTLRGVRGnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRnaAKRLSDFPHQLSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|....*.
gi 502863011 240 TAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-261 |
3.76e-90 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 279.69 E-value: 3.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSypQGDILFHGSSLLH 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI--GGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQLSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|.
gi 502863011 241 AAALLNAPQHPYTQRLLDSEP 261
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVP 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-265 |
1.51e-86 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 270.06 E-value: 1.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQG-----ETRTV--VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILF 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PTS---GEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 74 HGSSLLHADEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIR-NAAKRlsd 152
Cdd:COG4608 78 DGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADR--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQN 232
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270
....*....|....*....|....*....|...
gi 502863011 233 GRCVEQNTAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVPVPDP 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-262 |
1.16e-84 |
|
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: 262.43 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsyP-QGDILFHGSSLLHADE 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER------PwSGEVTFDGRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGvrgnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAargEILDCLDRTGIRNAAkrLSDFPHQLSGGERQ 163
Cdd:COG1124 75 KAFRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPSF--LDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAA 243
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
250
....*....|....*....
gi 502863011 244 LLNAPQHPYTQRLLDSEPA 262
Cdd:COG1124 226 LLAGPKHPYTRELLAASLA 244
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
274-528 |
9.68e-83 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 258.23 E-value: 9.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKGILRRVvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQ--QFEAVKPVSFTLEAGQTLAIIGENGSGKST----LAKMLAgiiepTSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRWNRRQmlpvRP---RMqvVFQDPNSSLNPRLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLDPETRHRYPAE 425
Cdd:COG4167 77 LEYGDYKY----RCkhiRM--IFQDPNTSLNPRLNIGQILEEPLRLNT-DLTAEEREERIFATLRLVGLLPEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 502863011 506 EQGECQRVFTAPTQSYTRQLLSA 528
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIES 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-264 |
2.44e-82 |
|
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: 265.78 E-value: 2.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAF-------SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSppvsypQGDILFHGS 76
Cdd:COG4172 274 PLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS------EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 77 SLLHADEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-GMRKEAARGEILDCLDRTGI-RNAAKRlsdFP 154
Cdd:COG4172 348 DLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHR---YP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|
gi 502863011 235 CVEQNTAAALLNAPQHPYTQRLLDSEPAGD 264
Cdd:COG4172 504 VVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
271-528 |
8.75e-80 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 252.70 E-value: 8.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFPIRKG---------ILRRVvdqnavlKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQG 340
Cdd:PRK15079 4 GKKVLLEVADLKVHFDIKDGkqwfwqppkTLKAV-------DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 341 EILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAEVGLDPETRH 420
Cdd:PRK15079 77 EVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 236
|
250 260
....*....|....*....|....*...
gi 502863011 501 QGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK15079 237 LGHAVELGTYDEVYHNPLHPYTKALMSA 264
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
271-528 |
1.81e-79 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 251.81 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFPIRKGILRrvvdQNAVLK---NIRFSLRPGESLGLVGESGSGKSTTGlALLRLI--ASQGEILFD 345
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFK----PERLVKaldGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIetPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLDPETRHRYPAE 425
Cdd:PRK11308 76 GQDLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINT-SLSAAERREKALAMMAKVGLRPEHYDRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
250 260
....*....|....*....|...
gi 502863011 506 EQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK11308 235 EKGTKEQIFNNPRHPYTQALLSA 257
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-261 |
1.19e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 249.66 E-value: 1.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSP-PVSYPQgdILFHGSSLLHADE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgRVMAEK--LEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQLSGGERQ 163
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAA 243
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*...
gi 502863011 244 LLNAPQHPYTQRLLDSEP 261
Cdd:PRK11022 241 IFRAPRHPYTQALLRALP 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-265 |
5.36e-68 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 222.15 E-value: 5.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFS-KQG---ETRTV--VSDLSLQIQRGETLALVGESGSGKSvsALSILHLLPSPPVSypqGDILFH 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvKRGlfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKS--TLARLLTMIETPTG---GELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 75 GSSLLHADEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIR-NAAKRlsdF 153
Cdd:PRK11308 76 GQDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDR---Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNG 233
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLG 231
|
250 260 270
....*....|....*....|....*....|..
gi 502863011 234 RCVEQNTAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:PRK11308 232 RCVEKGTKEQIFNNPRHPYTQALLSATPRLNP 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
269-528 |
3.44e-65 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 214.97 E-value: 3.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 269 QRDSAPLLNVEGLSVSFPIRKGILRRVVDQNavlknirFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEI----LF 344
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTPDGDVTAVNDLN-------FSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 345 DGMPLHRWNRRQMLPVRP-RMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQRENEVRrvMAEVGLDPETRHR-- 421
Cdd:PRK09473 79 NGREILNLPEKELNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVR--MLDAVKMPEARKRmk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 422 -YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:PRK09473 157 mYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250 260
....*....|....*....|....*...
gi 502863011 501 QGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-261 |
4.51e-63 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 209.38 E-value: 4.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAF-SKQGETRtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLL-PSPPVSypqGDIL-FHGSSLLH 80
Cdd:COG4170 2 PLLDIRNLTIEIdTPQGRVK-AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkDNWHVT---ADRFrWNGIDLLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVL--SLHRGM---RKEAARGEILDCLDRTGIRNAAKRLSDFPH 155
Cdd:COG4170 78 LSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpsWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250 260
....*....|....*....|....*.
gi 502863011 236 VEQNTAAALLNAPQHPYTQRLLDSEP 261
Cdd:COG4170 238 VESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-265 |
3.11e-62 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 207.25 E-value: 3.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQG---------ETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILF 73
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-----DGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 74 HGSSLLHADEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVL-SLHRGMRKEAARGEILDCLDRTGIR-NAAKRls 151
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLpNLINR-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 dFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQ 231
Cdd:PRK15079 158 -YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 236
|
250 260 270
....*....|....*....|....*....|....
gi 502863011 232 NGRCVEQNTAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:PRK15079 237 LGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDP 270
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-259 |
4.94e-61 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 201.47 E-value: 4.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAfskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsPPVSYPQGDILFHGSSLLHADeqt 85
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGVRQTAGRVLLDGKPVAPCA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 lrgVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLsLHRGmrKEAARGEILDCLDRTGIRNAAKRLSDFPHQLSGGERQRV 165
Cdd:PRK10418 76 ---LRGRKIATIMQNPRSAFNPLHTMHTHARETC-LALG--KPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALL 245
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....
gi 502863011 246 NAPQHPYTQRLLDS 259
Cdd:PRK10418 230 NAPKHAVTRSLVSA 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-528 |
2.36e-60 |
|
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: 200.03 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFpiRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 RRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRvHQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 434 IAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250
....*....|....*
gi 502863011 514 FTApTQSYTRQLLSA 528
Cdd:TIGR02769 239 LSF-KHPAGRNLQSA 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
274-528 |
6.59e-60 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 198.76 E-value: 6.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpiRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRW 352
Cdd:PRK10419 2 TLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRvHQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQ 432
Cdd:PRK10419 80 NRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 433 RIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ---GE 509
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGD 238
|
250
....*....|....*....
gi 502863011 510 CQRvFTAPTqsyTRQLLSA 528
Cdd:PRK10419 239 KLT-FSSPA---GRVLQNA 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-259 |
5.32e-58 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 193.52 E-value: 5.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIA-------FSKQgeTRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGS 76
Cdd:COG4167 3 ALLEVRNLSKTfkyrtglFRRQ--QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIE--PTS---GEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 77 SLLHADEQTlrgvRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRnaAKRLSDFPHQ 156
Cdd:COG4167 76 KLEYGDYKY----RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLL--PEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 502863011 237 EQNTAAALLNAPQHPYTQRLLDS 259
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIES 252
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
3-259 |
3.95e-57 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 191.18 E-value: 3.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSiLHLLPSppvsypQGDILFHGS---- 76
Cdd:COG4107 6 QPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKStlLKCLY-FDLAPT------SGSVYYRDRdggp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 77 -SLLHADEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLsLHRGMRK-EAARGEILDCLDRTGIrnAAKRLSDFP 154
Cdd:COG4107 79 rDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERL-MAAGERHyGDIRARALEWLERVEI--PLERIDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250 260
....*....|....*....|....*
gi 502863011 235 CVEQNTAAALLNAPQHPYTQRLLDS 259
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYTQLLVSS 260
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
271-508 |
7.16e-57 |
|
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: 189.81 E-value: 7.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFD 345
Cdd:COG1127 1 MSEPMIEVRNLTKSF-----------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSV----LLKLIIgllrpDSGEILVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRWNRRQMLPVRPRMQVVFQDP---NSslnprLSILQIIEEGLRVHqPTLTALQRENEVRRVMAEVGLdPETRHRY 422
Cdd:COG1127 66 GQDITGLSEKELYELRRRIGMLFQGGalfDS-----LTVFENVAFPLREH-TDLSEAEIRELVLEKLELVGL-PGAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
....*.
gi 502863011 503 EVVEQG 508
Cdd:COG1127 219 KIIAEG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
275-528 |
8.37e-57 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 190.77 E-value: 8.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKGILRRvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 ---RRQmlpvrpRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQ 430
Cdd:PRK15112 82 ysyRSQ------RIRMIFQDPSTSLNPRQRISQILDFPLRLNT-DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*...
gi 502863011 511 QRVFTAPTQSYTRQLLSA 528
Cdd:PRK15112 235 ADVLASPLHELTKRLIAG 252
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
276-517 |
5.70e-54 |
|
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: 181.76 E-value: 5.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKST----LLRLLNgllkpTSGEVLVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQmlpVRPRMQVVFQDPNSslnprlsilQIIEE--------GLRVHQptLTALQRENEVRRVMAEVGLDpETRHRY 422
Cdd:COG1122 67 KKNLRE---LRRKVGLVFQNPDD---------QLFAPtveedvafGPENLG--LPREEIRERVEEALELVGLE-HLADRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDG 210
|
250
....*....|....*
gi 502863011 503 EVVEQGECQRVFTAP 517
Cdd:COG1122 211 RIVADGTPREVFSDY 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-507 |
2.48e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 177.54 E-value: 2.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSFPIRKGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGM 347
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVT-------ALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 348 PLHRWNRRQMLPVRpRMQV--VFQDPNssLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAE 425
Cdd:COG1136 71 DISSLSERELARLR-RRHIgfVFQFFN--LLPELTALENVALPLLLAG--VSRKERRERARELLERVGLG-DRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVV 505
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
..
gi 502863011 506 EQ 507
Cdd:COG1136 224 SD 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-528 |
4.10e-52 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 180.32 E-value: 4.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKGILRRVvdqnavlKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIL-----FDGMPL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAV-------DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekleFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWN---RRQMlpVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQRENEVRrVMAEVGL-DPETR-HRYPA 424
Cdd:PRK11022 76 QRISekeRRNL--VGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAID-LLNQVGIpDPASRlDVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
250 260
....*....|....*....|....
gi 502863011 505 VEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK11022 233 VETGKAHDIFRAPRHPYTQALLRA 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-505 |
1.87e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 182.91 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFskqGETRtVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSypqGDILFHGSsll 79
Cdd:COG1129 1 AEPLLEMRGISKSF---GGVK-ALDGVSLELRPGEVHALLGENGAGKStlMKILSGVY----QPDS---GEILLDGE--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 hadEQTLRGVR---GNKIAMIFQEpmvsLNPLHTL----------EKQLYEVLSlHRGMRKEAARgeildCLDRTGIR-N 145
Cdd:COG1129 67 ---PVRFRSPRdaqAAGIAIIHQE----LNLVPNLsvaeniflgrEPRRGGLID-WRAMRRRARE-----LLARLGLDiD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 146 AAKRLSDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLAD 225
Cdd:COG1129 134 PDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIAD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 226 SVAVMQNGRCVEQNTAAALlnapqhpyTQR----------LLDSEPAGDPVPlqrdSAPLLNVEGLSVsfpirkgilrrv 295
Cdd:COG1129 209 RVTVLRDGRLVGTGPVAEL--------TEDelvrlmvgreLEDLFPKRAAAP----GEVVLEVEGLSV------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 296 vdqNAVLKNIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEILFDGMplhrwnrrqmlPVRPRmqvvfqd 370
Cdd:COG1129 265 ---GGVVRDVSFSVRAGEILGIAGLVGAGRT----ELARALfgadpADSGEIRLDGK-----------PVRIR------- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 pnsslNPRLSILQII--------EEGLRVHQP-----TLTAL-----------QRENE-VRRVMAEVGLDPETRHRYPAE 425
Cdd:COG1129 320 -----SPRDAIRAGIayvpedrkGEGLVLDLSireniTLASLdrlsrgglldrRRERAlAEEYIKRLRIKTPSPEQPVGN 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
278-527 |
2.01e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 178.73 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFPIRKGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRW 352
Cdd:COG1135 4 LENLSKTFPTKGGPVT-------ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInllerPTSGSVLVDGVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQMLPVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQ 432
Cdd:COG1135 73 SERELRAARRKIGMIFQHFN--LLSSRTVAENVALPLEIAG--VPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 433 RIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQR 512
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
250
....*....|....*
gi 502863011 513 VFTAPTQSYTRQLLS 527
Cdd:COG1135 228 VFANPQSELTRRFLP 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
278-524 |
2.57e-51 |
|
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: 175.00 E-value: 2.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEILFDGMPLHRW 352
Cdd:cd03261 3 LRGLTKSF-----------GGRTVLKGVDLDVRRGEILAIIGPSGSGKST----LLRLIVGLlrpdsGEVLIDGEDISGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQMLPVRPRMQVVFQDpnSSLNPRLSILQIIEEGLRVHqptlTALQrENEVRRV----MAEVGLdPETRHRYPAEFSG 428
Cdd:cd03261 68 SEAELYRLRRRMGMLFQS--GALFDSLTVFENVAFPLREH----TRLS-EEEIREIvlekLEAVGL-RGAEDLYPAELSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03261 140 GMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
250
....*....|....*.
gi 502863011 509 ECQRVFTApTQSYTRQ 524
Cdd:cd03261 220 TPEELRAS-DDPLVRQ 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
1.09e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 172.92 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSS 77
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS----TLLNILggldrPT------SGEVLIDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 LLHADEQTLRGVRGNKIAMIFQEPmvslnplhtlekQLYEVLS---------LHRGMRKEAARGEILDCLDRTGIrnaAK 148
Cdd:COG1136 72 ISSLSERELARLRRRHIGFVFQFF------------NLLPELTalenvalplLLAGVSRKERRERARELLERVGL---GD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 149 RLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIvKKLADSVA 228
Cdd:COG1136 137 RLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVI 215
|
250
....*....|
gi 502863011 229 VMQNGRCVEQ 238
Cdd:COG1136 216 RLRDGRIVSD 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-267 |
1.29e-50 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 176.15 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlPSPPVSYPQGDILFHGSSLLHADE 83
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVL--SLHRGM-------RKEAArgeiLDCLDRTGIRNAAKRLSDFP 154
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGRwwqrfgwRKRRA----IELLHRVGIKDHKDAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260 270
....*....|....*....|....*....|....
gi 502863011 235 CVEQNTAAALLNAPQHPYTQRLLDSEPA-GDPVP 267
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALIRAIPDfGSAMP 270
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-265 |
2.79e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.65 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLL--PSppvsypQGDILFHGSSLLHADE 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLLerPT------SGSVLVDGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRGnKIAMIFQepmvSLNPLHT----------LEkqlyevlslHRGMRKEAARGEILDCLDRTGIRNAAKRlsdF 153
Cdd:COG1135 75 RELRAARR-KIGMIFQ----HFNLLSSrtvaenvalpLE---------IAGVPKAEIRKRVAELLELVGLSDKADA---Y 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNG 233
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENG 217
|
250 260 270
....*....|....*....|....*....|..
gi 502863011 234 RCVEQNTAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:COG1135 218 RIVEQGPVLDVFANPQSELTRRFLPTVLNDEL 249
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-517 |
3.14e-50 |
|
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: 172.00 E-value: 3.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKGILrrvvdqnAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPL 349
Cdd:cd03258 1 MIELKNVSKVFGDTGGKV-------TALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCInglerPTSGSVLVDGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRQMLPVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGG 429
Cdd:cd03258 70 TLLSGKELRKARRRIGMIFQHFN--LLSSRTVFENVALPLEIAG--VPKAEIEERVLELLELVGLE-DKADAYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
....*...
gi 502863011 510 CQRVFTAP 517
Cdd:cd03258 225 VEEVFANP 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-518 |
4.04e-50 |
|
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: 172.54 E-value: 4.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG1120 1 MLEAENLSVGY-----------GGRPVLDDVSLSLPPGEVTALLGPNGSGKST----LLRALAgllkpSSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRQmlpVRPRMQVVFQDPNSSLNprLSILQIIEEGLRVHQPTLTALQRENE--VRRVMAEVGLDpETRHRYPAEFS 427
Cdd:COG1120 66 ASLSRRE---LARRIAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSAEDReaVEEALERTGLE-HLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
250
....*....|.
gi 502863011 508 GECQRVFTAPT 518
Cdd:COG1120 220 GPPEEVLTPEL 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
276-504 |
5.19e-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: 168.44 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPIRKGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQ-------ALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVRVDGTDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMLPVRPR-MQVVFQDPNssLNPRLSILQIIEEGLRVHQPTLTalQRENEVRRVMAEVGLDpETRHRYPAEFSGG 429
Cdd:cd03255 70 KLSEKELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLAGVPKK--ERRERAEELLERVGLG-DRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRaLCHQVIVLRQGEV 504
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-513 |
1.20e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.31 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNglvepTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRWNRRQMLPVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQPTLTAL---QRENEVRRVMA---EVGLDPETRHRy 422
Cdd:COG3638 67 VTALRGRALRRLRRRIGMIFQQFN--LVPRLSVLTNVLAGRLGRTSTWRSLlglFPPEDRERALEaleRVGLADKAYQR- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
250
....*....|.
gi 502863011 503 EVVEQGECQRV 513
Cdd:COG3638 224 RVVFDGPPAEL 234
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-257 |
1.81e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 167.85 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpsPPVSypqGDILFHGSSLLH 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL--RPDS---GEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRgNKIAMIFQEPMV--SLNPLHTLEKQLYEvlslHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLS 158
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGALfdSLTVFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---MPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VTVqAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250 260
....*....|....*....|
gi 502863011 238 QNTAAALLNAPqHPYTQRLL 257
Cdd:COG1127 223 EGTPEELLASD-DPWVRQFL 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-513 |
3.87e-48 |
|
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: 174.61 E-value: 3.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVsalsILHLLPS----PPVSypqGDILFH------- 74
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVLRGmdqyEPTS---GRIIYHvalcekc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 75 ----------------GSSL-------LHADEQTLRGVRgNKIAMIFQ-------EPMVSLNPLHTLEKQLYEvlslhrg 124
Cdd:TIGR03269 70 gyverpskvgepcpvcGGTLepeevdfWNLSDKLRRRIR-KRIAIMLQrtfalygDDTVLDNVLEALEEIGYE------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 125 mrKEAARGEILDCLDRTgirNAAKRLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRS 204
Cdd:TIGR03269 142 --GKEAVGRAVDLIEMV---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 205 ELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNApqhpYTQRLldSEPAGDPVPLQRDsaPLLNVEGLSVS 284
Cdd:TIGR03269 217 ASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV----FMEGV--SEVEKECEVEVGE--PIIKVRNVSKR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 285 F-PIRKGILRRVvdqnavlKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILF-------DGMPLHRWNRR 355
Cdd:TIGR03269 289 YiSVDRGVVKAV-------DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVrvgdewvDMTKPGPDGRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 356 QmlpVRPRMQVVFQDpnSSLNPRLSILQIIEEGLRVHQPTLTALQRENEVRRVmaeVGLDPETR----HRYPAEFSGGQR 431
Cdd:TIGR03269 362 R---AKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKM---VGFDEEKAeeilDKYPDELSEGER 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 432 QRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*.
gi 502863011 508 GECQRV 513
Cdd:TIGR03269 510 GDPEEI 515
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
278-503 |
6.19e-48 |
|
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: 165.33 E-value: 6.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFPirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRW 352
Cdd:cd03225 2 LKNLSFSYP---------DGARPALDDISLTIKKGEFVLIVGPNGSGKST----LLRLLNgllgpTSGEVLVDGKDLTKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQmlpVRPRMQVVFQDPNSSL-NPRlsilqIIEE---GLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSG 428
Cdd:cd03225 69 SLKE---LRRKVGLVFQNPDDQFfGPT-----VEEEvafGLENLG--LPEEEIEERVEEALELVGLE-GLRDRSPFTLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
272-506 |
6.30e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 166.80 E-value: 6.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFPIRKGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVT-------ALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIAglekpTSGEVLVDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRwnrrqmlpVRPRMQVVFQDPnsSLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEF 426
Cdd:COG1116 73 KPVTG--------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGLA-GFEDAYPHQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 427 SGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLLkglqEKHRLAYIFISHDLQ--VvrALCHQVIVL- 499
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLW----QETGKTVLFVTHDVDeaV--FLADRVVVLs 213
|
....*...
gi 502863011 500 -RQGEVVE 506
Cdd:COG1116 214 aRPGRIVE 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-265 |
1.83e-47 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 174.66 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGE-----TRTV--VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHG 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-----GGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 76 SSLLHADEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIR-NAAKRlsdFP 154
Cdd:PRK10261 386 QRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWR---YP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
250 260 270
....*....|....*....|....*....|.
gi 502863011 235 CVEQNTAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:PRK10261 542 IVEIGPRRAVFENPQHPYTRKLMAAVPVADP 572
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-527 |
2.90e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 164.40 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINlleepDSGTITVDGEDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRwNRRQMLPVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLdPETRHRYPAEFSGG 429
Cdd:COG1126 66 TD-SKKDINKLRRKVGMVFQQFN--LFPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLD-RTVqAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDpELV-GEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
250
....*....|....*....
gi 502863011 509 ECQRVFTAPTQSYTRQLLS 527
Cdd:COG1126 219 PPEEFFENPQHERTRAFLS 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
292-508 |
8.23e-47 |
|
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: 162.30 E-value: 8.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPR--- 363
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTT----LLRLIAglerpDSGEILIDGRDVTG------VPPERRnig 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 364 MqvVFQDPnsSLNPRLSILQIIEEGLRVHqpTLTALQRENEVRRVMAEVGLDPEtRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:cd03259 76 M--VFQDY--ALFPHLTVAENIAFGLKLR--GVPKAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 444 PELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
272-517 |
2.99e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 2.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:COG3842 2 AMPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAgfetpDSGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 mplhrwnrRQMLPVRP---RMQVVFQDPnsSLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYP 423
Cdd:COG3842 67 --------RDVTGLPPekrNVGMVFQDY--ALFPHLTVAENVAFGLRMRG--VPKAEIRARVAELLELVGLE-GLADRYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
250
....*....|....
gi 502863011 504 VVEQGECQRVFTAP 517
Cdd:COG3842 214 IEQVGTPEEIYERP 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-507 |
4.04e-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: 160.72 E-value: 4.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPIRKGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVT-------ALEDISLSVEEGEFVALVGPSGCGKST----LLRIIAglerpTSGEVLVDGEPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RwnrrqmlpVRPRMQVVFQDPnsSLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQ 430
Cdd:cd03293 70 G--------PGPDRGYVFQQD--ALLPWLTVLDNVALGLELQG--VPKAEARERAEELLELVGLS-GFENAYPHQLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL--RQGEVVEQ 507
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
5.31e-46 |
|
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: 160.35 E-value: 5.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpSPPVSypqGDILFHGSSLLHADEQT 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGL-DRPTS---GEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEpmvslnplHTLEKQL--YEVLSL---HRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGG 160
Cdd:cd03255 76 LAAFRRRHIGFVFQS--------FNLLPDLtaLENVELpllLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVkKLADSVAVMQNGR 234
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-249 |
5.42e-45 |
|
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: 158.13 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQ 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT----SGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRgNKIAMIFQ------EPMVSLNPLHTLEkqlyevlslHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLS 158
Cdd:cd03258 76 ELRKAR-RRIGMIFQhfnllsSRTVFENVALPLE---------IAGVPKAEIEERVLELLELVGLEDKADA---YPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
250
....*....|.
gi 502863011 239 NTAAALLNAPQ 249
Cdd:cd03258 223 GTVEEVFANPQ 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
271-526 |
5.99e-45 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 158.94 E-value: 5.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFPIRKGilrrvvdqnavLKNIRFSLRPGESLGLVGESGSGKSTTgLALL--RLIASQGEILFDG-- 346
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG-----------CRDVSFDLYPGEVLGIVGESGSGKTTL-LNALsaRLAPDAGEVHYRMrd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 ---MPLHRWN--RRQMLpVRPRMQVVFQDPNSSLNPRLSilqiieEGLRVHQPTLTALQRE-NEVRRV----MAEVGLDP 416
Cdd:PRK11701 70 gqlRDLYALSeaERRRL-LRTEWGFVHQHPRDGLRMQVS------AGGNIGERLMAVGARHyGDIRATagdwLERVEIDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 417 ETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:PRK11701 143 ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRL 222
|
250 260 270
....*....|....*....|....*....|
gi 502863011 497 IVLRQGEVVEQGECQRVFTAPTQSYTrQLL 526
Cdd:PRK11701 223 LVMKQGRVVESGLTDQVLDDPQHPYT-QLL 251
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
276-508 |
8.95e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 8.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRMLLgllrpTSGEVRVLGEDVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRqmlpVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQ 430
Cdd:COG1131 66 RDPAE----VRRRIGYVPQEPA--LYPDLTVRENLRFFARLYG--LPRKEARERIDELLELFGLT-DAADRKVGTLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFIS-HDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT--VLLStHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-247 |
2.09e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.76 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL--HLLPSppvsypQGDILFHGSSLLHADE 83
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIRMLlgLLRPT------SGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRgvrgnKIAMIFQEPmvSLNPLHTLEKQLYEVLSLHrGMRKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQ 163
Cdd:COG1131 70 EVRR-----RIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVG---TLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAA 243
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
....
gi 502863011 244 LLNA 247
Cdd:COG1131 218 LKAR 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
1.72e-43 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 155.08 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSiLHLLPSppvsypQGDILFHG--- 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTtlLNALS-ARLAPD------AGEVHYRMrdg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 76 --SSLLHADEQTLRGVRGNKIAMIFQEPMVSLNPLHT----LEKQLYEVLSLHRGMRKEAArgeiLDCLDRTGIrnAAKR 149
Cdd:PRK11701 71 qlRDLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSaggnIGERLMAVGARHYGDIRATA----GDWLERVEI--DAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 150 LSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAV 229
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|
gi 502863011 230 MQNGRCVEQNTAAALLNAPQHPYTQRLLDS 259
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
297-508 |
4.90e-43 |
|
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: 163.08 E-value: 4.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP 371
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKST----LLKLLLglyepTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 ---NSSlnprlsilqiIEEGLRVHQPTLTalqrENEVRRVMAEVGLDPETRHRyP-----------AEFSGGQRQRIAIA 437
Cdd:COG2274 559 flfSGT----------IRENITLGDPDAT----DEEIIEAARLAGLHDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 438 RALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGEVVEQG 508
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-252 |
7.45e-43 |
|
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: 152.66 E-value: 7.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQT 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--PDS---GEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRgNKIAMIFQEPMV--SLNPLHTLEKQLYEvlslHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQ 163
Cdd:cd03261 72 LYRLR-RRMGMLFQSGALfdSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAA 243
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 502863011 244 LLNApQHPY 252
Cdd:cd03261 224 LRAS-DDPL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-505 |
8.31e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.42 E-value: 8.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSkqgetrTVV--SDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSypqGDILFHGS 76
Cdd:COG3845 1 MMPPALELRGITKRFG------GVVanDDVSLTVRPGEIHALLGENGAGKStlMKILYGLY----QPDS---GEILIDGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 77 sllhadEQTLRG---VRGNKIAMIFQEPMvslnplhtlekqLYEVLS----LHRGMrkEAARGEILDcldRTGIRNAAKR 149
Cdd:COG3845 68 ------PVRIRSprdAIALGIGMVHQHFM------------LVPNLTvaenIVLGL--EPTKGGRLD---RKAARARIRE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 150 LSD---FP-------HQLSGGERQRVMIAMALLTRPELLIADEPTTALdvTVQ--AQILQLLRELRSElNMSLLFITHNL 217
Cdd:COG3845 125 LSErygLDvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 218 SIVKKLADSVAVMQNGRCV-EQNTAAAllnapqhpyTQRLLdsepA----GDPVPLQRD------SAPLLNVEGLSVsfP 286
Cdd:COG3845 202 REVMAIADRVTVLRRGKVVgTVDTAET---------SEEEL----AelmvGREVLLRVEkapaepGEVVLEVENLSV--R 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 287 IRKGILRrvvdqnavLKNIRFSLRPGESLGLVGESGSGKSttglALLRLIA-----SQGEILFDGMPLHRWNRRQMLpvr 361
Cdd:COG3845 267 DDRGVPA--------LKDVSLEVRAGEILGIAGVAGNGQS----ELAEALAglrppASGSIRLDGEDITGLSPRERR--- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 362 pRMQVVF--QDPNSS-LNPRLS-----ILQIIEEGLRVHQPTLTALQRENEVRRVMAE---VGLDPETRHRypaEFSGGQ 430
Cdd:COG3845 332 -RLGVAYipEDRLGRgLVPDMSvaenlILGRYRRPPFSRGGFLDRKAIRAFAEELIEEfdvRTPGPDTPAR---SLSGGN 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
297-509 |
1.59e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 151.36 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDP 371
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NssLNPRLSILQIIEEGLRVHQPTLTALQREneVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:COG2884 89 R--LLPDRTVYENVALPLRVTGKSRKEIRRR--VREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 452 PTSSLDRTVQAQILTLLKGLqekHRL--AYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEI---NRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
271-518 |
2.52e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFD 345
Cdd:COG1121 2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKAILgllppTSGTVRLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRWNRR-----QMLPVRPRMqvvfqdpnsslnPrLSILQIIEEGLRVHQPTLTALQRE--NEVRRVMAEVGLDpET 418
Cdd:COG1121 67 GKPPRRARRRigyvpQRAEVDWDF------------P-ITVRDVVLMGRYGRRGLFRRPSRAdrEAVDEALERVGLE-DL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 419 RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:COG1121 133 ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLL 211
|
250 260
....*....|....*....|
gi 502863011 499 LRQGeVVEQGECQRVFTAPT 518
Cdd:COG1121 212 LNRG-LVAHGPPEEVLTPEN 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
3.28e-42 |
|
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: 150.56 E-value: 3.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQT 85
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK--PTS---GEVLVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRgvrgNKIAMIFQEPmvslnplhtlEKQLYE--VLS------LHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQL 157
Cdd:COG1122 73 LR----RKVGLVFQNP----------DDQLFAptVEEdvafgpENLGLPREEIRERVEEALELVGLEHLADR---PPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|..
gi 502863011 238 QNTAAALLNAPQ 249
Cdd:COG1122 215 DGTPREVFSDYE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
292-504 |
3.34e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.97 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNrrqmlPVRPRMQV 366
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKST----LLRALAdldppTSGEIYLDGKPLSAMP-----PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 367 --VFQDPnsslnprlsilQIIEEGLRVH--QPTLTALQR--ENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARAL 440
Cdd:COG4619 77 ayVPQEP-----------ALWGGTVRDNlpFPFQLRERKfdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 441 ILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
271-506 |
4.26e-42 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 150.28 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFPIRKGILrrvvdqnAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFD 345
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGEL-------TILKGISLEVEAGESVAIVGASGSGKST----LLGLLAgldrpTSGTVRLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRWNRRQMLPVRPR-MQVVFQDpnsslnprlsiLQIIeeglrvhqPTLTALqrEN---------------EVRRVM 409
Cdd:COG4181 73 GQDLFALDEDARARLRARhVGFVFQS-----------FQLL--------PTLTAL--ENvmlplelagrrdaraRARALL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 410 AEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVV 489
Cdd:COG4181 132 ERVGLGHRLDH-YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
250
....*....|....*..
gi 502863011 490 rALCHQVIVLRQGEVVE 506
Cdd:COG4181 211 -ARCDRVLRLRAGRLVE 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
275-509 |
5.53e-42 |
|
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: 150.39 E-value: 5.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTT----LLRMLAgllkpDSGSILIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRqmlpVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGG 429
Cdd:COG4555 66 RKEPRE----ARRQIGVLPDERG--LYDRLTVRENIRYFAELYG--LFDEELKKRIEELIELLGLE-EFLDRRVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-294 |
7.07e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.03 E-value: 7.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 8 IDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTLR 87
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPT----SGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 88 GVRgNKIAMIFQEpmvsLNPLHTleKQLYEVLSLH---RGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQR 164
Cdd:PRK11153 79 KAR-RQIGMIFQH----FNLLSS--RTVFDNVALPlelAGTPKAEIKARVTELLELVGLSDKADR---YPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAAL 244
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 245 LNAPQHPYTQRLLDS-EPAGDPVPLQR--------DSAPLLNVE--GLSVSFPIRKGILRR 294
Cdd:PRK11153 229 FSHPKHPLTREFIQStLHLDLPEDYLArlqaepttGSGPLLRLEftGESVDAPLLSETARR 289
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-257 |
7.15e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.14 E-value: 7.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLlHADEQ 84
Cdd:COG1126 1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLEEPD----SGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRGnKIAMIFQE----P-M-----VSLNPLHtlekqlyevlslHRGMRKEAARGEILDCLDRTGIrnaAKRLSDFP 154
Cdd:COG1126 71 DINKLRR-KVGMVFQQfnlfPhLtvlenVTLAPIK------------VKKMSKAEAEERAMELLERVGL---ADKADAYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:COG1126 135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
250 260
....*....|....*....|...
gi 502863011 235 CVEQNTAAALLNAPQHPYTQRLL 257
Cdd:COG1126 214 IVEEGPPEEFFENPQHERTRAFL 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-233 |
1.46e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.85 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQ--PLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILF 73
Cdd:COG1116 1 MSAaaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIaglekPT------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 74 HGssllhadeQTLRGvRGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRlsdF 153
Cdd:COG1116 71 DG--------KPVTG-PGPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---Y 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLS--IVkkLADSVAVMQ 231
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaVF--LADRVVVLS 213
|
..
gi 502863011 232 NG 233
Cdd:COG1116 214 AR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
298-503 |
1.59e-41 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 146.95 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwNRRQMLPVRPRMQVVFQDPN 372
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKST----LLRCIAgleepDSGSILIDGEDLTD-LEDELPPLRRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 ssLNPRLSILQIIEEGLrvhqptltalqrenevrrvmaevgldpetrhrypaefSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03229 87 --LFPHLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
292-517 |
2.55e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 151.84 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWnrrqmLPVRPRmQV 366
Cdd:COG1118 8 ISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAgletpDSGRIVLNGRDLFTN-----LPPRER-RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 367 --VFQDPnsSLNPRLSILQIIEEGLRVHQPTLTALQREneVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:COG1118 78 gfVFQHY--ALFPHMTVAENIAFGLRVRPPSKAEIRAR--VEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 445 ELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
273-528 |
5.22e-41 |
|
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: 148.05 E-value: 5.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSFPIRKGilrrvvdqnavLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILF---DGMP 348
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKG-----------CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYimrSGAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 -----LHRWNRRQMLpvRPRMQVVFQDPNSSLNPRLSILQIIEEglrvhQPTLTALQRENEVRRV----MAEVGLDPETR 419
Cdd:TIGR02323 70 lelyqLSEAERRRLM--RTEWGFVHQNPRDGLRMRVSAGANIGE-----RLMAIGARHYGNIRATaqdwLEEVEIDPTRI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:TIGR02323 143 DDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
250 260
....*....|....*....|....*....
gi 502863011 500 RQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:TIGR02323 223 QQGRVVESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
6.37e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 6.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKS--VSAlsILHLLPspPVSypqGDILFHGSSL 78
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKStlLKA--ILGLLP--PTS---GTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 lhadeqtlrGVRGNKIAMIFQEPMVSLN-PLHtlekqLYEVLSL----HRGMRK---EAARGEILDCLDRTGIRNAAKR- 149
Cdd:COG1121 71 ---------RRARRRIGYVPQRAEVDWDfPIT-----VRDVVLMgrygRRGLFRrpsRADREAVDEALERVGLEDLADRp 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 150 LSdfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAV 229
Cdd:COG1121 137 IG----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLL 211
|
250
....*....|....*....
gi 502863011 230 MqNGRCVEQNTAAALLNAP 248
Cdd:COG1121 212 L-NRGLVAHGPPEEVLTPE 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
276-513 |
1.07e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 146.94 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLH 350
Cdd:cd03256 1 IEVENLSKTYP----------NGKKALKDVSLSINPGEFVALIGPSGAGKST----LLRCLnglvePTSGSVLIDGTDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQPTLTALQR---ENEVRRVMA---EVGLDPETRHRyPA 424
Cdd:cd03256 67 KLKGKALRQLRRQIGMIFQQFN--LIERLSVLENVLSGRLGRRSTWRSLFGlfpKEEKQRALAaleRVGLLDKAYQR-AD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
....*....
gi 502863011 505 VEQGECQRV 513
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
297-524 |
1.18e-40 |
|
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: 147.79 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNRRQMLPVR-PRMQVVFQd 370
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKST----LLRCInrliePTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQ- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 pNSSLNPRLSILQIIEEGLRV-HQPtltALQRENEVRRVMAEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03294 110 -SFALLPHRTVLENVAFGLEVqGVP---RAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 450 DEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQ 524
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-247 |
2.05e-40 |
|
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: 146.34 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSypqGDILFHGSSLLHAD 82
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKStlLRALAGLL----KPSS---GEVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 eqtlRGVRGNKIAMIFQEPMVSLnPLHtlekqLYEVLSL----HRGM---RKEAARGEILDCLDRTGIRNAAKRLSDfph 155
Cdd:COG1120 70 ----RRELARRIAYVPQEPPAPF-GLT-----VRELVALgrypHLGLfgrPSAEDREAVEEALERTGLEHLADRPVD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250
....*....|..
gi 502863011 236 VEQNTAAALLNA 247
Cdd:COG1120 217 VAQGPPEEVLTP 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
2.23e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.48 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFskqGETrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHG 75
Cdd:COG3842 1 MAMPALELENVSKRY---GDV-TALDDVSLSIEPGEFVALLGPSGCGKT----TLLRMIagfetPD------SGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 76 ssllhadeQTLRGVRGNK--IAMIFQEPmvSLNPLHT--------LEkqlyevlslHRGMRKEAARGEILDCLDRTGIRN 145
Cdd:COG3842 67 --------RDVTGLPPEKrnVGMVFQDY--ALFPHLTvaenvafgLR---------MRGVPKAEIRARVAELLELVGLEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 146 AAKRlsdFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHN----LSivk 221
Cdd:COG3842 128 LADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA--- 201
|
250 260 270
....*....|....*....|....*....|.
gi 502863011 222 kLADSVAVMQNGRCVEQNTAAALLNAPQHPY 252
Cdd:COG3842 202 -LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
297-503 |
5.78e-40 |
|
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: 142.52 E-value: 5.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---N 372
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPflfS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SSLnprlsilqiieeglrvhqptltalqRENevrrvmaevgLdpetrhrypaeFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03228 90 GTI-------------------------REN----------I-----------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGE 503
Cdd:cd03228 124 TSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-506 |
9.28e-40 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 151.37 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 8 IDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpsppvsypqgdilfhgSSLLHADEQTLR 87
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKIL----------------AGELEPDSGEVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 88 GVRGNKIAMIFQEP------------MVSLNPLHTLEKQLYEVLSLHRGMRKEAAR-GEILDCLDRTG-------IRNAA 147
Cdd:COG0488 57 IPKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERlAELQEEFEALGgweaearAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 148 KRL--SDFPHQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALDV-TVQaqilqLLRELRSELNMSLLFITHNLSI 219
Cdd:COG0488 137 SGLgfPEEDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHDRYF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 220 VKKLADSVAVMQNGRCVE--------------------------QNTAAALL--------NAPQHpyTQ----------- 254
Cdd:COG0488 212 LDRVATRILELDRGKLTLypgnysayleqraerleqeaaayakqQKKIAKEEefirrfraKARKA--KQaqsrikalekl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 255 RLLDSEPAGDPVPLQRDSAP-----LLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtg 329
Cdd:COG0488 290 EREEPPRRDKTVEIRFPPPErlgkkVLELEGLSKSY-----------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKST-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 330 laLLRLIA-----SQGEIlfdgmplhRWNrrqmlpvrPRMQVVF--QDpNSSLNPRLSILQIIEEGLRvhqptltaLQRE 402
Cdd:COG0488 357 --LLKLLAgelepDSGTV--------KLG--------ETVKIGYfdQH-QEELDPDKTVLDELRDGAP--------GGTE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 403 NEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAqiltLLKGLQEkhrlaY-- 479
Cdd:COG0488 410 QEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDiETLEA----LEEALDD-----Fpg 480
|
570 580
....*....|....*....|....*....
gi 502863011 480 --IFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:COG0488 481 tvLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
271-528 |
1.08e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.56 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFD 345
Cdd:COG4598 4 TAPPALEVRDLHKSF-----------GDLEVLKGVSLTARKGDVISIIGSSGSGKST----FLRCInlletPDSGEIRVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLhRW-----------NRRQMLPVRPRMQVVFQDPNssLNPRLSILQ-IIEEGLRVH-QPTLTALQReneVRRVMAEV 412
Cdd:COG4598 69 GEEI-RLkpdrdgelvpaDRRQLQRIRTRLGMVFQSFN--LWSHMTVLEnVIEAPVHVLgRPKAEAIER---AEALLAKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 413 GLdPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRAL 492
Cdd:COG4598 143 GL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDV 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 502863011 493 CHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:COG4598 221 SSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
254-508 |
1.46e-39 |
|
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: 151.45 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSEPAGDP---VPLQRDSAPLLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGL 330
Cdd:COG4988 312 FALLDAPEPAAPagtAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 331 ALLRLI-ASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPnsslnprlSILQI-IEEGLRVHQPTLTalqrENEVRRV 408
Cdd:COG4988 382 LLLGFLpPYSGSILINGVDLSDLDPAS---WRRQIAWVPQNP--------YLFAGtIRENLRLGRPDAS----DEELEAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 409 MAEVGLDPETRhRYP-----------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRL 477
Cdd:COG4988 447 LEAAGLDEFVA-ALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV 525
|
250 260 270
....*....|....*....|....*....|.
gi 502863011 478 ayIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG4988 526 --ILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-259 |
1.52e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 144.83 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQG-----ETRTVVSDLSLQIQRGETLALVGESGSGKSVSAlSILHLLPSPPvsypQGDILFHGSSL 78
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLA-RLLVGLESPS----QGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LHADEQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRnaAKRLSDFPHQLS 158
Cdd:PRK10419 77 AKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLD--DSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260
....*....|....*....|.
gi 502863011 239 NTAAALLnAPQHPYTQRLLDS 259
Cdd:PRK10419 234 QPVGDKL-TFSSPAGRVLQNA 253
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
299-517 |
1.59e-39 |
|
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: 143.63 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 299 NAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLhrwnrRQMLPVRPRMQVVFQdpNS 373
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSV----LLETIAGfikpdSGKILLNGKDI-----TNLPPEKRDISYVPQ--NY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 SLNPRLSILQIIEEGLRVHqpTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKR--KVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 454 SSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
303-528 |
2.60e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 143.69 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 303 KNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-----ASQGEILFDGMPLHRWNrrqmlpVRPRM-QVVFQDPNSSLN 376
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAPCA------LRGRKiATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIEEGLRVhqptLTALQRENEVRRVMAEVGLDPETR--HRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK10418 94 PLHTMHTHARETCLA----LGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 455 SLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
254-508 |
2.93e-39 |
|
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: 150.69 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSEPAGDPV-----PLQRDSAPLLNVEGLSVSFPirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTT 328
Cdd:COG4987 307 RRLNELLDAPPAVtepaePAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 329 GLALLRLI-ASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsilqiIEEGLRVHQPTLTalqrENE 404
Cdd:COG4987 378 LALLLRFLdPQSGSITLGGVDLRDLDEDD---LRRRIAVVPQRPhlfDTT----------LRENLRLARPDAT----DEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 405 VRRVMAEVGLDP---------ETR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL-TLLKGLQE 473
Cdd:COG4987 441 LWAALERVGLGDwlaalpdglDTWlGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAG 520
|
250 260 270
....*....|....*....|....*....|....*
gi 502863011 474 KhrlAYIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:COG4987 521 R---TVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-243 |
4.11e-39 |
|
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: 142.19 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPpvsyPQGDILFHGSSLLH 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRP----TSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEPMVsLNPLHTLEkqlYEVLSLH-RGMRKEAARGEILdcLDRTGIrnaAKRLSDFPHQLSG 159
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSFQL-LPTLTALE---NVMLPLElAGRRDARARARAL--LERVGL---GHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQN 239
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
....
gi 502863011 240 TAAA 243
Cdd:COG4181 229 AATA 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
302-454 |
5.43e-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: 139.32 E-value: 5.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNssLN 376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKST----LLKLIAgllspTEGTILLDGQDLTDDERKS---LRKEIGYVFQDPQ--LF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIEEGLRVhqPTLTALQRENEVRRVMAEVGL--DPETR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:pfam00005 72 PRLTVRENLRLGLLL--KGLSKREKDARAEEALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 502863011 454 S 454
Cdd:pfam00005 150 A 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-508 |
6.43e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 142.05 E-value: 6.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWN 353
Cdd:TIGR02315 1 MLEVENLSKVYP----------NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 RRQMLPVRPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQPTLTALQR---ENEVRRVMA---EVGLDpETRHRYPAEFS 427
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQHYN--LIERLTVLENVLHGRLGYKPTWRSLLGrfsEEDKERALSaleRVGLA-DKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
.
gi 502863011 508 G 508
Cdd:TIGR02315 228 G 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-234 |
9.32e-39 |
|
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: 140.68 E-value: 9.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLlhaDEQTL 86
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT-----SGEVLVDGKDL---TKLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 87 RGVRGnKIAMIFQEPmvslnplhtlEKQLY------EVLS--LHRGMRKEAARGEILDCLDRTGIRNAAKRLsdfPHQLS 158
Cdd:cd03225 71 KELRR-KVGLVFQNP----------DDQFFgptveeEVAFglENLGLPEEEIEERVEEALELVGLEGLRDRS---PFTLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-509 |
1.22e-38 |
|
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: 140.78 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA----------SQGEILFD 345
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKST----LLRLLNrlndlipgapDEGEVLLD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRWNRRQMLpVRPRMQVVFQDPNsslnP-RLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLDPET-RHRYP 423
Cdd:cd03260 66 GKDIYDLDVDVLE-LRRRVGMVFQKPN----PfPGSIYDNVAYGLRLHG-IKLKEELDERVEEALRKAALWDEVkDRLHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLqeKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
....*.
gi 502863011 504 VVEQGE 509
Cdd:cd03260 218 LVEFGP 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
297-521 |
1.34e-38 |
|
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: 140.84 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPR-MQVVFQd 370
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIAgfetpTSGEILLDGKDITN------LPPHKRpVNTVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 pNSSLNPRLSILQIIEEGLRVHQPTLTALQREneVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03300 80 -NYALFPHLTVFENIAFGLRLKKLPKAEIKER--VAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 451 EPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSY 521
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
298-518 |
1.43e-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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.21 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPN 372
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTliqhlNGL----LKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SslnprlsilQIIEE-------------GLrvhqPTLTALQReneVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARA 439
Cdd:TIGR04521 93 H---------QLFEEtvykdiafgpknlGL----SEEEAEER---VKEALELVGLDEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 440 LILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
278-508 |
1.57e-38 |
|
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: 139.11 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRW 352
Cdd:cd03214 2 VENLSVGY-----------GGRTVLDDLSLSIEAGEIVGILGPNGAGKST----LLKTLAgllkpSSGEILLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQMlpvRPRMQVVFQdpnsslnprlsilqiieeglrvhqptltalqrenevrrVMAEVGLDpETRHRYPAEFSGGQRQ 432
Cdd:cd03214 67 SPKEL---ARKIAYVPQ--------------------------------------ALELLGLA-HLADRPFNELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 433 RIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-259 |
1.67e-38 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 141.85 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQG-----ETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLL 79
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE--PTS---GELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HADeqtlRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNaaKRLSDFPHQLSG 159
Cdd:PRK15112 79 FGD----YSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP--DHASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
250 260
....*....|....*....|
gi 502863011 240 TAAALLNAPQHPYTQRLLDS 259
Cdd:PRK15112 233 STADVLASPLHELTKRLIAG 252
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-244 |
1.75e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.96 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQgetRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSL 78
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKS----TLLRCLnglvePT------SGEILVDGQDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LHADEQTLRGVRGnKIAMIFQEpmvslnplHTLEKQLYeVL-----------SLHRGMRKEAARGEI---LDCLDRTGIR 144
Cdd:COG3638 68 TALRGRALRRLRR-RIGMIFQQ--------FNLVPRLS-VLtnvlagrlgrtSTWRSLLGLFPPEDReraLEALERVGLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 145 NAAKRLSDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLA 224
Cdd:COG3638 138 DKAYQRAD---QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYA 214
|
250 260
....*....|....*....|
gi 502863011 225 DSVAVMQNGRCVEQNTAAAL 244
Cdd:COG3638 215 DRIIGLRDGRVVFDGPPAEL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
302-528 |
2.13e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 143.79 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPN--SS 374
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKST----LIRCInllerPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNllSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LN--------------PRLSILQIIEEglrvhqptLTALqrenevrrvmaeVGLDpETRHRYPAEFSGGQRQRIAIARAL 440
Cdd:PRK11153 97 RTvfdnvalplelagtPKAEIKARVTE--------LLEL------------VGLS-DKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 441 ILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQS 520
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*...
gi 502863011 521 YTRQLLSA 528
Cdd:PRK11153 236 LTREFIQS 243
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-235 |
3.76e-38 |
|
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: 139.14 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLP--SPPVSypqGDILFHGssllhade 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIIAglERPTS---GEVLVDG-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVrGNKIAMIFQEPmvSLNPLHTLEKQLyeVLSL-HRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGER 162
Cdd:cd03293 66 EPVTGP-GPDRGYVFQQD--ALLPWLTVLDNV--ALGLeLQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-237 |
4.07e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 139.41 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLL 79
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS----TLLHLLggldnPT------SGEVLFNGQSLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HADEQTLRGVRGNKIAMIFQ--EPMVSLNPLHTLEKQLyevlsLHRGMRKEAARGEILDCLDRTGIRnaaKRLSDFPHQL 157
Cdd:TIGR02211 71 KLSSNERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKSVKEAKERAYEMLEKVGLE---HRINHRPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLaDSVAVMQNGRCVE 237
Cdd:TIGR02211 143 SGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-259 |
5.63e-38 |
|
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: 139.97 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGETRtvvsDLSLQIQRGETLALVGESGSGKS--VSALSIlHLLPSP-PVSYPQGDILFHgsSLL 79
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCR----DVSFDLYPGEVLGIVGESGSGKStlLGCLAG-RLAPDHgTATYIMRSGAEL--ELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HADEQTLRGVRGNKIAMIFQEPMVSL----NPLHTLEKQLYEVLSLHRGMRKEAARgeilDCLDRTGIRnaAKRLSDFPH 155
Cdd:TIGR02323 74 QLSEAERRRLMRTEWGFVHQNPRDGLrmrvSAGANIGERLMAIGARHYGNIRATAQ----DWLEEVEID--PTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....
gi 502863011 236 VEQNTAAALLNAPQHPYTQRLLDS 259
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
276-504 |
1.07e-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: 136.37 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03230 1 IEVRNLSKRYG-----------KKTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIILgllkpDSGEIKVLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRqmlpVRPRMQVVFQDPnsSLNPRLSILQIIEeglrvhqptltalqrenevrrvmaevgldpetrhrypaeFSGGQ 430
Cdd:cd03230 66 KEPEE----VKRRIGYLPEEP--SLYENLTVRENLK---------------------------------------LSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAyIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
301-529 |
1.43e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 138.59 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQdpNSSLNPRL 379
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVEL---RRKIGYVIQ--QIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SILQIIeeGLrvhQPTLTALQRENEVRRV---MAEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:cd03295 91 TVEENI--AL---VPKLLKWPKEKIRERAdelLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 456 LDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSAD 529
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
299-504 |
1.43e-37 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 137.66 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 299 NAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwNRRQMLPVRPRMQVVFQDPNs 373
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleepDSGTIIIDGLKLTD-DKKNINELRQKVGMVFQQFN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 sLNPRLSILQIIEEGLR-VHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03262 87 -LFPHLTVLENITLAPIkVKG--MSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
274-528 |
1.47e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 141.20 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKGILRrVVDqnavlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMplhRWN 353
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVK-AVD------RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRF---RWN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 RRQMLPVRPR---------MQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAE----VGL-DPETR 419
Cdd:COG4170 72 GIDLLKLSPRerrkiigreIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIEllhrVGIkDHKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 420 HR-YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:COG4170 152 MNsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
250 260 270
....*....|....*....|....*....|
gi 502863011 499 LRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:COG4170 232 LYCGQTVESGPTEQILKSPHHPYTKALLRS 261
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-237 |
2.29e-37 |
|
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: 136.88 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIaglerPD------SGEILIDGRDVTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 adeqtlRGVRGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGG 160
Cdd:cd03259 67 ------VPPERRNIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-237 |
2.50e-37 |
|
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: 137.31 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVsALSILHLL----PSPPVSypqGDILFHGSSLLHA 81
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKST-LLRLLNRLndliPGAPDE---GEVLLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGVRgnKIAMIFQEPmvslNPLHtleKQLYEVLSL---HRGMRKEAARGEI-LDCLDRTGIRNAAKRLSDfPHQL 157
Cdd:cd03260 73 DVDVLELRR--RVGMVFQKP----NPFP---GSIYDNVAYglrLHGIKLKEELDERvEEALRKAALWDEVKDRLH-ALGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
256-508 |
2.58e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.31 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 256 LLDSEP----AGDPVPLQRDSAPLlNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtgla 331
Cdd:COG1132 317 LLDEPPeipdPPGAVPLPPVRGEI-EFENVSFSYP----------GDRPVLKDISLTIPPGETVALVGPSGSGKST---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 332 LLRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsilqiIEEGLRVHQPTLTalqrEN 403
Cdd:COG1132 382 LVNLLLrfydpTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTflfSGT----------IRENIRYGRPDAT----DE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 404 EVRRVMAEVGLDPETRhRYP-----------AEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLL 468
Cdd:COG1132 445 EVEEAAKAAQAHEFIE-ALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEALERLM 523
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 502863011 469 KGlqekhRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG1132 524 KG-----RTT-IVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
278-499 |
7.47e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 135.74 E-value: 7.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRw 352
Cdd:cd03235 2 VEDLTVSY-----------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKST----LLKAILgllkpTSGSIRVFGKPLEK- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 nrrqmlpVRPRMQVVFQDPNSSLNPRLSILQIIEEGL---RVHQPTLTALQREnEVRRVMAEVGLDpETRHRYPAEFSGG 429
Cdd:cd03235 66 -------ERKRIGYVPQRRSIDRDFPISVRDVVLMGLyghKGLFRRLSKADKA-KVDEALERVGLS-ELADRQIGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAyIFISHDLQVVRALCHQVIVL 499
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTI-LVVTHDLGLVLEYFDRVLLL 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
272-508 |
1.06e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 136.71 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFpirkGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG 346
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLV-------AVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLItgfyrPTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNRRQmlpvRPRMQVV--FQdpNSSLNPRLSILQIIEEGLRVHQ---------PTLTALQRENEVR----RVMAE 411
Cdd:COG0411 66 RDITGLPPHR----IARLGIArtFQ--NPRLFPELTVLENVLVAAHARLgrgllaallRLPRARREEREAReraeELLER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 412 VGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG0411 140 VGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMG 218
|
250
....*....|....*..
gi 502863011 492 LCHQVIVLRQGEVVEQG 508
Cdd:COG0411 219 LADRIVVLDFGRVIAEG 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
304-517 |
1.09e-36 |
|
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: 139.47 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 304 NIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPV-RPRMQVVFQDPnsSLNP 377
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTT----LLRAIAglerpDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQEA--RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 378 RLSILQIIEEGLRVHQPTLTALQREnevrRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFD----EVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 458 RTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
1.52e-36 |
|
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: 133.29 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQT 85
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK--PDS---GEIKVLGKDIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRgvrgnKIAMIFQEPMvslnplhtlekqLYEVLSLHrgmrkeaargEILDcldrtgirnaakrlsdfphqLSGGERQRV 165
Cdd:cd03230 72 KR-----RIGYLPEEPS------------LYENLTVR----------ENLK--------------------LSGGMKQRL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
272-513 |
1.53e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.69 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFPirkGILrrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:COG1129 1 AEPLLEMRGISKSFG---GVK--------ALDGVSLELRPGEVHALLGENGAGKST----LMKILSgvyqpDSGEILLDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNRRQMLpvRPRMQVVFQDPNssLNPRLSILQII------EEGLRVHQPTLTAlqrenEVRRVMAEVGL--DPET 418
Cdd:COG1129 66 EPVRFRSPRDAQ--AAGIAIIHQELN--LVPNLSVAENIflgrepRRGGLIDWRAMRR-----RARELLARLGLdiDPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 419 RHRypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIV 498
Cdd:COG1129 137 PVG---DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTV 212
|
250
....*....|....*
gi 502863011 499 LRQGEVVEQGECQRV 513
Cdd:COG1129 213 LRDGRLVGTGPVAEL 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
307-528 |
1.61e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 135.27 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPV--RPrMQVVFQDPNssLNPRL 379
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKST----LLNLIAgflppDSGRILWNGQDLTA------LPPaeRP-VSMLFQENN--LFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SILQIIEEGLRvhqPT--LTALQREnEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:COG3840 87 TVAQNIGLGLR---PGlkLTAEQRA-QVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 458 RTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
301-515 |
2.45e-36 |
|
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: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMplHRWNRRQMLPVRPRMQVVFQDPNSsl 375
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTlakllNGL----LLPTSGKVTVDGL--DTLDEENLWEIRKKVGMVFQNPDN-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 nprlsilQII----EE----GLRVHQptltaLQRENEVRRV---MAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:TIGR04520 89 -------QFVgatvEDdvafGLENLG-----VPREEMRKRVdeaLKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 445 ELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFT 515
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-508 |
2.53e-36 |
|
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: 134.87 E-value: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFpirkGILRrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG---- 346
Cdd:cd03219 1 LEVRGLTKRF----GGLV-------ALDDVSFSVRPGEIHGLIGPNGAGKTT----LFNLIsgflrPTSGSVLFDGedit 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 -MPLHRWNRRQMlpVRprmqvVFQdpNSSLNPRLSILQIIEEGLRVHQPTLTALQR--------ENEVRRVMAEVGLDPE 417
Cdd:cd03219 66 gLPPHEIARLGI--GR-----TFQ--IPRLFPELTVLENVMVAAQARTGSGLLLARarreereaRERAEELLERVGLADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 418 tRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:cd03219 137 -ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVT 214
|
250
....*....|.
gi 502863011 498 VLRQGEVVEQG 508
Cdd:cd03219 215 VLDQGRVIAEG 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
292-517 |
4.13e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.51 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplHRWNRrqmLPVRPR--- 363
Cdd:COG3839 9 VSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAgledpTSGEILIGG---RDVTD---LPPKDRnia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 364 MqvVFQDPnsSLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:COG3839 79 M--VFQSY--ALYPHMTVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 444 PELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDlQV-VRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD-QVeAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-504 |
6.54e-36 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 140.06 E-value: 6.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSYpQGDILFHGSsL 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKStlMKVLSGVY----PHGTY-EGEIIFEGE-E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LHAdeQTLRGVRGNKIAMIFQEPMvslnplhtLEKQLYEVLSLHRGmrKEAARGEILD----------CLDRTGIR-NAA 147
Cdd:PRK13549 71 LQA--SNIRDTERAGIAIIHQELA--------LVKELSVLENIFLG--NEITPGGIMDydamylraqkLLAQLKLDiNPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 148 KRLSDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSV 227
Cdd:PRK13549 139 TPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 228 AVMQNGRCVEQNTAAAL-------------LNA--PQHPYTqrlldsepAGDPVplqrdsaplLNVEGLSVSFPIRKGil 292
Cdd:PRK13549 214 CVIRDGRHIGTRPAAGMteddiitmmvgreLTAlyPREPHT--------IGEVI---------LEVRNLTAWDPVNPH-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 293 RRVVDqnavlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI--ASQGEILFDGMPLHRWNRRQ-------MLPV-RP 362
Cdd:PRK13549 275 IKRVD------DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpgRWEGEIFIDGKPVKIRNPQQaiaqgiaMVPEdRK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 363 RMQVVfqdpnsslnPRLSILQIIeeglrvhqpTLTALQR------------ENEVRRVMAEVGLDPETRHRYPAEFSGGQ 430
Cdd:PRK13549 349 RDGIV---------PVMGVGKNI---------TLAALDRftggsriddaaeLKTILESIQRLKVKTASPELAIARLSGGN 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
299-527 |
9.98e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 133.72 E-value: 9.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 299 NAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI----------ASQGEILFDG-MPLhrwNRRQMLPVRPRMQVV 367
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTT----LLRCInlleqpeagtIRVGDITIDTaRSL---SQQKGLIRQLRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 368 FQDPNSSLNPRLSILQIIEEGLRV--HQPTLTALQReneVRRVMAEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEGPVIvkGEPKEEATAR---ARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 446 LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIfISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQL 525
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
..
gi 502863011 526 LS 527
Cdd:PRK11264 244 LE 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-518 |
1.11e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 133.70 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSfpirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:COG4559 1 MLEAENLSVR-----------LGGRTLLDDVSLTLRPGELTAIIGPNGAGKST----LLKLLTgeltpSSGEVRLNGRPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRQMLPVRPRMQvvfQdpNSSLNPRLSILQIIEEGLRVHQPTltALQRENEVRRVMAEVGLDPeTRHRYPAEFSGG 429
Cdd:COG4559 66 AAWSPWELARRRAVLP---Q--HSSLAFPFTVEEVVALGRAPHGSS--AAQDRQIVREALALVGLAH-LAGRSYQTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALI-------LKPELIILDEPTSSLDRTVQAQILTLLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQG 216
|
250
....*....|....*.
gi 502863011 503 EVVEQGECQRVFTAPT 518
Cdd:COG4559 217 RLVAQGTPEEVLTDEL 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-505 |
1.62e-35 |
|
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: 130.24 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKST----LMKILSglykpDSGEILVDGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMLpvRPRMQVVFQdpnsslnprlsilqiieeglrvhqptltalqrenevrrvmaevgldpetrhrypaeFSGGQ 430
Cdd:cd03216 66 FASPRDAR--RAGIAMVYQ--------------------------------------------------------LSVGE 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:cd03216 88 RQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-234 |
1.81e-35 |
|
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: 130.20 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLP---SPPvsypQGDILFHGSSLLHAD 82
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKS----TLLKLLLrlyDPT----SGEILIDGVDLRDLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRgvrgNKIAMIFQEPmvslnplhtlekQLYEvlslhrgmrkeaarGEILDCLdrtgirnaakrlsdfphqLSGGER 162
Cdd:cd03228 71 LESLR----KNIAYVPQDP------------FLFS--------------GTIRENI------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGR 234
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
2.26e-35 |
|
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: 130.25 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQTL 86
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 87 RgvrgNKIAMIFQepmvslnplhtlekqlyevlslhrgmrkeaargeildCLDRTGIRNAAKRLSDfphQLSGGERQRVM 166
Cdd:cd03214 72 A----RKIAYVPQ-------------------------------------ALELLGLAHLADRPFN---ELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 167 IAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-244 |
2.83e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.42 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppVSYPQGDILFHGSSLLHADEQ 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-----VEPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRgNKIAMIFQEPMVsLNPLHTLEKQLYEVLSLHRGMR------KEAARGEILDCLDRTGIRNAAKRLSDfphQLS 158
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQHYNL-IERLTVLENVLHGRLGYKPTWRsllgrfSEEDKERALSALERVGLADKAYQRAD---QLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
....*.
gi 502863011 239 NTAAAL 244
Cdd:TIGR02315 228 GAPSEL 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-257 |
2.85e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.80 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 29 SLQIQRGETLALVGESGSGKSvsalSILHLLPS--PPVSypqGDILFHGSSLLHadeqTLRGVRgnKIAMIFQEpmvslN 106
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIAGflPPDS---GRILWNGQDLTA----LPPAER--PVSMLFQE-----N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 107 PL--H-TLEKQLYevLSLHRGMR-KEAARGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:COG3840 81 NLfpHlTVAQNIG--LGLRPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 183 PTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQRLL 257
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-252 |
2.92e-35 |
|
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: 140.35 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRgmrKEAARGEILDCLDRTGIRNAAKRL--------SD 152
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFL-------FSGTIRENITLGD---PDATDEEIIEAARLAGLHDFIEALpmgydtvvGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVkKLADSVAVMQN 232
Cdd:COG2274 608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDK 684
|
250 260
....*....|....*....|
gi 502863011 233 GRCVEQNTAAALLNAPQHPY 252
Cdd:COG2274 685 GRIVEDGTHEELLARKGLYA 704
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
302-514 |
4.03e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.25 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLhrWNRRQMLP-VRPRMQVVFQDPNSSL 375
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTliqhlNGL----LKPTSGKIIIDGVDI--TDKKVKLSdIRKKVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRlSILQIIEEGLRvhQPTLTALQRENEVRRVMAEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK13637 97 FEE-TIEKDIAFGPI--NLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 455 SLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-255 |
6.29e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 131.29 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSL---LHADEQTLRGVRGnKIAMIFQE 100
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPD----SGQLNIAGHQFdfsQKPSEKAIRLLRQ-KVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 pmVSLNPLHTLEKQLYE----VLslhrGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:COG4161 91 --YNLWPHLTVMENLIEapckVL----GLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALlnapQHPYTQR 255
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEA 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-249 |
6.61e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 131.29 E-value: 6.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSL---LHADEQTLRGVRgNKIAMIFQEpmV 103
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPR----SGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQ--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK11124 92 NLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 184 TTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAAlLNAPQ 249
Cdd:PRK11124 169 TAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
7.63e-35 |
|
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: 128.15 E-value: 7.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 25 VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpsppvSYPQGDILFHGSSLLHADEQTLRGvrgnKIAMIFQEPmvS 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-----SPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 LNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKR-LSDFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 502863011 184 TT 185
Cdd:pfam00005 149 TA 150
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
7.86e-35 |
|
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: 129.96 E-value: 7.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHaDEQT 85
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEEPD----SGTIIIDGLKLTD-DKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRV 165
Cdd:cd03262 71 INELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
304-508 |
9.09e-35 |
|
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: 130.11 E-value: 9.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 304 NIRFSLrPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPR-MQVVFQdpNSSLNP 377
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKST----LLRCIAglekpDGGTIVLNGTVLFDSRKKINLPPQQRkIGLVFQ--QYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 378 RLSILQIIEEGLRVHQPTltalQRENEVRRVMAEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:cd03297 89 HLNVRENLAFGLKRKRNR----EDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502863011 458 RTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-237 |
9.27e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 9.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIafsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:COG2884 2 IRFENVSK---RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLygeerPT------SGQVLVNGQDLSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRgNKIAMIFQEpmvslnplHTL--EKQLYE--VLSLH-RGMRKEAARGEILDCLDRTGIRNAAKRlsdFPH 155
Cdd:COG2884 69 LKRREIPYLR-RRIGVVFQD--------FRLlpDRTVYEnvALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKA---LPH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
..
gi 502863011 236 VE 237
Cdd:COG2884 216 VR 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-244 |
1.62e-34 |
|
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: 130.00 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQT 85
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE--PTS---GSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGnKIAMIFQEPMVsLNPLHTLEKQLYEVLSLH------RGMRKEAARGEILDCLDRTGIRN-AAKRLSdfphQLS 158
Cdd:cd03256 73 LRQLRR-QIGMIFQQFNL-IERLSVLENVLSGRLGRRstwrslFGLFPKEEKQRALAALERVGLLDkAYQRAD----QLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
....*.
gi 502863011 239 NTAAAL 244
Cdd:cd03256 227 GPPAEL 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
274-518 |
1.81e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.28 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSfpirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMP 348
Cdd:PRK13548 1 AMLEARNLSVR-----------LGGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelsPDSGEVRLNGRP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRWNRRQMLPVRPRM-QvvfqdpNSSLNPRLSILQIIEEGLRVHQPTLTALQRenEVRRVMAEVGLDpETRHRYPAEFS 427
Cdd:PRK13548 66 LADWSPAELARRRAVLpQ------HSSLSFPFTVEEVVAMGRAPHGLSRAEDDA--LVAAALAQVDLA-HLAGRDYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALI------LKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250
....*....|....*..
gi 502863011 502 GEVVEQGECQRVFTAPT 518
Cdd:PRK13548 217 GRLVADGTPAEVLTPET 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
292-503 |
2.65e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 126.59 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQV 366
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKST----LLRAIAgllkpTSGEILIDGKDIAKLPLEE---LRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 367 VFQdpnsslnprlsilqiieeglrvhqptltalqrenevrrvmaevgldpetrhrypaeFSGGQRQRIAIARALILKPEL 446
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 447 IILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
301-506 |
3.89e-34 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 128.62 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPR-MQVVFQdpNSS 374
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKST----LLHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIYQ--FHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQiieeglRVHQPTLTALQRENEVRR----VMAEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:TIGR02211 94 LLPDFTALE------NVAMPLLIGKKSVKEAKErayeMLEKVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 451 EPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALcHQVIVLRQGEVVE 506
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-240 |
6.42e-34 |
|
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: 129.09 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSA--LSILhLLPSppvsypQGDILFHGSSLLhaDE 83
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAklLNGL-LLPT------SGKVTVDGLDTL--DE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRgNKIAMIFQepmvslNPlhtlEKQLyeVLSL----------HRGMRKEAARGEILDCLDRTGIRNAAKRLsdf 153
Cdd:TIGR04520 70 ENLWEIR-KKVGMVFQ------NP----DNQF--VGATveddvafgleNLGVPREEMRKRVDEALKLVGMEDFRDRE--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVkKLADSVAVMQNG 233
Cdd:TIGR04520 134 PHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKG 212
|
....*..
gi 502863011 234 RCVEQNT 240
Cdd:TIGR04520 213 KIVAEGT 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-260 |
8.79e-34 |
|
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: 128.19 E-value: 8.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQT 85
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKT-TTMKMINRLIEPT----SGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRgvrgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIrNAAKRLSDFPHQLSGGERQRV 165
Cdd:cd03295 73 LR----RKIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALL 245
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|....*
gi 502863011 246 NAPQHPYTQRLLDSE 260
Cdd:cd03295 225 RSPANDFVAEFVGAD 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
1.35e-33 |
|
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: 125.38 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVsALSILHLLPSPPvsypQGDILFHGSSLlhADEQT 85
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKST-LLRCIAGLEEPD----SGSILIDGEDL--TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEPmvslnplhtlekQLYEVLSlhrgmrkeaargeILDcldrtgirNAAkrlsdfpHQLSGGERQRV 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDF------------ALFPHLT-------------VLE--------NIA-------LGLSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
278-505 |
2.90e-33 |
|
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: 125.45 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQ 356
Cdd:cd03226 2 IENISFSYK----------KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 357 MlpvrprMQVVFQDPNSSLnprlsILQIIEEGLRVHQPTLTAlqRENEVRRVMAEVGL-DPETRHryPAEFSGGQRQRIA 435
Cdd:cd03226 72 S------IGYVMQDVDYQL-----FTDSVREELLLGLKELDA--GNEQAETVLKDLDLyALKERH--PLSLSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 436 IARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
4.90e-33 |
|
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: 132.57 E-value: 4.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFskqGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGS 76
Cdd:COG4988 333 GPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKS----TLLNLLlgflpPY------SGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 77 SLLHADEQTLRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLHRgmrKEAARGEILDCLDRTGIRNAAKRLS---DF 153
Cdd:COG4988 400 DLSDLDPASWR----RQIAWVPQNP-------YLFAGTIRENLRLGR---PDASDEELEAALEAAGLDEFVAALPdglDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 P-----HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELnmSLLFITHNLSIVkKLADSVA 228
Cdd:COG4988 466 PlgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRIL 542
|
250
....*....|....*....
gi 502863011 229 VMQNGRCVEQNTAAALLNA 247
Cdd:COG4988 543 VLDDGRIVEQGTHEELLAK 561
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
301-508 |
5.02e-33 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 125.06 E-value: 5.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGmplhrwNRRQMLPVRPR-MQVVFQdpNSS 374
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGG------RDVTDLPPKDRdIAMVFQ--NYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIEEGLRV-HQPTLTALQReneVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLrKVPKDEIDER---VREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 454 SSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-230 |
5.46e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.95 E-value: 5.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsyP-QGDILFHGSSLlhadeqt 85
Cdd:cd03235 1 EVEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK------PtSGSIRVFGKPL------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 lrGVRGNKIAMIFQEPMVSLN-PLHTLE---KQLYEVLSLHRGMRKEAARgEILDCLDRTGIRNAAKRLSDfphQLSGGE 161
Cdd:cd03235 64 --EKERKRIGYVPQRRSIDRDfPISVRDvvlMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIG---ELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVM 230
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
301-508 |
5.54e-33 |
|
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: 125.42 E-value: 5.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDP---NSSln 376
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKS---LRSMIGVVLQDTflfSGT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 prlsilqiIEEGLRVHQPTLTalqrENEVRRVMAEVGLDPETRHR------YPAE----FSGGQRQRIAIARALILKPEL 446
Cdd:cd03254 93 --------IMENIRLGRPNAT----DEEVIEAAKEAGAHDFIMKLpngydtVLGEnggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 447 IILDEPTSSLD----RTVQAQILTLLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03254 161 LILDEATSNIDteteKLIQEALEKLMKG-----RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-227 |
6.86e-33 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 124.65 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSppvsYPQGDILFHGSSLLHADEQTLRGVRGNKIA 95
Cdd:TIGR03608 5 SKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEK----FDSGQVYLNGQETPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 96 MIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAaRGEILDCLDRTGIRNaakRLSDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:TIGR03608 80 YLFQN--FALIENETVEENLDLGLKYKKLSKKEK-REKKKEALEKVGLNL---KLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502863011 176 ELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKlADSV 227
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRV 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-504 |
7.05e-33 |
|
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: 131.49 E-value: 7.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 23 TVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSYpQGDILFHGSSLlhaDEQTLRGVRGNKIAMIFQE 100
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKStlMKILSGVY----PHGTW-DGEIYWSGSPL---KASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 PMVSLNpLHTLEKQLYEVLSLHRGMRKEAA----RGEILDCLDRTGIRNAAKRLSDfphqLSGGERQRVMIAMALLTRPE 176
Cdd:TIGR02633 87 LTLVPE-LSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGD----YGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVeQNTAAALLNAPQ------H 250
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMSEDDiitmmvG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 251 PYTQRLLDSEP--AGDPVplqrdsaplLNVEGLSVSFPIRKGILRrvVDqnavlkNIRFSLRPGESLGLVGESGSGKSTT 328
Cdd:TIGR02633 240 REITSLYPHEPheIGDVI---------LEARNLTCWDVINPHRKR--VD------DVSFSLRRGEILGVAGLVGAGRTEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 329 GLALLRLIASQ--GEILFDGMPLHRWNRRQmlPVRPRMQVVFQDpnsslNPRLSILQIIEEGlrvHQPTLTALQRENEVR 406
Cdd:TIGR02633 303 VQALFGAYPGKfeGNVFINGKPVDIRNPAQ--AIRAGIAMVPED-----RKRHGIVPILGVG---KNITLSVLKSFCFKM 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 407 RVMAEVGLDP--------ETRHRYP----AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEK 474
Cdd:TIGR02633 373 RIDAAAELQIigsaiqrlKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE 452
|
490 500 510
....*....|....*....|....*....|
gi 502863011 475 HrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:TIGR02633 453 G-VAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
274-501 |
7.78e-33 |
|
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: 124.51 E-value: 7.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG4133 1 MMLEAENLSCRR-----------GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILAgllppSAGEVLWNGEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRwnrrqmLPVRPRMQVVFQDPNSSLNPRLSILqiieEGLRVHQPTLTALQRENEVRRVMAEVGLDPEtRHRYPAEFSG 428
Cdd:COG4133 66 IRD------AREDYRRRLAYLGHADGLKPELTVR----ENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAyIFISHDLqvVRALCHQVIVLRQ 501
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQP--LELAAARVLDLGD 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-234 |
8.81e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 124.33 E-value: 8.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQ---RGETLALVGESGSGKSvSALSILHLLPSPPVsypqGDILFHGSSLLHADEQTLRGVRGNKIAMIFQEpmV 103
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKS-TLLRCIAGLEKPDG----GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAakrlsdFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502863011 184 TTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-257 |
9.08e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.96 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiafsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGssllh 80
Cdd:COG1118 3 IEVRNIS----KRFGSFTLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEPM------VSLNPLHTLEkqlyevlslHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFP 154
Cdd:COG1118 64 RDLFTNLPPRERRVGFVFQHYAlfphmtVAENIAFGLR---------VRPPSKAEIRARVEELLELVQLEGLADR---YP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
250 260
....*....|....*....|...
gi 502863011 235 CVEQNTAAALLNAPQHPYTQRLL 257
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-252 |
9.13e-33 |
|
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: 126.22 E-value: 9.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 25 VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQTLRGVRGNKIAMIFQEpmVS 104
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--PTS---GKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 LNPLHT-LEKQLY--EVLSLHRGMRKEAARgeilDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:cd03294 113 LLPHRTvLENVAFglEVQGVPRAEREERAA----EALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 182 EPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPY 252
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-258 |
1.31e-32 |
|
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: 131.43 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsYPQGDILFHGSSLLHA 81
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLHRGmrkEAARGEILDCLDRTGIrnaAKRLSDFPH------ 155
Cdd:COG4987 403 DEDDLR----RRIAVVPQRP-------HLFDTTLRENLRLARP---DATDEELWAALERVGL---GDWLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVM 230
Cdd:COG4987 466 geggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVL 542
|
250 260
....*....|....*....|....*...
gi 502863011 231 QNGRCVEQNTAAALLNapQHPYTQRLLD 258
Cdd:COG4987 543 EDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-245 |
1.74e-32 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 124.58 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILH--LLPSppvsypQGDILFHGSSLLHAD 82
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKT-TLLRMLAglLKPD------SGSILIDGEDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRgvrgnKIAMIFQEPMVSLNplHTLEKQLYEVLSLHrGMRKEAARGEILDCLDRTGIRNAAKRLSdfpHQLSGGER 162
Cdd:COG4555 70 REARR-----QIGVLPDERGLYDR--LTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRV---GELSTGMK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAA 242
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLD 217
|
...
gi 502863011 243 ALL 245
Cdd:COG4555 218 ELR 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
274-519 |
2.41e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.13 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLhrw 352
Cdd:PRK13635 4 EIIRVEHISFRYP---------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQMLPVRPRMQVVFQDPNSslnprlsilQIIeeGLRVHQPTLTALQ-----RENEVRRV---MAEVGLDpETRHRYPA 424
Cdd:PRK13635 72 SEETVWDVRRQVGMVFQNPDN---------QFV--GATVQDDVAFGLEnigvpREEMVERVdqaLRQVGME-DFLNREPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEV 504
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
250
....*....|....*
gi 502863011 505 VEQGECQRVFTAPTQ 519
Cdd:PRK13635 219 LEEGTPEEIFKSGHM 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
298-526 |
3.24e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.66 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLhRWNRRQMLPVRPRMQVVFQDPN 372
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCInkleeITSGDLIVDGLKV-NDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 ssLNPRLSILQIIEEGlRVHQPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK09493 88 --LFPHLTALENVMFG-PLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLL 526
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-258 |
3.73e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.66 E-value: 3.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHLLPSppvsypqGDILFHGSSLL--HADEQTLRGVRG 91
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKStlLRCINKLEEITS-------GDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 92 nkiaMIFQEpmVSLNP-LHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMA 170
Cdd:PRK09493 81 ----MVFQQ--FYLFPhLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 171 LLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNapqH 250
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK---N 226
|
....*...
gi 502863011 251 PYTQRLLD 258
Cdd:PRK09493 227 PPSQRLQE 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-247 |
3.96e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.90 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 19 GETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPS--PPVSypqGDILFHGSSLLHADEQTLRgvrgNKIAM 96
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRfyDPTS---GRILIDGVDIRDLTLESLR----RQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 97 IFQEPMVslnplhtLEKQLYEVLSLhrGmRKEAARGEILDCLDRTgirNAAKRLSDFPHQ-----------LSGGERQRV 165
Cdd:COG1132 419 VPQDTFL-------FSGTIRENIRY--G-RPDATDEEVEEAAKAA---QAHEFIEALPDGydtvvgergvnLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAALL 245
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
..
gi 502863011 246 NA 247
Cdd:COG1132 563 AR 564
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-249 |
6.27e-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: 122.83 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetrTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGssllhADEQT 85
Cdd:cd03299 1 LKVENLSKDWKE-----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDS---GKILLNG-----KDITN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNkIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARgEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRV 165
Cdd:cd03299 66 LPPEKRD-ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGIDHLLNR---KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALL 245
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
....
gi 502863011 246 NAPQ 249
Cdd:cd03299 219 KKPK 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
292-527 |
9.70e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.16 E-value: 9.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHR----------WNRRQ 356
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCInflekPSEGSIVVNGQTINLvrdkdgqlkvADKNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 357 MLPVRPRMQVVFQDPNssLNPRLSILQIIEEGlRVHQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAI 436
Cdd:PRK10619 87 LRLLRTRLTMVFQHFN--LWSHMTVLENVMEA-PIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 437 ARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTA 516
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|.
gi 502863011 517 PTQSYTRQLLS 527
Cdd:PRK10619 243 PQSPRLQQFLK 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-240 |
1.04e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLlh 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--PEA---GTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 aDEQTLRGVRgNKIAMIFQEP-------MVSLNPLHTLEKQlyevlslhrGMRKEAARGEILDCLDRTGIRNAAKRLsdf 153
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPdnqfvgaTVQDDVAFGLENI---------GVPREEMVERVDQALRQVGMEDFLNRE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQNG 233
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
....*..
gi 502863011 234 RCVEQNT 240
Cdd:PRK13635 217 EILEEGT 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-258 |
1.15e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.55 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 17 KQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVSYPQ-GDILFHGSSLLHADEQTLRGVRgNKIA 95
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAGTIRvGDITIDTARSLSQQKGLIRQLR-QHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 96 MIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:PRK11264 89 FVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 176 ELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQR 255
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
...
gi 502863011 256 LLD 258
Cdd:PRK11264 243 FLE 245
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
301-528 |
1.20e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 122.22 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPR-MQVVFQdpNSS 374
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKST----LLRIIAgleqpDSGRIRLNGQDATR------VHARDRkIGFVFQ--HYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIEEGLRVHQPTLTALQ-RENEVRRVMAEVGLdpetRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKaRVEELLELVQLEGL----GDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 454 SSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGE 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
294-514 |
1.21e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.42 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 294 RVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHrWNRRQMLPVRPRMQVVFQDPN 372
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SSLNPRlSILQIIEEG-LRVHQPTLTALQReneVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK13636 93 NQLFSA-SVYQDVSFGaVNLKLPEDEVRKR---VDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-234 |
1.58e-31 |
|
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: 119.27 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTL 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKS-TLLRAIAGLLKPT----SGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 87 RgvrgNKIAMIFQepmvslnplhtlekqlyevlslhrgmrkeaargeildcldrtgirnaakrlsdfphqLSGGERQRVM 166
Cdd:cd00267 72 R----RRIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 167 IAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
300-518 |
1.68e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.99 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 300 AVLKNIRFSLRPGESLGLVGESGSGKST-----TGLaLLRLIASQGEILFDGMPLhrwNRRQMLPVRPRMQVVFQDPNSS 374
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTiskliNGL-LLPDDNPNSKITVDGITL---TAKTVWDIREKVGIVFQNPDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LnprlsILQIIEE----GLRVHQPTLTALQREneVRRVMAEVGL----DPEtrhryPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PRK13640 97 F-----VGATVGDdvafGLENRAVPRPEMIKI--VRDVLADVGMldyiDSE-----PANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 447 IILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-234 |
2.49e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.31 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsYPQGDILFHGSSLLHADEQT 85
Cdd:COG4619 1 LELEGLSFRVG----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGKPLSAMPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGvrgnKIAMIFQEPmvslnplHTLEKQLYEVLSLHRGMRKEAargeildcLDRTGIRNAAKRLsDFP--------HQL 157
Cdd:COG4619 72 WRR----QVAYVPQEP-------ALWGGTVRDNLPFPFQLRERK--------FDRERALELLERL-GLPpdildkpvERL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:COG4619 132 SGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
305-521 |
2.70e-31 |
|
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: 124.07 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 305 IRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPV-RPRMQVVFQDpnSSLNPR 378
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTT----LIRLIAgltrpDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 379 LSILQIIEEGLRVHQPTLTALQREnevrRVMAEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDR 458
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFE----RVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 459 TVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSY 521
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
301-527 |
3.78e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 120.89 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRL-----IASQGEILFDGMPL---HRWNRRQMLPVRPRMQVVFQDPN 372
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSS----LLRVlnlleTPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 ssLNPRLSILQ-IIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:COG4161 93 --LWPHLTVMEnLIEAPCKVLG--LSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQrVFTAPTQSYTRQLLS 527
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTEAFAHYLS 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
274-502 |
4.06e-31 |
|
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: 120.23 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPI-RKGILRRVVdqnavLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFD-- 345
Cdd:COG4778 3 TLLEVENLSKTFTLhLQGGKRLPV-----LDGVSFSVAAGECVALTGPSGAGKST----LLKCIygnylPDSGSILVRhd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 --GMPLHRWNRRQMLPVRPR--------MQVVfqdpnsslnPRLSILQIIEEGLRVHQ-PTLTALQReneVRRVMAEVGL 414
Cdd:COG4778 74 ggWVDLAQASPREILALRRRtigyvsqfLRVI---------PRVSALDVVAEPLLERGvDREEARAR---ARELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 415 DPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLqeKHR-LAYIFISHDLQVVRALC 493
Cdd:COG4778 142 PERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA--KARgTAIIGIFHDEEVREAVA 219
|
....*....
gi 502863011 494 HQVIVLRQG 502
Cdd:COG4778 220 DRVVDVTPF 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
299-527 |
1.67e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 299 NAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRL-----IASQGEILFDGMPL---HRWNRRQMLPVRPRMQVVFQD 370
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSS----LLRVlnlleMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 PNssLNPRLSILQ-IIEEGLRVHQptLTALQRENEVRRVMAEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:PRK11124 91 YN--LWPHLTVQQnLIEAPCRVLG--LSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 450 DEPTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRvFTAPTQSYTRQLLS 527
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYLS 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
302-526 |
2.57e-30 |
|
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: 118.60 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPRmQV--VFQdpNSS 374
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTT----LLRLIAglerpDSGTILFGGEDATD------VPVQER-NVgfVFQ--HYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIEEGLRV----HQPTLTALQREneVRRVMAEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVkprsERPPEAEIRAK--VHELLKLVQLDWLAD-RYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 451 EPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLL 526
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
2.79e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 124.13 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSypqGDILFHGSS- 77
Cdd:PRK09700 1 MATPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKStlMKVLSGIH----EPTK---GTITINNINy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 --LLHADEQTLrgvrgnKIAMIFQEPMVsLNPLHTLEkQLY-------EVLSL----HRGMRKEAArgeILdcLDRTGIR 144
Cdd:PRK09700 70 nkLDHKLAAQL------GIGIIYQELSV-IDELTVLE-NLYigrhltkKVCGVniidWREMRVRAA---MM--LLRVGLK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 145 naaKRLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLA 224
Cdd:PRK09700 137 ---VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRIC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 225 DSVAVMQNGRCVEQNTAAALLNAPqhpyTQRLLDSEPAGDPVPLQRDSAPLLNVEglsVSFPIRKgILRRvvDQNAVlKN 304
Cdd:PRK09700 213 DRYTVMKDGSSVCSGMVSDVSNDD----IVRLMVGRELQNRFNAMKENVSNLAHE---TVFEVRN-VTSR--DRKKV-RD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 305 IRFSLRPGESLGLVGESGSGKSTTGLALLRL--IASqGEILFDGMPLHrwNRRQMLPVRPRMQVVFQD-------PNSSL 375
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVdkRAG-GEIRLNGKDIS--PRSPLDAVKKGMAYITESrrdngffPNFSI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRLSILQIIEEGlrVHQPTLTALQRENEVRRVMAE---VGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK09700 359 AQNMAISRSLKDG--GYKGAMGLFHEVDEQRTAENQrelLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
300-504 |
2.96e-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: 117.51 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 300 AVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDpnSS 374
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKST----LLKLIYkeelpTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIEEGLRVHQPTLTALQREneVRRVMAEVGLdpETRHR-YPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03292 89 LLPDRNVYENVAFALEVTGVPPREIRKR--VPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502863011 454 SSLDRTVQAQILTLLKGLQEkhRLAYIFIS-HDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINK--AGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-248 |
4.46e-30 |
|
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: 120.59 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSvsalSILHL---LPSPPvsypQGDILFHGSSLLHADEQTLRGVRGNKIAMIFQEPmv 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKT----TLLRAiagLERPD----SGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNPlHtlekqlYEVLS-LHRGMR---KEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:COG4148 87 RLFP-H------LSVRGnLLYGRKrapRAERRISFDEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 180 ADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAP 248
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-528 |
8.05e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 119.52 E-value: 8.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKGILRrVVDQnavlknIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMplhRWN 353
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVK-AVDR------VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRM---RFD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 RRQMLPVRPR---------MQVVFQDPNSSLNPRLSI-LQIIEEglrvhQPTLTA----LQRENEVRRVMAE----VGL- 414
Cdd:PRK15093 72 DIDLLRLSPRerrklvghnVSMIFQEPQSCLDPSERVgRQLMQN-----IPGWTYkgrwWQRFGWRKRRAIEllhrVGIk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 415 DP-ETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALC 493
Cdd:PRK15093 147 DHkDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
250 260 270
....*....|....*....|....*....|....*
gi 502863011 494 HQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK15093 227 DKINVLYCGQTVETAPSKELVTTPHHPYTQALIRA 261
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
9.36e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.45 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILH-LLPSPPVSypqGDILFHGSSL 78
Cdd:COG1117 8 LEPKIEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKStlLRCLNRMNdLIPGARVE---GEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LHA--DEQTLRgvRgnKIAMIFQEPmvslNPLhtlEKQLYE-V---LSLHrGMRKEAARGEIL-DCLDRTGIRNAAK-RL 150
Cdd:COG1117 81 YDPdvDVVELR--R--RVGMVFQKP----NPF---PKSIYDnVaygLRLH-GIKSKSELDEIVeESLRKAALWDEVKdRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 151 SDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVKKLADSVAVM 230
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|....
gi 502863011 231 QNGRCVEQNTAAALLNAPQHPYTQ 254
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
297-517 |
1.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.87 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhRWNRRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 -NPRlsILQIIEEGlrvhqPTLTALQRENEVRRVM---AEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK13639 92 fAPT--VEEDVAFG-----PLNLGLSKEEVEKRVKealKAVGMEGFEN-KPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
297-508 |
1.09e-29 |
|
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: 116.05 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPLHRWnrrqmlpvRPRMQVVFQD 370
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGvdiskIGLHDL--------RSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 PnsslnprlsilqIIEEGlrvhqpTLtalqREN----------EVRRVMAEVGLD-----PETRHRYPAE-----FSGGQ 430
Cdd:cd03244 87 P------------VLFSG------TI----RSNldpfgeysdeELWQALERVGLKefvesLPGGLDTVVEeggenLSVGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLkglqeKHRLA---YIFISHDLQVVrALCHQVIVLRQGEVVEQ 507
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI-----REAFKdctVLTIAHRLDTI-IDSDRILVLDKGRVVEF 218
|
.
gi 502863011 508 G 508
Cdd:cd03244 219 D 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
274-520 |
1.28e-29 |
|
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: 116.72 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI------ASQGEI-LFdG 346
Cdd:COG1119 2 PLLELRNVTVRR-----------GGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLItgdlppTYGNDVrLF-G 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNrrqMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGL-----RVHQPTLTALQReneVRRVMAEVGLDpETRHR 421
Cdd:COG1119 66 ERRGGED---VWELRKRIGLVSPALQLRFPRDETVLDVVLSGFfdsigLYREPTDEQRER---ARELLELLGLA-HLADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 422 YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218
|
250
....*....|....*....
gi 502863011 502 GEVVEQGECQRVFTAPTQS 520
Cdd:COG1119 219 GRVVAAGPKEEVLTSENLS 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-252 |
1.35e-29 |
|
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: 116.28 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGssllhaDEQTLRGVRGNKIA 95
Cdd:cd03296 9 SKRFGDFVALDDVSLDIPSGELVALLGPSGSGKT-TLLRLIAGLERPD----SGTILFGG------EDATDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 96 MIFQ------EPMVSLNPLHTLEKQlyevlslHRGMRKEAA--RGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMI 167
Cdd:cd03296 78 FVFQhyalfrHMTVFDNVAFGLRVK-------PRSERPPEAeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 168 AMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRcVEQ-NTAAALLN 246
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQvGTPDEVYD 226
|
....*.
gi 502863011 247 APQHPY 252
Cdd:cd03296 227 HPASPF 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-249 |
1.37e-29 |
|
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: 116.38 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqGETrTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL--HLLPSppvsypQGDILFHGSSLLH--A 81
Cdd:cd03219 1 LEVRGLTKRF---GGL-VALDDVSFSVRPGEIHGLIGPNGAGKT-TLFNLIsgFLRPT------SGSVLFDGEDITGlpP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGV-RGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKE-AARGEILDCLDRTGIRNAAKRLSDfphQLSG 159
Cdd:cd03219 70 HEIARLGIgRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREErEARERAEELLERVGLADLADRPAG---ELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
250
....*....|
gi 502863011 240 TAAALLNAPQ 249
Cdd:cd03219 226 TPDEVRNNPR 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
297-514 |
1.98e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.77 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtgLALLRL---IASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNS 373
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKST--IAKLMIgieKVKSGEIFYNNQAITDDNFEK---LRKHIGIVFQNPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 SLNPrlSILQI-IEEGLRVHQPTLTALQREneVRRVMAEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK13648 95 QFVG--SIVKYdVAFGLENHAVPYDEMHRR--VSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDL-QVVRAlcHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAMEA--DHVIVMNKGTVYKEGTPTEIF 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
271-527 |
2.01e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.29 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-------LIASQ---G 340
Cdd:COG1117 7 TLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPGArveG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 341 EILFDGMPLHRwnrRQMLPVRPRMQV--VFQDPNsslnP-RLSILQIIEEGLRVHQPTLTAlQRENEVRRVMAEVGLDPE 417
Cdd:COG1117 72 EILLDGEDIYD---PDVDVVELRRRVgmVFQKPN----PfPKSIYDNVAYGLRLHGIKSKS-ELDEIVEESLRKAALWDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 418 TRHR---YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLqeKHRLAYIFISHDLQVVRALCH 494
Cdd:COG1117 144 VKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSD 221
|
250 260 270
....*....|....*....|....*....|...
gi 502863011 495 QVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLS 527
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
275-521 |
3.01e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.63 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWN 353
Cdd:PRK13644 1 MIRLENVSYSYP----------DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 354 RRQmlPVRPRMQVVFQDPNSSLNPRlsilqIIEEGLRV--HQPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQR 431
Cdd:PRK13644 71 KLQ--GIRKLVGIVFQNPETQFVGR-----TVEEDLAFgpENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQ 511
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
250
....*....|
gi 502863011 512 RVFTAPTQSY 521
Cdd:PRK13644 221 NVLSDVSLQT 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
256-518 |
3.63e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 122.14 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 256 LLDSEPAgdpVPLQRDSAPLlNVEGL------SVSFPIRKgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTTG 329
Cdd:TIGR00958 457 YLDRKPN---IPLTGTLAPL-NLEGLiefqdvSFSYPNRP--------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 330 LALLRL-IASQGEILFDGMPL----HRWNRRQMlpvrprmQVVFQDPnssLNPRLSILQIIEEGLRVHQptltalqrENE 404
Cdd:TIGR00958 525 ALLQNLyQPTGGQVLLDGVPLvqydHHYLHRQV-------ALVGQEP---VLFSGSVRENIAYGLTDTP--------DEE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 405 VRRVMAEVGLDP---ETRHRYPAE-------FSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILTLLKGLQEK 474
Cdd:TIGR00958 587 IMAAAKAANAHDfimEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSR 662
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 502863011 475 HRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
276-504 |
3.91e-29 |
|
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: 113.08 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:cd03246 1 LEVENVSFRYP---------GAEPPVLRNVSFSIEPGESLAIIGPSGSGKST----LARLILgllrpTSGRVRLDGADIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMlpvRPRMQVVFQDPNsslnprL---SILQIIeeglrvhqptltalqrenevrrvmaevgldpetrhrypaeFS 427
Cdd:cd03246 68 QWDPNEL---GDHVGYLPQDDE------LfsgSIAENI----------------------------------------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIFISHDLQVVrALCHQVIVLRQGEV 504
Cdd:cd03246 99 GGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-521 |
4.57e-29 |
|
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: 117.21 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 317 LVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLhrwnrRQMLPVRPRMQVVFQdpNSSLNPRLSILQIIEEGLRV 391
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAgfeqpDSGSIMLDGEDV-----TNVPPHLRHINMVFQ--SYALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 392 HQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGL 471
Cdd:TIGR01187 70 RK--VPRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502863011 472 QEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSY 521
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
274-522 |
5.28e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.13 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:PRK09452 13 PLVELRGISKSF-----------DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIMLDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRwnrrqmLPVRPR-MQVVFQdpNSSLNPRLSILQIIEEGLRvhqptltaLQR--ENEVR-RVM---AEVGLDpETRHR 421
Cdd:PRK09452 78 ITH------VPAENRhVNTVFQ--SYALFPHMTVFENVAFGLR--------MQKtpAAEITpRVMealRMVQLE-EFAQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 422 YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD 220
|
250 260
....*....|....*....|.
gi 502863011 502 GEVVEQGECQRVFTAPTQSYT 522
Cdd:PRK09452 221 GRIEQDGTPREIYEEPKNLFV 241
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
8-276 |
5.29e-29 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 117.79 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 8 IDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSypqGDILFHGSSLLHADEQTlr 87
Cdd:TIGR03258 8 IDHLRVAYG----ANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLT---GRIAIADRDLTHAPPHK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 88 gvRGnkIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARgEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMI 167
Cdd:TIGR03258 79 --RG--LALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAE-RVADALKLVGLGDAAAHL---PAQLSGGMQQRIAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 168 AMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSEL-NMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLN 246
Cdd:TIGR03258 149 ARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYD 228
|
250 260 270
....*....|....*....|....*....|
gi 502863011 247 APQHPYTQRLLDSEPAGDPVPLQRDSAPLL 276
Cdd:TIGR03258 229 APADGFAAEFLGAANILPAIALGITEAPGL 258
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
301-508 |
7.18e-29 |
|
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: 114.25 E-value: 7.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNR---RQMLPVRPRMQVVFQDpn 372
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLfrfydVSSGSILIDGQDIREVTLdslRRAIGVVPQDTVLFND-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 sslnprlsilqIIEEGLRVHQPTLTalqrENEVRRVmAEVGLDPETRHRYPAEF-----------SGGQRQRIAIARALI 441
Cdd:cd03253 90 -----------TIGYNIRYGRPDAT----DEEVIEA-AKAAQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 442 LKPELIILDEPTSSLD----RTVQAQILTLLKGlqekhRLAyIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03253 154 KNPPILLLDEATSALDthteREIQAALRDVSKG-----RTT-IVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
297-529 |
7.86e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 115.96 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEILFDGMPLhrwnrRQMLPVRPRMQV--VFQ 369
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT----LRMInrliePTSGRILIDGEDI-----RDLDPVELRRRIgyVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 dpNSSLNPRLSILQIIEeglRVhqPTLTALQRENEVRRV---MAEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:COG1125 84 --QIGLFPHMTVAENIA---TV--PRLLGWDKERIRARVdelLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 446 LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQL 525
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236
|
....
gi 502863011 526 LSAD 529
Cdd:COG1125 237 VGAD 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-508 |
7.98e-29 |
|
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: 113.62 E-value: 7.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFpirkGILRRVVdqnAVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEILFDGMPL 349
Cdd:cd03266 1 MITADALTKRF----RDVKKTV---QAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDGFDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRwnrrQMLPVRPRMQVVFQdpNSSLNPRLSILQIIEEGLRVHqptltALQRENEVRRV--MAEVGLDPETRHRYPAEFS 427
Cdd:cd03266 70 VK----EPAEARRRLGFVSD--STGLYDRLTARENLEYFAGLY-----GLKGDELTARLeeLADRLGMEELLDRRVGGFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
.
gi 502863011 508 G 508
Cdd:cd03266 218 G 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-245 |
8.94e-29 |
|
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: 114.17 E-value: 8.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLlhaDEQTLRGVRgNKIAMIF 98
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLerfydPT------SGEILLDGVDI---RDLNLRWLR-SQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 99 QEPMVSLNPLhtLEKQLYEVLSLHRGMRKEAARgeildcldrtgIRNAAKRLSDFPH-----------QLSGGERQRVMI 167
Cdd:cd03249 84 QEPVLFDGTI--AENIRYGKPDATDEEVEEAAK-----------KANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 168 AMALLTRPELLIADEPTTALDVTVQAQILQLLRELRseLNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAALL 245
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-527 |
1.18e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA------SQGEILFDGMPLHRWNrrqMLPVRPRMQ 365
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMD---VIELRRRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 366 VVFQDPNSSlnPRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAEVGLDPETRHRYPA---EFSGGQRQRIAIARALIL 442
Cdd:PRK14247 86 MVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 443 KPELIILDEPTSSLDRTVQAQILTLLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYT 522
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....*
gi 502863011 523 RQLLS 527
Cdd:PRK14247 242 EKYVT 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
296-524 |
1.21e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 114.37 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 296 VDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-------ASQGEILFDGMPLHRWNrrqMLPVRPRMQVVF 368
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQID---AIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 369 QDPNSSlnPRLSILQIIEEGLRVHqptltALQRENEVRRVMAE----VGLDPETRHRY--PA-EFSGGQRQRIAIARALI 441
Cdd:PRK14246 97 QQPNPF--PHLSIYDNIAYPLKSH-----GIKEKREIKKIVEEclrkVGLWKEVYDRLnsPAsQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 442 LKPELIILDEPTSSLDRTVQAQILTLLKGLqeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSY 521
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
...
gi 502863011 522 TRQ 524
Cdd:PRK14246 248 TEK 250
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
298-496 |
1.48e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.37 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRmQVVFQDPN 372
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKST----LLHLLGgldtpTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SSLNPRLSILQIIEEGLRV-HQPTLTALQRENEVrrvMAEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK11629 96 HHLLPDFTALENVAMPLLIgKKKPAEINSRALEM---LAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
302-509 |
2.24e-28 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 112.94 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmlPVRPRMqVVFQdpNSSLN 376
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST----LLNLISglaqpTSGGVILEGKQITE-------PGPDRM-VVFQ--NYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502863011 457 DRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-238 |
2.67e-28 |
|
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: 111.99 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADeqt 85
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL--PDS---GEVLFDGKPLDIAA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 lrgvrGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQRV 165
Cdd:cd03269 69 -----RNRIGYLPEER--GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-240 |
4.18e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.22 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLP--SPPVSypqGDILFHGSSL 78
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS----TLLHLLGglDTPTS---GDVIFNGQPM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LHADEQTLRGVRGNKIAMIFQ--EPMVSLNPLHTLEKQLyevlsLHRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQ 156
Cdd:PRK11629 74 SKLSSAAKAELRNQKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAvMQNGRCV 236
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLT 224
|
....
gi 502863011 237 EQNT 240
Cdd:PRK11629 225 AELS 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
254-514 |
4.33e-28 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 117.93 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSEPA-GDPVPLQRDSAPLlNVEGLSVSFPIRkgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaL 332
Cdd:COG4618 309 NELLAAVPAePERMPLPRPKGRL-SVENLTVVPPGS---------KRPILRGVSFSLEPGEVLGVIGPSGSGKST----L 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 333 LRLI-----ASQGEILFDGMPLHRWNRRQM------LPvrprmQVV-------------FQDPNSSlnprlsilQIIEeg 388
Cdd:COG4618 375 ARLLvgvwpPTAGSVRLDGADLSQWDREELgrhigyLP-----QDVelfdgtiaeniarFGDADPE--------KVVA-- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 389 lrvhqptltALQRenevrrvmaeVGLDpETRHRYP-----------AEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:COG4618 440 ---------AAKL----------AGVH-EMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 458 RTVQAQILTLLKGLQEKHRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVF 514
Cdd:COG4618 500 DEGEAALAAAIRALKARGATV-VVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-255 |
5.33e-28 |
|
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: 114.82 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 11 LSIAFSK-QGETRTvvsDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVsypqGDILFHGSSLLHADEQTLRGV 89
Cdd:TIGR02142 1 LSARFSKrLGDFSL---DADFTLPGQGVTAIFGRSGSGKT-TLIRLIAGLTRPDE----GEIVLNGRTLFDSRKGIFLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 90 RGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLdrtGIRNAAKRLsdfPHQLSGGERQRVMIAM 169
Cdd:TIGR02142 73 EKRRIGYVFQE--ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRL---PGRLSGGEKQRVAIGR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 170 ALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQ 249
Cdd:TIGR02142 145 ALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
....*.
gi 502863011 250 HPYTQR 255
Cdd:TIGR02142 225 LPWLAR 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
279-508 |
5.41e-28 |
|
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: 111.86 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 279 EGLSVSFPIRKGILrrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQm 357
Cdd:cd03249 4 KNVSFRYPSRPDVP--------ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILLDGVDIRDLNLRW- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 358 lpVRPRMQVVFQDP---NSSlnprlsilqiIEEGLRVHQPTLTALQRENEVRrvMAEV---------GLDPETRHRYpAE 425
Cdd:cd03249 75 --LRSQIGLVSQEPvlfDGT----------IAENIRYGKPDATDEEVEEAAK--KANIhdfimslpdGYDTLVGERG-SQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLLKGlqekhRLAyIFISHDLQVVRAlCHQVIVLRQ 501
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDaeseKLVQEALDRAMKG-----RTT-IVIAHRLSTIRN-ADLIAVLQN 212
|
....*..
gi 502863011 502 GEVVEQG 508
Cdd:cd03249 213 GQVVEQG 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
271-515 |
8.57e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.39 E-value: 8.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 271 DSAPLLNVEGLSVSFPirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFD 345
Cdd:PRK13632 3 NKSVMIKVENVSFSYP---------NSENNALKNVSFEINEGEYVAILGHNGSGKSTiskilTGL----LKPQSGEIKID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRWNRRQmlpVRPRMQVVFQDPNSslnprlsilQIIeeGLRVHQPTLTALQRENEVRRVM--------AEVGLDpE 417
Cdd:PRK13632 70 GITISKENLKE---IRKKIGIIFQNPDN---------QFI--GATVEDDIAFGLENKKVPPKKMkdiiddlaKKVGME-D 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVI 497
Cdd:PRK13632 135 YLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVI 213
|
250
....*....|....*...
gi 502863011 498 VLRQGEVVEQGECQRVFT 515
Cdd:PRK13632 214 VFSEGKLIAQGKPKEILN 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-507 |
1.04e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.88 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKGilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTT----LLNLIAgflapSSGEITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRwnrrqmlPVRPRmQVVFQDpnSSLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSG 428
Cdd:COG4525 71 VTG-------PGADR-GVVFQK--DALLPWLNVLDNVAFGLRLRG--VPKAERRARAEELLALVGLA-DFARRRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL--RQGEVVE 506
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
.
gi 502863011 507 Q 507
Cdd:COG4525 218 R 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
297-508 |
1.13e-27 |
|
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: 117.36 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLHRWNRRQmlpVRPRMQVVFQdp 371
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKST----LLRLLLGfetpeSGSVFYDGQDLAGLDVQA---VRRQLGVVLQ-- 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSLNPRlSILQIIEEGLRVhqpTLtalqreNEVRRVMAEVGLDPETR------HRYPAE----FSGGQRQRIAIARALI 441
Cdd:TIGR03797 535 NGRLMSG-SIFENIAGGAPL---TL------DEAWEAARMAGLAEDIRampmgmHTVISEgggtLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 442 LKPELIILDEPTSSLDRTVQAQILTLLKGLQekhrLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-255 |
1.22e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.11 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVSYP-QGDILFHGSSLL-HA 81
Cdd:PRK14271 20 PAMAAVNLTLGFAG----KTVLDQVSMGFPARAVTSLMGPTGSGKT-TFLRTLNRMNDKVSGYRySGDVLLGGRSIFnYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRgvrgNKIAMIFQEPmvSLNPLHTLEKQLYEVLSlHRGMRKEAARGEILDCLDRTGIRNAAK-RLSDFPHQLSGG 160
Cdd:PRK14271 95 DVLEFR----RRVGMLFQRP--NPFPMSIMDNVLAGVRA-HKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELnmSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250
....*....|....*
gi 502863011 241 AAALLNAPQHPYTQR 255
Cdd:PRK14271 246 TEQLFSSPKHAETAR 260
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
27-289 |
1.36e-27 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 113.63 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSVsalsILHLLPS--PPVSypqGDILFHGSSL-LHADEQtlrgvRGnkIAMIFQEPMv 103
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTV----LLELIAGiwPPDS---GKIYLDGKDItNLPPEK-----RG--IAYVYQNYM- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 sLNPLHTLEKQLYEVLSLHRGMRKEAAR--GEILDCLdrtGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:NF040840 83 -LFPHKTVFENIAFGLKLRKVPKEEIERkvKEIMELL---GISHLLHRK---PRTLSGGEQQRVALARALIIEPKLLLLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 182 EPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQRLLDSEP 261
Cdd:NF040840 156 EPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFEN 235
|
250 260
....*....|....*....|....*...
gi 502863011 262 AGDPVPLQRDSAPLLNVEGLSVSFPIRK 289
Cdd:NF040840 236 IIEGVAEKGGEGTILDTGNIKIELPEEK 263
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-254 |
1.44e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.36 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 25 VSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTLRGVRGNKIAMIFQEpmVS 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEPT----RGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 LNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKrlsDFPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 185 TALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQ 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
297-504 |
1.89e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEILFDGMPL---HRWNRRQmlpvrpRMQVVF 368
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIdglleAESGQIIIDGDLLteeNVWDIRH------KIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 369 QDPNSSL--------------NPRLSILQIIEeglRVHQptltALQRenevrrvmaeVGLDpETRHRYPAEFSGGQRQRI 434
Cdd:PRK13650 88 QNPDNQFvgatveddvafgleNKGIPHEEMKE---RVNE----ALEL----------VGMQ-DFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 435 AIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEV 504
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
301-504 |
2.15e-27 |
|
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: 109.87 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPL----HRWNRRQMlpvrprmQVVFQDPnsSL 375
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPIsqyeHKYLHSKV-------SLVGQEP--VL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRlSILQIIEEGLR-VHQPTLTALQRENEVRRVMAEV--GLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03248 100 FAR-SLQDNIAYGLQsCSFECVKEAAQKAHAHSFISELasGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRlaYIFISHDLQVV-RAlcHQVIVLRQGEV 504
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERRT--VLVIAHRLSTVeRA--DQILVLDGGRI 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-238 |
2.30e-27 |
|
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: 109.23 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTlrgvrgNKIA 95
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKT-TTMKIILGLIKPD----SGEITFDGKSYQKNIEAL------RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 96 MIFQEPmvSLNPLHTLEKQLYeVLSLHRGMRKEaargEILDCLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTRP 175
Cdd:cd03268 76 ALIEAP--GFYPNLTARENLR-LLARLLGIRKK----RIDEVLDVVGLKDSAKKKVK---GFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 176 ELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-238 |
2.37e-27 |
|
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: 109.50 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPPVsyPQ-GDILFHGSSLLHADeqtlrgVRGNKIAMIFQEPmvSL 105
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS----TLLNLIAGFET--PQsGRVLINGVDVTAAP------PADRPVSMLFQEN--NL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 106 NPLHTLEKQLyeVLSLHRGMR-KEAARGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:cd03298 82 FAHLTVEQNV--GLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 185 TALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
275-497 |
2.55e-27 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 109.79 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPI-RKGILRRvvdqnAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILF---- 344
Cdd:TIGR02324 1 LLEVEDLSKTFTLhQQGGVRL-----PVLKNVSLTVNAGECVALSGPSGAGKST----LLKSLyanylPDSGRILVrheg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 345 DGMPLHRWNRRQMLPVRpRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQreNEVRRVMAEVGLDPETRHRYPA 424
Cdd:TIGR02324 72 AWVDLAQASPREVLEVR-RKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAAR--ARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKglQEKHR-LAYIFISHDLQVVRALCHQVI 497
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIA--EAKARgAALIGIFHDEEVRELVADRVM 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
302-526 |
3.01e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.59 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMLPVR-PRMQVVFQdpNSSLNPRL 379
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQ--SFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SILQIIEEGLRVhqPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:PRK10070 122 TVLDNTAFGMEL--AGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 460 VQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLL 526
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
297-508 |
3.23e-27 |
|
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: 109.88 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPL----HRWNRRQMlpvrprmQVVFQDp 371
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLaladPAWLRRQV-------GVVLQE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSLNPrlSILQII---EEGLRVHQPTLTA-LQRENEVRRVMAEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPELI 447
Cdd:cd03252 85 NVLFNR--SIRDNIalaDPGMSMERVIEAAkLAGAHDFISELPE-GYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 448 ILDEPTSSLD----RTVQAQILTLLKGlqekhRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03252 161 IFDEATSALDyeseHAIMRNMHDICAG-----RTV-IIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-256 |
3.61e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 115.31 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGS 76
Cdd:PRK11160 335 DQVSLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLtrawdPQ------QGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 77 SLLHADEQTLRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLhrgmRKEAARGEIL-DCLDRTGIRN---AAKRLS- 151
Cdd:PRK11160 403 PIADYSEAALR----QAISVVSQRV-------HLFSATLRDNLLL----AAPNASDEALiEVLQQVGLEKlleDDKGLNa 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 ---DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLaDSVA 228
Cdd:PRK11160 468 wlgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRIC 544
|
250 260
....*....|....*....|....*...
gi 502863011 229 VMQNGRCVEQNTAAALLNapQHPYTQRL 256
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLA--QQGRYYQL 570
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-510 |
4.05e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFPirkgilrRVVdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG 346
Cdd:COG3845 2 MPPALELRGITKRFG-------GVV----ANDDVSLTVRPGEIHALLGENGAGKST----LMKILyglyqPDSGEILIDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNrrqmlpvrPR--------MqvVFQDPnsSLNPRLSILQ-II--EEGLRVHQPTLTALQREneVRRVMAEVGL- 414
Cdd:COG3845 67 KPVRIRS--------PRdaialgigM--VHQHF--MLVPNLTVAEnIVlgLEPTKGGRLDRKAARAR--IRELSERYGLd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 415 -DPetrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLdrTVQ--AQILTLLKGLQEKHRlAYIFISHDLQVVRA 491
Cdd:COG3845 133 vDP---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAEGK-SIIFITHKLREVMA 206
|
250
....*....|....*....
gi 502863011 492 LCHQVIVLRQGEVVeqGEC 510
Cdd:COG3845 207 IADRVTVLRRGKVV--GTV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
16-249 |
4.07e-27 |
|
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: 109.25 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSaLSILHLLPSPPvsypQGDILFHGSSLLHadeqtlrgVRGNK-- 93
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL-LRLIAGFETPT----SGEILLDGKDITN--------LPPHKrp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 94 IAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMIAMALLT 173
Cdd:cd03300 74 VNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 174 RPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQ 249
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
302-491 |
4.77e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.34 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA--------SQGEILFDGMPLHRwnrrqmLPVRPR-MQVVFQDPn 372
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKST----LLAAIAgtlspafsASGEVLLNGRRLTA------LPAEQRrIGILFQDD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 sSLNPRLSILQIIEEGLRvhqPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:COG4136 86 -LLFPHLSVGENLAFALP---PTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
5.47e-27 |
|
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: 5.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTqPLLSIDNLSIAFS--KQGETR-TVVSDLSLQIQRGETLALVGESGSGKSvsalSILHL-----LPSppvsypQGDIL 72
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCiygnyLPD------SGSIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 73 FHGSS----LLHADEQTLRGVRGNKIAMIFQ----EPMVSlnplhTLEkQLYEVLsLHRGMRKEAARGEILDCLDRTGIR 144
Cdd:COG4778 70 VRHDGgwvdLAQASPREILALRRRTIGYVSQflrvIPRVS-----ALD-VVAEPL-LERGVDREEARARARELLARLNLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 145 naaKRLSD-FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKL 223
Cdd:COG4778 143 ---ERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAV 218
|
250
....*....|.
gi 502863011 224 ADSVAVMQNGR 234
Cdd:COG4778 219 ADRVVDVTPFS 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
301-508 |
5.70e-27 |
|
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: 108.07 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPnsSLNPRL 379
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGK-----SYQKNIEALRRIGALIEAP--GFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SIlqiiEEGLRVHQptLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:cd03268 88 TA----RENLRLLA--RLLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502863011 460 VQAQILTLLKGLQEKHRLayIFI-SHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03268 161 GIKELRELILSLRDQGIT--VLIsSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
304-508 |
7.90e-27 |
|
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: 107.96 E-value: 7.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 304 NIRFSLR--PGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPNssLN 376
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKST----LLNLIAgfetpQSGRVLINGV-----DVTAAPPADRPVSMLFQENN--LF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIEEGlRVHQPTLTALQREnEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:cd03298 83 AHLTVEQNVGLG-LSPGLKLTAEDRQ-AIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502863011 457 DRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03298 160 DPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
9.62e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.71 E-value: 9.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQGETRTVvsdlSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHGSSLL- 79
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSV----SLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 -HADEQTLRgvrgNKIAMIFQEPmvslNPLhtlEKQLYEvlSLHRGMRKEAARG-EILDCLDRTGIRNAA------KRLS 151
Cdd:PRK14239 77 pRTDTVDLR----KEIGMVFQQP----NPF---PMSIYE--NVVYGLRLKGIKDkQVLDEAVEKSLKGASiwdevkDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMslLFITHNLSIVKKLADSVAVMQ 231
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|...
gi 502863011 232 NGRCVEQNTAAALLNAPQHPYTQ 254
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKETE 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
1.13e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.92 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVsaLS-ILHLLPSPPvsypQGDILFHGSSLlha 81
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKST--ISkILTGLLKPQ----SGEIKIDGITI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGVRgNKIAMIFQEP---MVSLnplhTLEKQLYEVLSLHRGMRKEAARgEILDCLDRTGIRNAAKRLsdfPHQLS 158
Cdd:PRK13632 74 SKENLKEIR-KKIGIIFQNPdnqFIGA----TVEDDIAFGLENKKVPPKKMKD-IIDDLAKKVGMEDYLDKE---PQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVkKLADSVAVMQNGRCVEQ 238
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQ 223
|
....*...
gi 502863011 239 NTAAALLN 246
Cdd:PRK13632 224 GKPKEILN 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-246 |
1.24e-26 |
|
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: 107.52 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqGETRtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpsPPVSypqGDILFHGSSLLHA--DE 83
Cdd:cd03224 1 LEVENLNAGY---GKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL--PPRS---GSIRFDGRDITGLppHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGvrgnkIAMIFQEPMV--SLNPLHTLEkqlyevLSLHRGMRKEAARG--EILDCLDRTgirnaAKRLSDFPHQLSG 159
Cdd:cd03224 72 RARAG-----IGYVPEGRRIfpELTVEENLL------LGAYARRRAKRKARleRVYELFPRL-----KERRKQLAGTLSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
....*..
gi 502863011 240 TAAALLN 246
Cdd:cd03224 215 TAAELLA 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-244 |
1.56e-26 |
|
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: 107.46 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 23 TVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLhadeQTLRGVRgNKIAMIFQEPm 102
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKT-TTIKMLTTLLKPT----SGRATVAGHDVV----REPREVR-RRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 103 vslnplhTLEKQL--YEVLSLH---RGMRKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03265 83 -------SVDDELtgWENLYIHarlYGVPGAERRERIDELLDFVGLLEAADRLVK---TYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 178 LIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAAL 244
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-236 |
1.61e-26 |
|
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: 105.59 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 23 TVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSypqGDILFHGssllhadeqtlrgvrgnkiamifqE 100
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKStlMKILSGLY----KPDS---GEILVDG------------------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 PMVSLNPLHTLekqlyevlslhrgmrkeaargeildcldRTGIRnaakrlsdFPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03216 63 EVSFASPRDAR----------------------------RAGIA--------MVYQLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 181 DEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-246 |
2.66e-26 |
|
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: 106.93 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLLHADEQTLRgvrgNKIAM 96
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLfrfydVS------SGSILIDGQDIREVTLDSLR----RAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 97 IFQEpMVSLNplhtlEKQLYEVlslhRGMRKEAARGEIldcldrtgiRNAAK------RLSDFPHQ-----------LSG 159
Cdd:cd03253 80 VPQD-TVLFN-----DTIGYNI----RYGRPDATDEEV---------IEAAKaaqihdKIMRFPDGydtivgerglkLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQN 239
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
....*..
gi 502863011 240 TAAALLN 246
Cdd:cd03253 218 THEELLA 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-508 |
2.76e-26 |
|
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: 106.69 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhrwnRRQMLPVRPRMQVVFQD 370
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDV----VREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 PnsSLNPRLSILQIIEEGLRVHqpTLTALQRENEVRRVMAEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03265 82 L--SVDDELTGWENLYIHARLY--GVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 451 EPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
297-527 |
2.84e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.79 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMlpvrpRMQVVFQdp 371
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAglehqTSGHIRFHGTDVSRLHARDR-----KVGFVFQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSLNPRLSILQIIEEGLRV----HQPTLTALQREneVRRVMAEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAK--VTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 448 ILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLS 527
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
297-512 |
2.86e-26 |
|
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: 106.44 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTgLALL--RLIASQGEILFDGMPLhrwnRRQMLPVRPRMQVVFQDpnSS 374
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtgELRPTSGTAYINGYSI----RTDRKAARQSLGYCPQF--DA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIEEGLRVHqpTLTALQRENEVRRVMAEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:cd03263 86 LFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 455 SLDRTVQAQILTLLKGLQEKHrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQR 512
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-516 |
3.08e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.09 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSFPIRKGILRRVVDQNA-----------VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA---- 337
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKELLLrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKST----LLKLIAgile 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 338 -SQGEILFDGmplhrwnrrqmlpvrpRMqvvfqdpnSSLnprlsilqiIEEGLRVHqPTLTAlqRENeVRRVMAEVGLDP 416
Cdd:COG1134 78 pTSGRVEVNG----------------RV--------SAL---------LELGAGFH-PELTG--REN-IYLNGRLLGLSR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 417 -ETRHRYP--AEFSG--------------GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAY 479
Cdd:COG1134 121 kEIDEKFDeiVEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TV 199
|
250 260 270
....*....|....*....|....*....|....*..
gi 502863011 480 IFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTA 516
Cdd:COG1134 200 IFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
297-508 |
3.45e-26 |
|
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: 112.91 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHR----WNRRQMlpvrprmQVVFQDP 371
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQhGQVLVDGVDLAIadpaWLRRQM-------GVVLQEN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 ---NSSL--NPRLSILQIIEEGLrVHQPTLT-ALQRENEVRRvmaevGLDPETRHRyPAEFSGGQRQRIAIARALILKPE 445
Cdd:TIGR01846 541 vlfSRSIrdNIALCNPGAPFEHV-IHAAKLAgAHDFISELPQ-----GYNTEVGEK-GANLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 446 LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
302-519 |
3.64e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.94 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLHRWNRRQML-PVRPRMQVVFQDPNSSL 375
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTliqniNAL----LKPTTGTVTVDDITITHKTKDKYIrPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRlSILQIIEEGLRVHQPTLTalQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKMNLD--EVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 456 LDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQ 519
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
301-514 |
3.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGL---ALLrlIASQGEILFDGMPL----HRWNrrqmlpVRPRMQVVFQDPNS 373
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALL--IPSEGKVYVDGLDTsdeeNLWD------IRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 SLnprlsILQIIEEGLrvhqptltALQREN------EVR-RV---MAEVGLDPETRHRyPAEFSGGQRQRIAIARALILK 443
Cdd:PRK13633 97 QI-----VATIVEEDV--------AFGPENlgippeEIReRVdesLKKVGMYEYRRHA-PHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 444 PELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDL-QVVRAlcHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
276-508 |
5.29e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.35 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPIRKgilrrvvdqnaVLKNIRFSLRPGeSLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLh 350
Cdd:cd03264 1 LQLENLTKRYGKKR-----------ALDGVSLTLGPG-MYGLLGPNGAGKTT----LMRILAtltppSSGTIRIDGQDV- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 rwnRRQMLPVRPRMQVVFQDPNSSlnPRLSIlqiiEEGLRvHQPTL---TALQRENEVRRVMAEVGLDpETRHRYPAEFS 427
Cdd:cd03264 64 ---LKQPQKLRRRIGYLPQEFGVY--PNFTV----REFLD-YIAWLkgiPSKEVKARVDEVLELVNLG-DRAKKKIGSLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03264 133 GGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
.
gi 502863011 508 G 508
Cdd:cd03264 211 G 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
297-508 |
6.34e-26 |
|
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: 105.36 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLhrwnrRQMLPV--RPRMQVVFQDPns 373
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDI-----RQLDPAdlRRNIGYVPQDV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 slnpRL---SILQIIEEGLRVHQptltalqrENEVRRVMAEVGLDPETRhRYPAEF-----------SGGQRQRIAIARA 439
Cdd:cd03245 88 ----TLfygTLRDNITLGAPLAD--------DERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 440 LILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
283-516 |
6.80e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.88 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 283 VSFPIRKG--ILRRVV-----DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLh 350
Cdd:TIGR03375 455 LHRPRLQGeiEFRNVSfaypgQETPALDNVSLTIRPGEKVAIIGRIGSGKST----LLKLLLglyqpTEGSVLLDGVDI- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 rwnrRQMLP--VRPRMQVVFQDPnsslnpRL---SILQIIEEGlrvhqptlTALQRENEVRRVMAEVGLDPETRhRYPAE 425
Cdd:TIGR03375 530 ----RQIDPadLRRNIGYVPQDP------RLfygTLRDNIALG--------APYADDEEILRAAELAGVTEFVR-RHPDG 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 F-----------SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVRaLCH 494
Cdd:TIGR03375 591 LdmqigergrslSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTSLLD-LVD 667
|
250 260
....*....|....*....|..
gi 502863011 495 QVIVLRQGEVVEQGECQRVFTA 516
Cdd:TIGR03375 668 RIIVMDNGRIVADGPKDQVLEA 689
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-311 |
8.60e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.12 E-value: 8.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiafsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpsppvsYP-QGDILFHGSSLlhaDEQ 84
Cdd:COG4152 2 LELKGLT----KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL------APdSGEVLWDGEPL---DPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGV------RGnkiamifqepmvsLNPLHTLEKQLYEVLSLHrGMRKEAARGEILDCLDRTGIRNAAKRLSDfphQLS 158
Cdd:COG4152 69 DRRRIgylpeeRG-------------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKVE---ELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VTVQAqILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 238 QNTAAALLNApqhpYTQRLLDSEPAGDPVPLqRDSAPLLNVE--GLSVSFPIRKG-----ILRRVVDQNAVlknIRFSLR 310
Cdd:COG4152 210 SGSVDEIRRQ----FGRNTLRLEADGDAGWL-RALPGVTVVEedGDGAELKLEDGadaqeLLRALLARGPV---REFEEV 281
|
.
gi 502863011 311 P 311
Cdd:COG4152 282 R 282
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-238 |
9.33e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.25 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 8 IDNLSIAFskqGETRtVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSppvsYPQGDILFHGS--SLLHAdeqt 85
Cdd:PRK10851 5 IANIKKSF---GRTQ-VLNDISLDIPSGQMVALLGPSGSGKT-TLLRIIAGLEH----QTSGHIRFHGTdvSRLHA---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 lrgvRGNKIAMIFQ------EPMVSLNPLHTLEkqlyeVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSG 159
Cdd:PRK10851 72 ----RDRKVGFVFQhyalfrHMTVFDNIAFGLT-----VLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGrCVEQ 238
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-486 |
1.02e-25 |
|
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: 110.53 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSEPAGDPVPLQRDSA--------PLLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGK 325
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPAagavglgkPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 326 STTGLALLRLIA-SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPN---SSlnprlsilqiIEEGLRVHQPTLTalqr 401
Cdd:TIGR02868 375 STLLATLAGLLDpLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAHlfdTT----------VRENLRLARPDAT---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 402 ENEVRRVMAEVGLDPETR----------HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL-TLLKG 470
Cdd:TIGR02868 438 DEELWAALERVGLADWLRalpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAA 517
|
250
....*....|....*.
gi 502863011 471 LQEKhrlAYIFISHDL 486
Cdd:TIGR02868 518 LSGR---TVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
254-499 |
1.16e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 110.45 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSE--PAGDPVPLQRDSAPLLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLA 331
Cdd:TIGR02857 298 FAVLDAAprPLAGKAPVTAAPASSLEFSGVSVAYP----------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 332 LLRLI-ASQGEILFDGMPLHRWN----RRQM--LPVRPRMqvvFQDPnsslnprlsilqiIEEGLRVHQPTLTALqrenE 404
Cdd:TIGR02857 368 LLGFVdPTEGSIAVNGVPLADADadswRDQIawVPQHPFL---FAGT-------------IAENIRLARPDASDA----E 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 405 VRRVMAEVGLD------PETRHR----YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEK 474
Cdd:TIGR02857 428 IREALERAGLDefvaalPQGLDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG 507
|
250 260
....*....|....*....|....*
gi 502863011 475 HRLayIFISHDLqVVRALCHQVIVL 499
Cdd:TIGR02857 508 RTV--LLVTHRL-ALAALADRIVVL 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-257 |
1.29e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.69 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHGSSLLHADEQTLRgVRgNKIAMIFQEPmv 103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIE-VR-REVGMVFQYP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 slNPLHTLekQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAA------KRLSDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK14267 95 --NPFPHL--TIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 178 LIADEPTTALDVTVQAQILQLLRELRSELnmSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQRLL 257
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
273-518 |
1.48e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGM 347
Cdd:PRK09536 1 MPMIDVSDLSVEF-----------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLRAIngtltPTAGTVLVAGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 348 PLHRWNRRQmlpVRPRMQVVFQDpnSSLNPRLSILQIIEEGlrvHQPTLTALQRENE-----VRRVMAEVGLDpETRHRY 422
Cdd:PRK09536 66 DVEALSARA---ASRRVASVPQD--TSLSFEFDVRQVVEMG---RTPHRSRFDTWTEtdraaVERAMERTGVA-QFADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFIsHDLQVVRALCHQVIVLRQG 502
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADG 215
|
250
....*....|....*.
gi 502863011 503 EVVEQGECQRVFTAPT 518
Cdd:PRK09536 216 RVRAAGPPADVLTADT 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
298-507 |
1.78e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.48 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPR-MQVVFQdp 371
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKST----LLAILAglddgSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSLNPRLSILQiieeglRVHQPTLTALQRENEVRR----VMAEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK10584 96 SFMLIPTLNALE------NVELPALLRGESSRQSRNgakaLLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 448 ILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQ 507
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
301-508 |
1.92e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.05 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQmlpvRPRMQVVFQDPNSSLNPRL 379
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHE----RARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SIlqiiEEGLRVhqpTLTALQREnEVRRVMAEV-GLDP---ETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:cd03224 91 TV----EENLLL---GAYARRRA-KRKARLERVyELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502863011 456 LDRTVQAQILTLLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-216 |
2.04e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.48 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 18 QGETR-TVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTLRGVRGNKIAM 96
Cdd:PRK10584 18 QGEHElSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQMDEEARAKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 97 IFQEPMVsLNPLHTLEKqlYEVLSLHRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:PRK10584 93 VFQSFML-IPTLNALEN--VELPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHN 216
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
289-505 |
4.02e-25 |
|
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: 108.76 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 289 KGILRRVVDQNAvLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEILFDGMPLHRWNRRQMlpvr 361
Cdd:TIGR02633 5 KGIVKTFGGVKA-LDGIDLEVRPGECVGLCGENGAGKST----LMKILSGvyphgtwDGEIYWSGSPLKASNIRDT---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 362 PRMQVVFQDPNSSLNPRLSILQ-------IIEEGLRVHQPTLTalqreNEVRRVMAEVGLDPETRHRYPAEFSGGQRQRI 434
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAEniflgneITLPGGRMAYNAMY-----LRAKNLLRELQLDADNVTRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 435 AIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-245 |
4.02e-25 |
|
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: 103.85 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 12 SIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPpVSYPQGDILFHGSSLLHADEQTLRgvrg 91
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRF-YDVDSGRILIDGHDVRDYTLASLR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 92 NKIAMIFQEPMVSLNPLHtlEKQLYEvlslhrgmRKEAARGEILDCLDrtgIRNAAKRLSDFPH-----------QLSGG 160
Cdd:cd03251 76 RQIGLVSQDVFLFNDTVA--ENIAYG--------RPGATREEVEEAAR---AANAHEFIMELPEgydtvigergvKLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNT 240
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
....*
gi 502863011 241 AAALL 245
Cdd:cd03251 220 HEELL 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-248 |
4.78e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.04 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLL 79
Cdd:COG4559 1 MLEAENLSVRLGG----RTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HADEQTLRGVRgnkiAMIFQEpmVSLN-PLHTLEkqlyeVLSLHR---GMRKEAARGEILDCLDRTGIRNAAKRlsDFPh 155
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFTVEE-----VVALGRaphGSSAAQDRQIVREALALVGLAHLAGR--SYQ- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALL-------TRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVA 228
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRIL 211
|
250 260
....*....|....*....|
gi 502863011 229 VMQNGRCVEQNTAAALLNAP 248
Cdd:COG4559 212 LLHQGRLVAQGTPEEVLTDE 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
301-514 |
5.35e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.32 E-value: 5.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHrWNRRQMLPVRPRMQVVFQDPNSSLnprl 379
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQI---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 sILQIIEEGLRVHQPTLTALQREnEVRRVMAEVGLDPETRHRY-PAE-FSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK13638 91 -FYTDIDSDIAFSLRNLGVPEAE-ITRRVDEALTLVDAQHFRHqPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 458 RTVQAQILTLLKGLQEKHRLAYIfISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-257 |
5.41e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLlhADEQT-LRGVRgNKIAMIFQEPmvsl 105
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK--PTS---GKIIIDGVDI--TDKKVkLSDIR-KKVGLVFQYP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 106 nplhtlEKQLYEvlslhRGMRKEAARGEILDCLDRTGIRNAAKR--------LSDF----PHQLSGGERQRVMIAMALLT 173
Cdd:PRK13637 93 ------EYQLFE-----ETIEKDIAFGPINLGLSEEEIENRVKRamnivgldYEDYkdksPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 174 RPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAAL--------- 244
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfkevetles 241
|
250
....*....|....*
gi 502863011 245 --LNAPQHPYTQRLL 257
Cdd:PRK13637 242 igLAVPQVTYLVRKL 256
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-508 |
5.44e-25 |
|
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: 103.46 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDP 371
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPrfydvDSGRILIDGHDVRDYTLASL---RRQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 ---NSSlnprlsilqiIEEGLRVHQPTLTALQRENEVRRVMA-------EVGLDPETRHRyPAEFSGGQRQRIAIARALI 441
Cdd:cd03251 86 flfNDT----------VAENIAYGRPGATREEVEEAARAANAhefimelPEGYDTVIGER-GVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 442 LKPELIILDEPTSSLD----RTVQAQILTLLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03251 155 KDPPILILDEATSALDteseRLVQAALERLMKN-----RTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-255 |
5.47e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVSYPQ--GDILFHGSSLLHADEQTLRgvrgNKIAMIFQ 99
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKS-TLLKVLNRLIEIYDSKIKvdGKVLYFGKDIFQIDAIKLR----KEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 100 EPmvslNPLHTLE--KQLYEVLSLHRGMRKEAARGEILDCLDRTGI-RNAAKRLSDFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:PRK14246 98 QP----NPFPHLSiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQR 255
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
302-514 |
5.57e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.40 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS-QGEILFDGmplHRWNRRQMLPVRPRMQVVFQDPNSSLnprls 380
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDG---ELLTAENVWNLRRKIGMVFQNPDNQF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 381 ILQIIEEGLRVHQPTlTALQRENEVRRV----MAEVGLDPETRHryPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13642 95 VGATVEDDVAFGMEN-QGIPREEMIKRVdealLAVNMLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 457 DRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
5.89e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 102.56 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFskqGEtRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL-HLLPspPVSypqGDILFHGSSLLHAD 82
Cdd:COG4133 1 MMLEAENLSCRR---GE-RLLFSGLSFTLAAGEALALTGPNGSGKT-TLLRILaGLLP--PSA---GEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRgvrgnKIAMIFQEPMV--SLNPLhtlekqlyEVLSLHRGMRK-EAARGEILDCLDRTGIrnaAKRLSDFPHQLSG 159
Cdd:COG4133 71 EDYRR-----RLAYLGHADGLkpELTVR--------ENLRFWAALYGlRADREAIDEALEAVGL---AGLADLPVRQLSA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMsLLFITH 215
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTH 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-245 |
7.27e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.51 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 13 IAFSKQGeTRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTLRgvrgN 92
Cdd:PRK13657 340 VSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPQ----SGRILIDGTDIRTVTRASLR----R 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 93 KIAMIFQEPMVslnplhtLEKQLYEVLSLHRG------MRKEAARGEILDCLDRTGIR---NAAKRLSdfphQLSGGERQ 163
Cdd:PRK13657 410 NIAVVFQDAGL-------FNRSIEDNIRVGRPdatdeeMRAAAERAQAHDFIERKPDGydtVVGERGR----QLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAA 243
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
..
gi 502863011 244 LL 245
Cdd:PRK13657 556 LV 557
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
284-517 |
8.93e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.57 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 284 SFPIRKGILRRVVDqNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL-HRwnrrqm 357
Cdd:PRK11432 5 NFVVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDGEDVtHR------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 358 lPVRPR-MQVVFQdpNSSLNPRLSILQIIEEGLRVHQptLTALQRENEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAI 436
Cdd:PRK11432 74 -SIQQRdICMVFQ--SYALFPHMSLGENVGYGLKMLG--VPKEERKQRVKEALELVDLAG-FEDRYVDQISGGQQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 437 ARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTA 516
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
.
gi 502863011 517 P 517
Cdd:PRK11432 228 P 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-504 |
1.06e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.44 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHade 83
Cdd:PRK15439 10 PLLCARSISKQYSGV----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-----SGTLEIGGNPCAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 qtLRGVRGNK--IAMIFQEPMVSLNpLHTLEKQLYEVLSLHRGMRKEAARGEILDC-LDrtgirnaakrLSDFPHQLSGG 160
Cdd:PRK15439 78 --LTPAKAHQlgIYLVPQEPLLFPN-LSVKENILFGLPKRQASMQKMKQLLAALGCqLD----------LDSSAGSLEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCV---- 236
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIAlsgk 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 237 -EQNTAAALLNA-------PQHPYTQRLLDSEPAGDPVplQRDSAPLLNVEGLSvsfpirkgilrrvvdqNAVLKNIRFS 308
Cdd:PRK15439 224 tADLSTDDIIQAitpaareKSLSASQKLWLELPGNRRQ--QAAGAPVLTVEDLT----------------GEGFRNISLE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 309 LRPGESLGLVGESGSGKSTTGLAL--LRLIASqGEILFDGMPLHRWNRRQ-------MLPVRPRMQVVFQDPNSSLNPrl 379
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLygLRPARG-GRIMLNGKEINALSTAQrlarglvYLPEDRQSSGLYLDAPLAWNV-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 silqiieEGLRVHQPTL-TALQRENEV-RRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK15439 363 -------CALTHNRRGFwIKPARENAVlERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 502863011 458 RTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-245 |
1.08e-24 |
|
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: 102.30 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 13 IAFSkQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsyPQ-GDILFHGSSLLHADEQTLRgvrg 91
Cdd:cd03254 8 VNFS-YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------PQkGQILIDGIDIRDISRKSLR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 92 NKIAMIFQEPMVslnplhtLEKQLYEVLSLHrgmRKEAARGEILDCLDRTGIRNAAKRL--------SDFPHQLSGGERQ 163
Cdd:cd03254 77 SMIGVVLQDTFL-------FSGTIMENIRLG---RPNATDEEVIEAAKEAGAHDFIMKLpngydtvlGENGGNLSQGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAA 243
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
..
gi 502863011 244 LL 245
Cdd:cd03254 224 LL 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
305-510 |
1.20e-24 |
|
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: 101.86 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 305 IRFSL--RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPNssLNP 377
Cdd:TIGR01277 15 MEFDLnvADGEIVAIMGPSGAGKST----LLNLIAgfiepASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENN--LFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 378 RLSILQIIEEGLRvhqPTL--TALQREnEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:TIGR01277 84 HLTVRQNIGLGLH---PGLklNAEQQE-KVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 456 LDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
272-508 |
1.29e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.60 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFPIRkgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG 346
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQ---------PQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLtrawdPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNRRQMlpvRPRMQVVFQdpnsslnpRLSIL-QIIEEGLRVHQPTLTalqrENEVRRVMAEVGLDP--ETRHRYP 423
Cdd:PRK11160 402 QPIADYSEAAL---RQAISVVSQ--------RVHLFsATLRDNLLLAAPNAS----DEALIEVLQQVGLEKllEDDKGLN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 424 A-------EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLL-KGLQEKhrlAYIFISHDLqvvRALCH- 494
Cdd:PRK11160 467 AwlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLaEHAQNK---TVLMITHRL---TGLEQf 540
|
250
....*....|....*
gi 502863011 495 -QVIVLRQGEVVEQG 508
Cdd:PRK11160 541 dRICVMDNGQIIEQG 555
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-236 |
1.49e-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: 101.68 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQ 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKT-TTLRMLAGLLEPD----AGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLR--GVRGNKIAmifqepmvsLNPLHTLEKQLYEVLSLHrGMRKEAARGEILDCLDRTGIRN-AAKRLSDFphqlSGGE 161
Cdd:cd03266 76 ARRrlGFVSDSTG---------LYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEElLDRRVGGF----STGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-271 |
1.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 25 VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHGSSllhaDEQTLRGVRgNKIAMIFQEPmvs 104
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT----KDKYIRPVR-KRIGMVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 lnplhtlEKQLYEVlSLHR---------GMRKEAARGEILDCLDRTGI-RNAakrLSDFPHQLSGGERQRVMIAMALLTR 174
Cdd:PRK13646 95 -------ESQLFED-TVEReiifgpknfKMNLDEVKNYAHRLLMDLGFsRDV---MSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 175 PELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNApqhpyTQ 254
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD-----KK 238
|
250
....*....|....*...
gi 502863011 255 RLLDSEPA-GDPVPLQRD 271
Cdd:PRK13646 239 KLADWHIGlPEIVQLQYD 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-240 |
2.35e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 25 VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHAdEQTLRGVRGNkIAMIFQEPMVS 104
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK--PSS---GRILFDGKPIDYS-RKGLMKLRES-VGMVFQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 LNPLHTLEKQLYEVLSLhrGMRKEAARGEILDCLDRTGIrnaaKRLSDFP-HQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK13636 95 LFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 184 TTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
26-234 |
2.58e-24 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 100.79 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 26 SDLSLQIQRGETLALVGESGSGKSvSALSILH--LLPSppvsypQGDILFHGSSLLHADEQTLRGVRgNKIAMIFQEPMV 103
Cdd:TIGR02673 19 HDVSLHIRKGEFLFLTGPSGAGKT-TLLKLLYgaLTPS------RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNplhtleKQLYE--VLSLH-RGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:TIGR02673 91 LPD------RTVYEnvALPLEvRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 181 DEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
256-508 |
2.61e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 256 LLDSEPAGDPVPlqrDSAPLLNVEGL------SVSFPIRkgilRRVVDqnavlkNIRFSLRPGESLGLVGESGSGKSTTg 329
Cdd:PRK13657 312 VEDAVPDVRDPP---GAIDLGRVKGAvefddvSFSYDNS----RQGVE------DVSFEAKPGQTVAIVGPTGAGKSTL- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 330 LALLRLI--ASQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDP---NSSlnprlsilqiIEEGLRVHQPTLTalqrENE 404
Cdd:PRK13657 378 INLLQRVfdPQSGRILIDGTDIRTVTRASL---RRNIAVVFQDAglfNRS----------IEDNIRVGRPDAT----DEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 405 VRRVMA-----------EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLLK 469
Cdd:PRK13657 441 MRAAAEraqahdfierkPDGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILILDEATSALDveteAKVKAALDELMK 519
|
250 260 270
....*....|....*....|....*....|....*....
gi 502863011 470 GlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PRK13657 520 G-----RTTFI-IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
298-504 |
2.75e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.06 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmlpVRPRMQVVFQDpn 372
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLAgletpSAGELLAGTAPLAE--------AREDTRLMFQD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SSLNPRLSILQIIEEGLRVHQptltalqrENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQW--------RDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
276-508 |
3.18e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 101.30 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSfpirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDGMPLhrw 352
Cdd:COG0396 1 LEIKNLHVS-----------VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKYEVTSGSILLDGEDI--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 nrrQMLPV--RPRMQV--VFQDP-------NSSLnprlsiLQIIEEGLRvhQPTLTALQRENEVRRVMAEVGLDPETRHR 421
Cdd:COG0396 67 ---LELSPdeRARAGIflAFQYPveipgvsVSNF------LRTALNARR--GEELSAREFLKLLKEKMKELGLDEDFLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 422 YPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQIltllKGLQEKHRlAYIFISHD---LQVVRAlc 493
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidalRIVAEGV----NKLRSPDR-GILIITHYqriLDYIKP-- 208
|
250
....*....|....*
gi 502863011 494 HQVIVLRQGEVVEQG 508
Cdd:COG0396 209 DFVHVLVDGRIVKSG 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
298-517 |
3.66e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 106.34 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWnrrQMLPVRPRMQVVFQDP- 371
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKST----LLSLIqrhfdVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPf 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 --------NSSLNPRLSILQIIEEGLR---VHQPTLTALQ-RENEV--RRVMaevgldpetrhrypaeFSGGQRQRIAIA 437
Cdd:PRK10789 400 lfsdtvanNIALGRPDATQQEIEHVARlasVHDDILRLPQgYDTEVgeRGVM----------------LSGGQKQRISIA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 438 RALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQvvrAL--CHQVIVLRQGEVVEQGECQRVFT 515
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLS---ALteASEILVMQHGHIAQRGNHDQLAQ 538
|
..
gi 502863011 516 AP 517
Cdd:PRK10789 539 QS 540
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-512 |
3.68e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.81 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 306 RFSL--RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMplhrwNRRQMLPVRPRMQVVFQDPNssLNPR 378
Cdd:PRK10771 17 RFDLtvERGERVAILGPSGAGKST----LLNLIAgfltpASGSLTLNGQ-----DHTTTPPSRRPVSMLFQENN--LFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 379 LSILQIIeeGLRVHqP--TLTALQREnEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK10771 86 LTVAQNI--GLGLN-PglKLNAAQRE-KLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 457 DRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQR 512
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-257 |
3.68e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.58 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGS----------SLLHADEQTLRGVRgNK 93
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGSIVVNGQtinlvrdkdgQLKVADKNQLRLLR-TR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 94 IAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKrlSDFPHQLSGGERQRVMIAMALLT 173
Cdd:PRK10619 94 LTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 174 RPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYT 253
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
....
gi 502863011 254 QRLL 257
Cdd:PRK10619 249 QQFL 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-247 |
4.30e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpSPPVSYPQGDILFHGSSLLHADE 83
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRAL-SGELSPDSGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRgnkiAMIFQEPMVSLnPLhTLEkqlyEVLSL----HRGMRKEAARgEILDCLDRTGIRNAAKRlsDFPhQLSG 159
Cdd:PRK13548 72 AELARRR----AVLPQHSSLSF-PF-TVE----EVVAMgrapHGLSRAEDDA-LVAAALAQVDLAHLAGR--DYP-QLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMAL--LTRPE----LLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNG 233
Cdd:PRK13548 138 GEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
250
....*....|....
gi 502863011 234 RCVEQNTAAALLNA 247
Cdd:PRK13548 218 RLVADGTPAEVLTP 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
269-526 |
4.56e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 269 QRDSAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIL 343
Cdd:PRK11607 13 RKALTPLLEIRNLTKSF-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAgfeqpTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 344 FDGMPLhrwnrRQMLPVRPRMQVVFQdpNSSLNPRLSILQIIEEGLRvhQPTLTALQRENEVRRVMAEVGLDpETRHRYP 423
Cdd:PRK11607 78 LDGVDL-----SHVPPYQRPINMMFQ--SYALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQ-EFAKRKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
250 260
....*....|....*....|...
gi 502863011 504 VVEQGECQRVFTAPTQSYTRQLL 526
Cdd:PRK11607 228 FVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-527 |
4.63e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.07 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 285 FPIRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA------SQGEILFDGMPLHRwnrRQML 358
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYS---PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 359 PVRPRMQV--VFQDPNSSlnPRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAEVGLDPETRHR---YPAEFSGGQRQR 433
Cdd:PRK14267 80 PIEVRREVgmVFQYPNPF--PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 434 IAIARALILKPELIILDEPTSSLDRTVQAQILTLLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
250
....*....|....
gi 502863011 514 FTAPTQSYTRQLLS 527
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
301-508 |
4.70e-24 |
|
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: 98.92 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRWNRRqmlpVRPRMQVVFQDP---NSSL 375
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTgdLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPylfDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 nprlsilqiieeglrvhqptltalqRENEVRRvmaevgldpetrhrypaeFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:cd03247 92 -------------------------RNNLGRR------------------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 456 LDRTVQAQIL-TLLKGLQEKhrlAYIFISHDLQVVRALcHQVIVLRQGEVVEQG 508
Cdd:cd03247 129 LDPITERQLLsLIFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
302-518 |
5.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.02 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-----LIASQGEI-LFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKST----LLQhlnglLQPTSGTVtIGERVITAGKKNKKLKPLRKKVGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRlSILQIIEEG-LRVHQPTLTALQReneVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK13634 99 FEE-TVEKDICFGpMNFGVSEEDAKQK---AREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 455 SLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
16-238 |
5.91e-24 |
|
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: 99.64 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpSPPVSypqGDILFhgssllhaDEQTLRGVRGNK-- 93
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL--EEPTS---GRIYI--------GGRDVTDLPPKDrd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 94 IAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAARGeildcldrtgIRNAAKRL------SDFPHQLSGGERQRVMI 167
Cdd:cd03301 74 IAMVFQN--YALYPHMTVYDNIAFGLKLRKVPKDEIDER----------VREVAELLqiehllDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 168 AMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRcVEQ 238
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-512 |
6.33e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 104.87 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 26 SDLSLQIQRGETLALVGESGSGKS--VSALSILHllpsPPVSYpQGDILFHGssllhaDEQTLRGVRGNK---IAMIFQE 100
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKStlMKVLSGVY----PHGSY-EGEILFDG------EVCRFKDIRDSEalgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 pmVSLNPLHTLEKQLYevlslhrgMRKEAARGEILDcLDRTGIRNAA--KR--LSDFPHQLSG----GERQRVMIAMALL 172
Cdd:NF040905 87 --LALIPYLSIAENIF--------LGNERAKRGVID-WNETNRRAREllAKvgLDESPDTLVTdigvGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 173 TRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQntaaalLNAPQHPY 252
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET------LDCRADEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 253 TQ---------RLLDSE-PAGDPvplqRDSAPLLNVEGLSVSFPIRKGilRRVVDqnavlkNIRFSLRPGESLGLVGESG 322
Cdd:NF040905 229 TEdriirgmvgRDLEDRyPERTP----KIGEVVFEVKNWTVYHPLHPE--RKVVD------DVSLNVRRGEIVGIAGLMG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 323 SGKstTGLALL-------RLIAsqGEILFDGMPLHRWNRRQmlPVRPRMQVVFQDpnsslnpRLSILQIIEEGLRvHQPT 395
Cdd:NF040905 297 AGR--TELAMSvfgrsygRNIS--GTVFKDGKEVDVSTVSD--AIDAGLAYVTED-------RKGYGLNLIDDIK-RNIT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 396 LTALQR--------ENEVRRVmAEvGLDPETRHRYPAEF------SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQ 461
Cdd:NF040905 363 LANLGKvsrrgvidENEEIKV-AE-EYRKKMNIKTPSVFqkvgnlSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAK 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502863011 462 AQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVeqGECQR 512
Cdd:NF040905 441 YEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRIT--GELPR 488
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
9-240 |
9.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.93 E-value: 9.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 9 DNLSIAFSK--QGETRTVVSDLSLQIQRGETLALVGESGSGKSVSA--LSILhLLPSPPVSYPQGdilfhgssLLHADEQ 84
Cdd:PRK13633 8 KNVSYKYESneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkhMNAL-LIPSEGKVYVDG--------LDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRgNKIAMIFQEPM-----------VSLNPlhtlekqlyEVLslhrGMRKEAARGEILDCLDRTGIRNAAKRLsdf 153
Cdd:PRK13633 79 NLWDIR-NKAGMVFQNPDnqivativeedVAFGP---------ENL----GIPPEEIRERVDESLKKVGMYEYRRHA--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQNG 233
Cdd:PRK13633 142 PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSG 220
|
....*..
gi 502863011 234 RCVEQNT 240
Cdd:PRK13633 221 KVVMEGT 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
298-508 |
1.23e-23 |
|
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: 98.89 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS-QGEILFDGMPLHRWNRRQM--LPvrprmqvvfqdPNSS 374
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGKPLDIAARNRIgyLP-----------EERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIeeglrVHQPTLTALQRE---NEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:cd03269 81 LYPKMKVIDQL-----VYLAQLKGLKKEearRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
301-516 |
1.28e-23 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 104.40 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhrwnrRQMLP--VRPRMQVVFQDPN---SS 374
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYdPQSGRILLDGVDL-----RQLDPaeLRARMALVPQDPVlfaAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 lnprlsilqiIEEGLRVHQPTLTALQRENEVRRVMAE--VGLDPETRHRYPAE----FSGGQRQRIAIARALILKPELII 448
Cdd:TIGR02204 430 ----------VMENIRYGRPDATDEEVEAAARAAHAHefISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 449 LDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFTA 516
Cdd:TIGR02204 500 LDEATSALDAESEQLVQQALETLM-KGRTTLI-IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
275-506 |
1.56e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.77 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFPIRKgilrrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPL 349
Cdd:PRK11248 1 MLQISHLYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAgfvpyQHGSITLDGKPV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRwnrrqmlPVRPRmQVVFQdpNSSLNPRLSILQIIEEGLRVhqPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGG 429
Cdd:PRK11248 66 EG-------PGAER-GVVFQ--NEGLLPWRNVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR--QGEVVE 506
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-504 |
1.59e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.93 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFS--KqgetrtVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSppvSYP--QGDILFHGss 77
Cdd:PRK10762 1 MQALLQLKGIDKAFPgvK------ALSGAALNVYPGRVMALVGENGAGKS----TMMKVLTG---IYTrdAGSILYLG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 llhaDEQTLRGVRGNK---IAMIFQEpmVSLNPLHTLEKQLY---EVLS-----LHRGMRKEAARgeildCLDRTGIRNA 146
Cdd:PRK10762 66 ----KEVTFNGPKSSQeagIGIIHQE--LNLIPQLTIAENIFlgrEFVNrfgriDWKKMYAEADK-----LLARLNLRFS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 147 AKRLSDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADS 226
Cdd:PRK10762 135 SDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 227 VAVMQNGRCVEQNTAAALLN------------APQHPYtqrlLDSEPAGdpvplqrdsaPLLNVEGLSVSfpirkGIlrr 294
Cdd:PRK10762 211 VTVFRDGQFIAEREVADLTEdsliemmvgrklEDQYPR----LDKAPGE----------VRLKVDNLSGP-----GV--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 295 vvdqnavlKNIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEILFDGMPLHrwnrrqmlPVRPrmqvvfQ 369
Cdd:PRK10762 269 --------NDVSFTLRKGEILGVSGLMGAGRT----ELMKVLygalpRTSGYVTLDGHEVV--------TRSP------Q 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DpnsSLNPrlSILQIIEE--------GLRVHQP-TLTAL----------QRENEVRRVMAEVGL----DPeTRHRYPAEF 426
Cdd:PRK10762 323 D---GLAN--GIVYISEDrkrdglvlGMSVKENmSLTALryfsraggslKHADEQQAVSDFIRLfnikTP-SMEQAIGLL 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-234 |
1.75e-23 |
|
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: 98.73 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQgeTRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLlh 80
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKT----TTLKMLtgelrPT------SGTAYINGYSI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 adeQTLRGVRGNKIAMIFQEPMvsLNPLHTLEKQLYeVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSdfpHQLSGG 160
Cdd:cd03263 67 ---RTDRKAARQSLGYCPQFDA--LFDELTVREHLR-FYARLKGLPKSEIKEEVELLLRVLGLTDKANKRA---RTLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03263 138 MKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-230 |
1.88e-23 |
|
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: 103.91 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPPVSYpQGDILFHGSSLLHADEQT 85
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS----TLLNLLLGFVDPT-EGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGvrgnKIAMIFQEPmvslnplHTLEKQLYEVLSLHRgmrKEAARGEILDCLDRTGI--------RNAAKRLSDFPHQL 157
Cdd:TIGR02857 394 WRD----QIAWVPQHP-------FLFAGTIAENIRLAR---PDASDAEIREALERAGLdefvaalpQGLDTPIGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSiVKKLADSVAVM 230
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA-LAALADRIVVL 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
300-508 |
1.88e-23 |
|
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: 97.62 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 300 AVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-------GEILFDGMPLHRWNrrqmlpVRPRMQVVFQDpn 372
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKST----LLNALAGRrtglgvsGEVLINGRPLDKRS------FRKIIGYVPQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 sslnprlsilqiieeglRVHQPTLTalqreneVRRVMaevgldpetrhRYPAE---FSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03213 91 -----------------DILHPTLT-------VRETL-----------MFAAKlrgLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 450 DEPTSSLDRTVQAQILTLLKGLQEKHRLAyIFISHDL-QVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTI-ICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
276-508 |
2.13e-23 |
|
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: 97.87 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVsfpirkgilRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPL 349
Cdd:cd03369 7 IEVENLSV---------RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGidistIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRwnrrqmlpVRPRMQVVFQDP-------NSSLNP--RLSILQIIeEGLRVhqptltalqrenevrrvmAEVGLDpetrh 420
Cdd:cd03369 78 ED--------LRSSLTIIPQDPtlfsgtiRSNLDPfdEYSDEEIY-GALRV------------------SEGGLN----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 421 rypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKglQEKHRLAYIFISHDLQVVrALCHQVIVLR 500
Cdd:cd03369 126 -----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTI-IDYDKILVMD 197
|
....*...
gi 502863011 501 QGEVVEQG 508
Cdd:cd03369 198 AGEVKEYD 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-248 |
2.24e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQTLRgvrgNKIAMIFQEPmv 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ--PTG---GQVLLDGVPLVQYDHHYLH----RQVALVGQEP-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 slnplhtlekQLYEvlslhRGMRKEAARGeiLDCLDRTGIRNAAKR------LSDFPH-----------QLSGGERQRVM 166
Cdd:TIGR00958 565 ----------VLFS-----GSVRENIAYG--LTDTPDEEIMAAAKAanahdfIMEFPNgydtevgekgsQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 167 IAMALLTRPELLIADEPTTALDvtvqAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAALLN 246
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 502863011 247 AP 248
Cdd:TIGR00958 703 DQ 704
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-255 |
2.27e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.22 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqGETRtVVSDLSLQIQRGETLALVGESGSGKSvSALSILH----LLPSPPVSypqGDILFHGSSLLHA 81
Cdd:PRK14247 4 IEIRDLKVSF---GQVE-VLDGVNLEIPDNTITALMGPSGSGKS-TLLRVFNrlieLYPEARVS---GEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRgvrgNKIAMIFQEPmvslNPLHTLE--KQLYEVLSLHRGMR-KEAARGEILDCLDRTGIRNAAKRLSDFPH-QL 157
Cdd:PRK14247 76 DVIELR----RRVQMVFQIP----NPIPNLSifENVALGLKLNRLVKsKKELQERVRWALEKAQLWDEVKDRLDAPAgKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
250
....*....|....*...
gi 502863011 238 QNTAAALLNAPQHPYTQR 255
Cdd:PRK14247 226 WGPTREVFTNPRHELTEK 243
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
301-508 |
2.32e-23 |
|
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: 104.26 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGlallRLIA-----SQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDpnssl 375
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIPREEIPREV---LANSVAMVDQD----- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 nprlsILQI---IEEGLRVHQPTLTalqrENEVRRVMAEVGLDPETRHR---YPAE-------FSGGQRQRIAIARALIL 442
Cdd:TIGR03796 562 -----IFLFegtVRDNLTLWDPTIP----DADLVRACKDAAIHDVITSRpggYDAElaegganLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 443 KPELIILDEPTSSLDRTVQAQILTLLKglqeKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-244 |
2.40e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.81 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLlhaDEQ 84
Cdd:PRK13650 4 IIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGQIIIDGDLL---TEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRgNKIAMIFQEP-------MVSLNPLHTLEKQlyevlslhrGMRKEAARGEILDCLDRTGIRNAAKRLsdfPHQL 157
Cdd:PRK13650 75 NVWDIR-HKIGMVFQNPdnqfvgaTVEDDVAFGLENK---------GIPHEEMKERVNEALELVGMQDFKERE---PARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVkKLADSVAVMQNGRCVE 237
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
....*..
gi 502863011 238 QNTAAAL 244
Cdd:PRK13650 221 TSTPREL 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-247 |
3.20e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 103.26 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 13 IAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPpVSYPQGDILFHGSSLLHADEQTLRgvrgN 92
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRF-YEPDSGQILLDGHDLADYTLASLR----R 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 93 KIAMIFQEpmvslnpLHTLEKQLYEvlSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQ--------LSGGERQR 164
Cdd:TIGR02203 407 QVALVSQD-------VVLFNDTIAN--NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAAL 244
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
...
gi 502863011 245 LNA 247
Cdd:TIGR02203 555 LAR 557
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
260-502 |
4.00e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 260 EPAGDPVPLQRDSAPLLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-- 337
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRTP----------DGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRAIAgl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 338 ---SQGEILfdgMPLHRwnrRQM-LPVRP-------RMQVVFQDPNSSLNprlsilqiieeglrvhqptltalqrENEVR 406
Cdd:COG4178 413 wpyGSGRIA---RPAGA---RVLfLPQRPylplgtlREALLYPATAEAFS-------------------------DAELR 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 407 RVMAEVGLDP-----ETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKglQEKHRLAYIF 481
Cdd:COG4178 462 EALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVIS 539
|
250 260
....*....|....*....|.
gi 502863011 482 ISHDlQVVRALCHQVIVLRQG 502
Cdd:COG4178 540 VGHR-STLAAFHDRVLELTGD 559
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-261 |
4.96e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.53 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:COG3839 4 LELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKS----TLLRMIagledPT------SGEILIGGRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTlrgvRGnkIAMIFQEPMvslnplhtlekqLYEVLSLH---------RGMRKEAARGEILDCLDRTGIRNAAKRLs 151
Cdd:COG3839 70 LPPKD----RN--IAMVFQSYA------------LYPHMTVYeniafplklRKVPKAEIDRRVREAAELLGLEDLLDRK- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 dfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHN----LSivkkLADSV 227
Cdd:COG3839 131 --PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRI 204
|
250 260 270
....*....|....*....|....*....|....*
gi 502863011 228 AVMQNGRcVEQN-TAAALLNAPQHPYTQRLLDSEP 261
Cdd:COG3839 205 AVMNDGR-IQQVgTPEELYDRPANLFVAGFIGSPP 238
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-262 |
5.45e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.40 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSL 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIagflaPS------SGEITLDGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LH--ADeqtlRGVrgnkiamIFQEP--MVSLNPLHTLEkqlyevLSLH-RGMRKEAARGEILDCLDRTGIRNAAKRlsdF 153
Cdd:COG4525 72 TGpgAD----RGV-------VFQKDalLPWLNVLDNVA------FGLRlRGVPKAERRARAEELLALVGLADFARR---R 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQN- 232
Cdd:COG4525 132 IWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPg 211
|
250 260 270
....*....|....*....|....*....|.
gi 502863011 233 -GRCVEQNTAaallnapqhPYTQRLLDSEPA 262
Cdd:COG4525 212 pGRIVERLEL---------DFSRRFLAGEDA 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-528 |
5.49e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.63 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 317 LVGESGSGKSTTGLALLRL------IASQGEILFDGMPLhrWNRRQMLPVRPRMQVVFQDPNSSlnpRLSILQIIEEGLR 390
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF---PMSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 391 VHQptltaLQRENEVRRV----MAEVGLDPETRHRY---PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQ 463
Cdd:PRK14271 127 AHK-----LVPRKEFRGVaqarLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 464 ILTLLKGLQEkhRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLLSA 528
Cdd:PRK14271 202 IEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-512 |
6.10e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.91 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSsllha 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGV----KALDDISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPD----AGSILIDGQ----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 dEQTLRGVR---GNKIAMIFQEpmvslnpLHTL-EKQLYEVLSL----HRG--MRKEAARGEILDCLDRTGIR-NAAKRL 150
Cdd:PRK11288 67 -EMRFASTTaalAAGVAIIYQE-------LHLVpEMTVAENLYLgqlpHKGgiVNRRLLNYEAREQLEHLGVDiDPDTPL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 151 SDfphqLSGGERQRVMIAMALLtRPELLIA-DEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAV 229
Cdd:PRK11288 139 KY----LSIGQRQMVEIAKALA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 230 MQNGRCVEQNTAAALLNAPQ-------------HPYTQRlldsePAGDpVPLQRDsapllNVEGLSVSFPirkgilrrvv 296
Cdd:PRK11288 213 FKDGRYVATFDDMAQVDRDQlvqamvgreigdiYGYRPR-----PLGE-VRLRLD-----GLKGPGLREP---------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 dqnavlknIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEILFDGMPLHRWNRRQmlPVRPRMQVVFQDP 371
Cdd:PRK11288 272 --------ISFSVRAGEIVGLFGLVGAGRS----ELMKLLygatrRTAGQVYLDGKPIDIRSPRD--AIRAGIMLCPEDR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NS-SLNPRLSILQIIEEGLRVHQPTLTAL-----QRENEVRRVMAevgLDPETRHRYPA--EFSGGQRQRIAIARALILK 443
Cdd:PRK11288 338 KAeGIIPVHSVADNINISARRHHLRAGCLinnrwEAENADRFIRS---LNIKTPSREQLimNLSGGNQQKAILGRWLSED 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 444 PELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVeqGECQR 512
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-240 |
6.70e-23 |
|
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: 96.79 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGETrtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQT 85
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRgvrgNKIAMIFQEPMV-------SLNPLHtlekqlyevlslhrgmrkEAARGEILDCLDRTGIRNAAKRLS---DFPH 155
Cdd:cd03244 76 LR----SRISIIPQDPVLfsgtirsNLDPFG------------------EYSDEELWQALERVGLKEFVESLPgglDTVV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVM 230
Cdd:cd03244 134 eeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVL 210
|
250
....*....|
gi 502863011 231 QNGRCVEQNT 240
Cdd:cd03244 211 DKGRVVEFDS 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-249 |
8.04e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.97 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFskqGETRtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSL--LHA 81
Cdd:COG0410 2 PMLEVENLHAGY---GGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRS---GSIRFDGEDItgLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGV------RGnkiamIFqepmvslnPLHTLEKQLyeVLSLHRGMRKEAARGEILDCLDRtgirnaakrlsdFP- 154
Cdd:COG0410 73 HRIARLGIgyvpegRR-----IF--------PSLTVEENL--LLGAYARRDRAEVRADLERVYEL------------FPr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 -----HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLAD 225
Cdd:COG0410 126 lkerrRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIAD 204
|
250 260
....*....|....*....|....
gi 502863011 226 SVAVMQNGRCVEQNTAAALLNAPQ 249
Cdd:COG0410 205 RAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-508 |
1.03e-22 |
|
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: 96.45 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPIRKGILRRVVDQNA-----------VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQ 339
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGIlgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAgiyppDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 340 GEILFDGMplhrwnrrqmlpVRPRMqvvfqDPNSSLNPRLSilqiieeGlrvhqptltalqRENeVRRVMAEVGLDP-ET 418
Cdd:cd03220 77 GTVTVRGR------------VSSLL-----GLGGGFNPELT-------G------------REN-IYLNGRLLGLSRkEI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 419 RHRYP--AEFSG--------------GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFI 482
Cdd:cd03220 120 DEKIDeiIEFSElgdfidlpvktyssGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILV 198
|
250 260
....*....|....*....|....*.
gi 502863011 483 SHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03220 199 SHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
1.03e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILH-------LLPSPPVsypQGDILFH 74
Cdd:PRK14243 7 TETVLRTENLNVYYGSF----LAVKNVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRV---EGKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 75 GSSLL--HADEQTLRgvrgNKIAMIFQEPmvslNPLhtlEKQLYEVLSLhrGMRKEAARGEiLDCLDRTGIRNAA----- 147
Cdd:PRK14243 76 GKNLYapDVDPVEVR----RRIGMVFQKP----NPF---PKSIYDNIAY--GARINGYKGD-MDELVERSLRQAAlwdev 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 148 -KRLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVKKLADS 226
Cdd:PRK14243 142 kDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDM 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 502863011 227 VAVM---------QNGRCVEQNTAAALLNAPQHPYTQ 254
Cdd:PRK14243 220 TAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATR 256
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-234 |
1.11e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.39 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 10 NLSIAFSKQGETRtVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTLRgv 89
Cdd:cd03248 16 NVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKS-TVVALLENFYQPQ----GGQVLLDGKPISQYEHKYLH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 90 rgNKIAMIFQEPMVSLNPLHtlEKQLYEVLSLHRGMRKEAARGEildcldrtgirNAAKRLSDFPH-----------QLS 158
Cdd:cd03248 88 --SKVSLVGQEPVLFARSLQ--DNIAYGLQSCSFECVKEAAQKA-----------HAHSFISELASgydtevgekgsQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRElrSELNMSLLFITHNLSIVKKlADSVAVMQNGR 234
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-508 |
1.54e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.20 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHR 351
Cdd:COG0410 1 MPMLEVENLHAGY-----------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLpPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 352 WNRRQmlpvRPRM---QV-----VFqdpnsslnPRLSIlqiiEEGLRVhqpTLTALQRENEVRRVMAEV-GLDP---ETR 419
Cdd:COG0410 70 LPPHR----IARLgigYVpegrrIF--------PSLTV----EENLLL---GAYARRDRAEVRADLERVyELFPrlkERR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKhRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:COG0410 131 RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVL 209
|
....*....
gi 502863011 500 RQGEVVEQG 508
Cdd:COG0410 210 ERGRIVLEG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
272-527 |
2.00e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFPIRKGilrrvvdqnavLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL------IASQGEILFD 345
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKA-----------LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GMPLHRwNRRQMLPVRPRMQVVFQDPNSSlnPrLSILQIIEEGLRVHQPTLTALQREnEVRRVMAEVGLDPETRHRYPAE 425
Cdd:PRK14239 71 GHNIYS-PRTDTVDLRKEIGMVFQQPNPF--P-MSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKDRLHDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 ---FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVRALCHQVIVLRQG 502
Cdd:PRK14239 146 algLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|....*
gi 502863011 503 EVVEQGECQRVFTAPTQSYTRQLLS 527
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-227 |
2.41e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 96.34 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILhllpsppvsypqgdilfhgsSLLHADE 83
Cdd:PRK09544 3 SLVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL--------------------GLVAPDE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRGNKIAMIFQEpmVSLNPlhTLEKQLYEVLSLHRGMRKeaarGEILDCLDRTgirnAAKRLSDFPHQ-LSGGER 162
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPGTKK----EDILPALKRV----QAGHLIDAPMQkLSGGET 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSV 227
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
2.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpsppvSYPQGDILFHGSSLlh 80
Cdd:PRK13648 3 DKNSIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE-----KVKSGEIFYNNQAI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 aDEQTLRGVRgNKIAMIFQEP-------MVSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDcldrtgirnaakRLSDF 153
Cdd:PRK13648 74 -TDDNFEKLR-KHIGIVFQNPdnqfvgsIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE------------RADYE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQNG 233
Cdd:PRK13648 140 PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
250
....*....|...
gi 502863011 234 RCVEQNTAAALLN 246
Cdd:PRK13648 219 TVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-249 |
2.57e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSYPQGDILFHGSSLlh 80
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL--PDDNPNSKITVDGITL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 aDEQTLRGVRgNKIAMIFQEP-------MVSLNPLHTLEkqlyevlslHRGMRKEAARGEILDCLDRTGIRNAAKRLsdf 153
Cdd:PRK13640 75 -TAKTVWDIR-EKVGIVFQNPdnqfvgaTVGDDVAFGLE---------NRAVPRPEMIKIVRDVLADVGMLDYIDSE--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSiVKKLADSVAVMQNG 233
Cdd:PRK13640 141 PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDG 219
|
250
....*....|....*.
gi 502863011 234 RCVEQNTAAALLNAPQ 249
Cdd:PRK13640 220 KLLAQGSPVEIFSKVE 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-271 |
2.62e-22 |
|
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: 95.92 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPS--PPVSYPQGDILfhGSSLLH 80
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGdlPPTYGNDVRLF--GERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLR---GVRGNKIAMIFQepmVSLNPLHTLEKQLYEVLSLHRGMrKEAARGEILDCLDRTGIRNAAKRLsdFpHQL 157
Cdd:COG1119 71 EDVWELRkriGLVSPALQLRFP---RDETVLDVVLSGFFDSIGLYREP-TDEQRERARELLELLGLAHLADRP--F-GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
250 260 270
....*....|....*....|....*....|....
gi 502863011 238 QNTAAALLnapqhpyTQRLLdSEPAGDPVPLQRD 271
Cdd:COG1119 224 AGPKEEVL-------TSENL-SEAFGLPVEVERR 249
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-246 |
2.79e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.42 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 29 SLQIQRGETLALVGESGSGKSvsalSILHLLPS--PPVSypqgdilfhGSSLLHADEQTLRGVRGNKIAMIFQEPmvSLN 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGflTPAS---------GSLTLNGQDHTTTPPSRRPVSMLFQEN--NLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 107 PLHTLEKQLyeVLSLHRGMRKEAA-RGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK10771 84 SHLTVAQNI--GLGLNPGLKLNAAqREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 186 ALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLN 246
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
220-508 |
2.94e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 100.18 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 220 VKKLADSVAVMQNGrcveqntaaalLNAPQHPYTqrLLDSEPAGDP--VPLQRDSApLLNVEGLSVSFPirkgilrrvVD 297
Cdd:TIGR02203 287 LKSLTNVNAPMQRG-----------LAAAESLFT--LLDSPPEKDTgtRAIERARG-DVEFRNVTFRYP---------GR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 QNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWN----RRQMLPVRprMQVVFQDPN 372
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQILLDGHDLADYTlaslRRQVALVS--QDVVLFNDT 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SSLNPRLSIL-QIIEEGLRvhqptlTALQRENEVRRVMA-EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:TIGR02203 422 IANNIAYGRTeQADRAEIE------RALAAAYAQDFVDKlPLGLDTPIGEN-GVLLSGGQRQRLAIARALLKDAPILILD 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 451 EPTSSLD----RTVQAQILTLLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR02203 495 EATSALDneseRLVQAALERLMQG-----RTTLV-IAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
259-508 |
4.10e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 259 SEPAGDPVPLQRDSAPLLNVEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS 338
Cdd:PRK11174 333 AHPQQGEKELASNDPVTIEAEDLEILSP----------DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 339 QGEILFDGMPLHRWNRRQMlpvrpRMQV--VFQdpnsslNPRLsILQIIEEGLRVHQPTLTALQRENEVRRVMA------ 410
Cdd:PRK11174 403 QGSLKINGIELRELDPESW-----RKHLswVGQ------NPQL-PHGTLRDNVLLGNPDASDEQLQQALENAWVseflpl 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 411 -EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKglQEKHRLAYIFISHDLQVV 489
Cdd:PRK11174 471 lPQGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDL 547
|
250
....*....|....*....
gi 502863011 490 RAlCHQVIVLRQGEVVEQG 508
Cdd:PRK11174 548 AQ-WDQIWVMQDGQIVQQG 565
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
5.60e-22 |
|
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: 93.75 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlPSPPVSypQGDILFHGSSLLHA--DE 83
Cdd:cd03217 1 LEIKDLHVSVGG----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVT--EGEILFKGEDITDLppEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGvrgnkIAMIFQEPMvslnplhtlekqlyevlslhrgmrkeaargEIldcldrTGIRNAaKRLSDFPHQLSGGERQ 163
Cdd:cd03217 74 RARLG-----IFLAFQYPP------------------------------EI------PGVKNA-DFLRYVNEGFSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKL-ADSVAVMQNGRCVE 237
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-505 |
6.44e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLH 350
Cdd:COG1101 2 LELKNLSKTFN------PGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAgslppDSGSILIDGKDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWN--RRQMLPVRprmqvVFQDPNSSLNPRLSIlqiiEE------------GLRvhqPTLTALQREnEVRRVMAEVGLDP 416
Cdd:COG1101 72 KLPeyKRAKYIGR-----VFQDPMMGTAPSMTI----EEnlalayrrgkrrGLR---RGLTKKRRE-LFRELLATLGLGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 417 ETRHRYPAEF-SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQ 495
Cdd:COG1101 139 ENRLDTKVGLlSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNR 218
|
250
....*....|
gi 502863011 496 VIVLRQGEVV 505
Cdd:COG1101 219 LIMMHEGRII 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-240 |
6.91e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.53 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 28 LSLQIQRGETLALVGESGSGKSVSalsILH----LLPSppvsypQGDILFHGSSLLHaDEQTLRGVRgNKIAMIFQEPMV 103
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTL---FLHfngiLKPT------SGEVLIKGEPIKY-DKKSLLEVR-KTVGIVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNPLHTLEKQLYEVLSLhrGMRKEAARGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK13639 90 QLFAPTVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 184 TTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-237 |
8.21e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLH 80
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQPT----AGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTlrgvrgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRKEAArGEILDCLDRTGIRNAAKRLsdfPHQLSGG 160
Cdd:PRK11607 86 VPPYQ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQEFAKRK---PHQLSGG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-233 |
8.73e-22 |
|
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: 93.48 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSIAFSKQGEtrtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGssllhadEQTL 86
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-----SGSILLNG-------KPIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 87 RGVRGNKIAMIFQEPmvslnplhtlEKQLYE--VLS-LHRGMRKEAARGEILDC-LDRTGIRNAAKRLsdfPHQLSGGER 162
Cdd:cd03226 66 AKERRKSIGYVMQDV----------DYQLFTdsVREeLLLGLKELDAGNEQAETvLKDLDLYALKERH---PLSLSGGQK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLfITHNLSIVKKLADSVAVMQNG 233
Cdd:cd03226 133 QRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
301-517 |
1.08e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-----LIASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNSSL 375
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKST----LFRhfngiLKPTSGSVLIRGEPITKENIRE---VRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 -NPrlSILQIIEEGlrvhqPTLTALQRENEVRRV---MAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK13652 92 fSP--TVEQDIAFG-----PINLGLDEETVAHRVssaLHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-238 |
1.37e-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: 91.99 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPPVSyPQGDILFHGSSLlhadeQT 85
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKP-QQGEITLDGVPV-----SD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEPMvslnplhtlekqlyevlslhrgmrkeaargeildcLDRTGIRNAAKRlsdfphQLSGGERQRV 165
Cdd:cd03247 69 LEKALSSLISVLNQRPY-----------------------------------LFDTTLRNNLGR------RFSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRE-LRselNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQ 238
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLK---DKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
301-508 |
1.53e-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: 98.35 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLhrwnrRQMLP--VRPRMQVVFQDP---NSS 374
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRILIDGQDI-----RDVTQasLRAAIGIVPQDTvlfNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 lnprlsilqiIEEGLRVHQPTLTalqrENEVRRV--MA------------------EVGLdpetrhrypaEFSGGQRQRI 434
Cdd:COG5265 448 ----------IAYNIAYGRPDAS----EEEVEAAarAAqihdfieslpdgydtrvgERGL----------KLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 435 AIARALILKPELIILDEPTSSLD-RTVQAqILTLLKGLQEKHrlAYIFISHDLQ-VVRAlcHQVIVLRQGEVVEQG 508
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDsRTERA-IQAALREVARGR--TTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
301-508 |
1.73e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEILFDGMPLHRWNRRQM--LP----VRPRMQVvfQ 369
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTT----IRIIlgilaPDSGEVLWDGEPLDPEDRRRIgyLPeergLYPKMKV--G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DpnsslnprlsilQIIEEGlRVHQptLTALQRENEVRRVMAEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:COG4152 90 E------------QLVYLA-RLKG--LSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 450 DEPTSSLDrTVQAQIL-TLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4152 154 DEPFSGLD-PVNVELLkDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-524 |
1.85e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.95 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDG----MPL 349
Cdd:PRK14258 6 PAIKVNNLSFYY-----------DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrvefFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRWNRRQMLPvRPRMQVVFQDPNSSLNPrLSILQIIEEGLRV--HQPTLtalQRENEVRRVMAEVGLDPETR---HRYPA 424
Cdd:PRK14258 75 NIYERRVNLN-RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLWDEIKhkiHKSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL----- 499
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnen 229
|
250 260
....*....|....*....|....*
gi 502863011 500 RQGEVVEQGECQRVFTAPTQSYTRQ 524
Cdd:PRK14258 230 RIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-248 |
2.18e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFskqGETrTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpSPPVsypqGDILFHGSSLLHADE 83
Cdd:PRK09536 2 PMIDVSDLSVEF---GDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL-TPTA----GTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLrgvrGNKIAMIFQEPMVSLNplHTLEKQLYEVLSLHRG---MRKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGG 160
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLSFE--FDVRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQFADRPVT---SLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFItHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
....*...
gi 502863011 241 AAALLNAP 248
Cdd:PRK09536 223 PADVLTAD 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
2.22e-21 |
|
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: 92.91 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypqgdilfHGSSLLHADEQTlrgVRGNKIAMIFQEpmVSLN 106
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQPT----------SGGVILEGKQIT---EPGPDRMVVFQN--YSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 107 PLHTLEKQLY-EVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:TIGR01184 67 PWLTVRENIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502863011 186 ALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNG 233
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
302-505 |
2.66e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.63 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLN 376
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICgierpSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSIlqiieeglRVHQPTLTALQRENEVRR----VMAEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK10908 94 RTVYD--------NVAIPLIIAGASGDDIRRrvsaALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 453 TSSLDRTVQAQILTLlkgLQEKHRLA--YIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK10908 165 TGNLDDALSEGILRL---FEEFNRVGvtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-247 |
2.74e-21 |
|
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: 92.93 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 13 IAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQTLRgvrgN 92
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-----NGRVLVDGHDLALADPAWLR----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 93 KIAMIFQEPMVslnplhtLEKQLYEVLSLHR---GMRK--EAARgeildcldrtgIRNAAKRLSDFPH-----------Q 156
Cdd:cd03252 77 QVGVVLQENVL-------FNRSIRDNIALADpgmSMERviEAAK-----------LAGAHDFISELPEgydtivgeqgaG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCV 236
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
250
....*....|.
gi 502863011 237 EQNTAAALLNA 247
Cdd:cd03252 216 EQGSHDELLAE 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
297-508 |
2.98e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLHRWNRRQmlpVRPRMQVVFQDPNSSL 375
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKW---VRSKVGLVFQDPDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPrLSILQIIEEGLRvhQPTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13647 93 FS-STVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502863011 456 LDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
278-508 |
3.61e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFPIR----------KGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTT-----GLallrLIASQGEI 342
Cdd:COG4586 4 VENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltGI----LVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 343 LFDGM-PlhrWNRRQMLpVRpRMQVVF-QdpNSSLNPRLSILqiieEGLRVHQ-----PTLTALQRENEVRRVMaEVG-- 413
Cdd:COG4586 80 RVLGYvP---FKRRKEF-AR-RIGVVFgQ--RSQLWWDLPAI----DSFRLLKaiyriPDAEYKKRLDELVELL-DLGel 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 414 LDPETRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALC 493
Cdd:COG4586 148 LDTPVR-----QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALC 222
|
250
....*....|....*
gi 502863011 494 HQVIVLRQGEVVEQG 508
Cdd:COG4586 223 DRVIVIDHGRIIYDG 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-266 |
3.74e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQT 85
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQS---GTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LrgvrGNKIAMIFQEPMVslnPLHTLEKQLYEV-----LSLHrGMRKEAARGEILDCLDRTGIRN-AAKRLSDfphqLSG 159
Cdd:PRK11231 74 L----ARRLALLPQHHLT---PEGITVRELVAYgrspwLSLW-GRLSAEDNARVNQAMEQTRINHlADRRLTD----LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
250 260 270
....*....|....*....|....*....|...
gi 502863011 240 TaaallnaPQHPYTQRLL------DSEPAGDPV 266
Cdd:PRK11231 221 T-------PEEVMTPGLLrtvfdvEAEIHPEPV 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-248 |
3.98e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHL---LPSPPvsypQGDILFHGss 77
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLvagLEKPT----EGQIFIDG-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 llhaDEQTLRGVRGNKIAMIFQE----PMVSL--NPLHTLEkqlyeVLSLHRGMRKEAARgEILDCLDRTGIRNaakRLS 151
Cdd:PRK11432 68 ----EDVTHRSIQQRDICMVFQSyalfPHMSLgeNVGYGLK-----MLGVPKEERKQRVK-EALELVDLAGFED---RYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 DfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQ 231
Cdd:PRK11432 135 D---QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMN 211
|
250
....*....|....*..
gi 502863011 232 NGRCVEQNTAAALLNAP 248
Cdd:PRK11432 212 KGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
302-517 |
4.29e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.36 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMPLH-RWNRRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRlSILQIIEEGLRvhQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13641 99 FEN-TVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 456 LDRTVQAQILTLLKGLQ-EKHRLayIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAP 517
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQkAGHTV--ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
301-516 |
5.92e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWNRRQmlpvrprmqvvfqdpnssLNPRL 379
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQ------------------LARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SIL-QI--IEEGLRVHQ-------PTLT---ALQRENE--VRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:PRK11231 79 ALLpQHhlTPEGITVRElvaygrsPWLSlwgRLSAEDNarVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 445 ELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTA 516
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
6.06e-21 |
|
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: 90.18 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAfskqgetrTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsYPQGDILFHGSSLLHADe 83
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPVTRRS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 qtLRGVRGNKIAMIFQEPmvslnplhtlekqlyevlsLHRGMrkeaargeildCLDRTGIRNAAkrlsdFPHQLSGGERQ 163
Cdd:cd03215 69 --PRDAIRAGIAYVPEDR-------------------KREGL-----------VLDLSVAENIA-----LSSLLSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
278-508 |
7.51e-21 |
|
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: 91.63 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFPIR----------KGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFD 345
Cdd:cd03267 3 VSNLSKSYRVYskepgligslKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-LKILSglLQPTSGEVRVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 346 GmpLHRWNRRQMLpvRPRMQVVFQDPNS---SLNPRlsilqiieEGLRVHQPT--LTALQRENEVRRV--MAEVG--LDP 416
Cdd:cd03267 82 G--LVPWKRRKKF--LRRIGVVFGQKTQlwwDLPVI--------DSFYLLAAIydLPPARFKKRLDELseLLDLEelLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 417 ETRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:cd03267 150 PVR-----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRV 224
|
250
....*....|..
gi 502863011 497 IVLRQGEVVEQG 508
Cdd:cd03267 225 LVIDKGRLLYDG 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-237 |
1.14e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL---PSPPVSYpQGDILFHGSSLLHAd 82
Cdd:COG4136 2 LSLENLTITL----GGRPLLAPLSLTVAPGEILTLMGPSGSGKS----TLLAAIagtLSPAFSA-SGEVLLNGRRLTAL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 eQTLRgvrgNKIAMIFQEPMvsLNPLHTLEKQLyeVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGER 162
Cdd:COG4136 72 -PAEQ----RRIGILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHnlsivkklaDSVAVMQNGRCVE 237
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH---------DEEDAPAAGRVLD 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
301-509 |
1.27e-20 |
|
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: 95.58 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNR---RQMLPVRPRMQVVFQDpnssln 376
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDIDRhtlRQFINYLPQEPYIFSG------ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 prlSILQ--IIEEGLRVHQPTLTALQRENEVRRVMAEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:TIGR01193 563 ---SILEnlLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTElSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 454 SSLDRTVQAQILTLLKGLQEKhrlAYIFISHDLQVVRaLCHQVIVLRQGEVVEQGE 509
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGS 691
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-280 |
1.39e-20 |
|
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: 92.56 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 40 LVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQtLRGvrgnkIAMIFQEpmVSLNPLHTLEKQLYEVL 119
Cdd:TIGR01187 1 LLGPSGCGKT-TLLRLLAGFEQPD----SGSIMLDGEDVTNVPPH-LRH-----INMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 120 SLhRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLL 199
Cdd:TIGR01187 68 KM-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 200 RELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQRLLDSEPAGDPVPLQRDSAPLL--N 277
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVlaG 223
|
...
gi 502863011 278 VEG 280
Cdd:TIGR01187 224 VEG 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
254-516 |
1.49e-20 |
|
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: 95.11 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSEPAGDP-VPLQRDSAPLLnVEGLSVSFPIRKgilrrvvdqNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaL 332
Cdd:TIGR01842 295 NELLANYPSRDPaMPLPEPEGHLS-VENVTIVPPGGK---------KPTLRGISFSLQAGEALAIIGPSGSGKST----L 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 333 LRLIA-----SQGEILFDGMPLHRWNRRQM------LPvrprmQVV-------------FQDpnsSLNPRlsilQIIEEG 388
Cdd:TIGR01842 361 ARLIVgiwppTSGSVRLDGADLKQWDRETFgkhigyLP-----QDVelfpgtvaeniarFGE---NADPE----KIIEAA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 389 L--RVHQptlTALQRENEVRRVMAEVGldpetrhrypAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILT 466
Cdd:TIGR01842 429 KlaGVHE---LILRLPDGYDTVIGPGG----------ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAN 495
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 502863011 467 LLKGLQEKHRLAyIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFTA 516
Cdd:TIGR01842 496 AIKALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-247 |
1.52e-20 |
|
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: 95.27 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 15 FSKQGEtRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSSLLHADEQTLRGV 89
Cdd:COG5265 365 FGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVT------SGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 90 rgnkIAMIFQEPmVSLNplHTLEkqlYEVlslhRGMRKEAARGEIldcldrtgiRNAAK--RLSDF----PHQ------- 156
Cdd:COG5265 434 ----IGIVPQDT-VLFN--DTIA---YNI----AYGRPDASEEEV---------EAAARaaQIHDFieslPDGydtrvge 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLS-IVKklADSVAVMQ 231
Cdd:COG5265 491 rglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStIVD--ADEILVLE 566
|
250
....*....|....*.
gi 502863011 232 NGRCVEQNTAAALLNA 247
Cdd:COG5265 567 AGRIVERGTHAELLAQ 582
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
302-514 |
2.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRWNR-RQMLPVRPRMQVVFQDPNSSLNPR 378
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTI-MQLLNglHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 379 lSILQIIEEGLR---VHQPTLTALQRENevrrvMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13649 102 -TVLKDVAFGPQnfgVSQEEAEALAREK-----LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 456 LDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-508 |
2.19e-20 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 89.91 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 307 FSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPlHRWNRRQMLPVRPRMQVVFQDPnsslnprLSILQII 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKVAGAS-PGKGWRHIGYVPQRHEFAWDFP-------ISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 386 EEGLRVHQPTLTALQREN--EVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQ 463
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADfaAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502863011 464 ILTLLKGL-QEKHrlAYIFISHDLQVVRALCHQViVLRQGEVVEQG 508
Cdd:TIGR03771 152 LTELFIELaGAGT--AILMTTHDLAQAMATCDRV-VLLNGRVIADG 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-215 |
3.42e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSkqgETRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILhllpsppvsYPQGDilfhGSSLLHADE 83
Cdd:COG4178 363 LALEDLTLRTP---DGRPLLEDLSLSLKPGERLLITGPSGSGKStlLRAIAGL---------WPYGS----GRIARPAGA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLrgvrgnkiaMIFQEPMVslnPLHTLEKQLyevlsLHRGMRKEAARGEILDCLDRTGIRNAAKRLS---DFPHQLSGG 160
Cdd:COG4178 427 RVL---------FLPQRPYL---PLGTLREAL-----LYPATAEAFSDAELREALEAVGLGHLAERLDeeaDWDQVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRElrsEL-NMSLLFITH 215
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELpGTTVISVGH 542
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
302-514 |
3.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEI-LFDGMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRl 379
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SILQIIEEGlrvhqPTLTALQREnEVRRVMAE----VGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13643 101 TVLKDVAFG-----PQNFGIPKE-KAEKIAAEklemVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 456 LDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
273-504 |
3.90e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.87 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSfpirkgilrrvvdqnAVLKNIRFSLRPGESLGLVGESGSGKSTTGLAL--LRLIASqGEILFDGMPLH 350
Cdd:cd03215 2 EPVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALfgLRPPAS-GEITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMlpVRPRMQVVFQDPNSS-LNPRLSIlqiieeglrvhqptltalqRENevrrvmaeVGLdpetrhryPAEFSGG 429
Cdd:cd03215 66 RRSPRDA--IRAGIAYVPEDRKREgLVLDLSV-------------------AEN--------IAL--------SSLLSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-238 |
4.53e-20 |
|
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: 88.79 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGeTLALVGESGSGKSvSALSILHLLpSPPVSypqGDILFHGSSLLhADEQT 85
Cdd:cd03264 1 LQLENLTKRYGK----KRALDGVSLTLGPG-MYGLLGPNGAGKT-TLMRILATL-TPPSS---GTIRIDGQDVL-KQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVrgnkIAMIFQEPMVSlnPLHTLEKQLYEVLSLHrGMRKEAARGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRV 165
Cdd:cd03264 70 LRRR----IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKK---IGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
301-516 |
4.55e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEILFDGMPLHRWNRRQmlpVRPRMQVVFQdpNSSLNPRL 379
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAhGHVWLDGEHIQHYASKE---VARRIGLLAQ--NATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 SILQIIEEGLRVHQPTLTALQRENE--VRRVMAEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK10253 97 TVQELVARGRYPHQPLFTRWRKEDEeaVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 458 RTVQAQILTLLKGLQEKHRLAYIFISHDL-QVVRALCHqVIVLRQGEVVEQGECQRVFTA 516
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASH-LIALREGKIVAQGAPKEIVTA 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
301-508 |
4.93e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 89.14 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPLHRwnrrqmlpvRPRMQVVFQDPNSS 374
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGqditkLPMHK---------RARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSILQIIEEGLRVHqpTLTALQRENEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:cd03218 86 IFRKLTVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 455 SLDRTVQAQILTLLKGLqeKHRLAYIFIS-HDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03218 163 GVDPIAVQDIQKIIKIL--KDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-262 |
4.97e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 15 FSKQGetrtvVSDLSLQIQRGETLALVGESGSGKSV-----SALsilhLLPSppvsypQGDILFHGSSL-LHADEQTLRG 88
Cdd:PRK13641 18 MEKKG-----LDNISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPS------SGTITIAGYHItPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 89 VRgNKIAMIFQEPmvslnplhtlEKQLYE--VLS------LHRGMRKEAARGEILDCLDRTGIRNAAkrLSDFPHQLSGG 160
Cdd:PRK13641 83 LR-KKVSLVFQFP----------EAQLFEntVLKdvefgpKNFGFSEDEAKEKALKWLKKVGLSEDL--ISKSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHAS 228
|
250 260
....*....|....*....|..
gi 502863011 241 AAALLNAPQhpYTQRLLDSEPA 262
Cdd:PRK13641 229 PKEIFSDKE--WLKKHYLDEPA 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-234 |
5.51e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 16 SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSppVSYPQGDILFHGSSLLHADEQTLRgvrgnkia 95
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAG--LETPSAGELLAGTAPLAEAREDTR-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 96 MIFQEpmVSLNPLhtleKQLYEVLSLH-RGMRKEAArgeiLDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMALLTR 174
Cdd:PRK11247 85 LMFQD--ARLLPW----KKVIDNVGLGlKGQWRDAA----LQALAAVGL---ADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 175 PELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
301-518 |
5.63e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNRR----------QMLPVRPRMQ 365
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKST----LLKMLgrhqpPSEGEILLDAQPLESWSSKafarkvaylpQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 366 VvfqdpnsslnprlsiLQIIEEGlrvHQPTLTALQR-----ENEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARAL 440
Cdd:PRK10575 102 V---------------RELVAIG---RYPWHGALGRfgaadREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 441 ILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
278-484 |
5.68e-20 |
|
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: 86.82 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 278 VEGLSVSFPirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIlfdGMPLHrw 352
Cdd:cd03223 3 LENLSLATP----------DGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALAglwpwGSGRI---GMPEG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 NRRQMLPVRPRMqvvfqdpnsslnPRLSILQIIeeglrvhqptltalqrenevrrvmaevgldpetrhRYP--AEFSGGQ 430
Cdd:cd03223 64 EDLLFLPQRPYL------------PLGTLREQL-----------------------------------IYPwdDVLSGGE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKglqeKHRLAYIFISH 484
Cdd:cd03223 97 QQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-247 |
7.19e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.86 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 2 TQPLLS----IDNLSIAFSKQgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsYPQGDILFHGSS 77
Cdd:PRK10790 333 DRPLQSgridIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 LLHADEQTLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRGMRKEAargeILDCLDRTGIRNAAKRLSDFPH-- 155
Cdd:PRK10790 405 LSSLSHSVLR----QGVAMVQQDPVV-------LADTFLANVTLGRDISEEQ----VWQALETVQLAELARSLPDGLYtp 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLS-IVKklADSVA 228
Cdd:PRK10790 470 lgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStIVE--ADTIL 545
|
250
....*....|....*....
gi 502863011 229 VMQNGRCVEQNTAAALLNA 247
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAA 564
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-236 |
9.19e-20 |
|
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: 87.22 E-value: 9.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 21 TRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILH-LLPSPPVSypqGDILFHGSSLlhaDEQTLRGvrgnKIAMIFQ 99
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKS-TLLNALAgRRTGLGVS---GEVLINGRPL---DKRSFRK----IIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 100 EPMVslnpLHTLekQLYEVLSLHRGMRkeaargeildcldrtgirnaakrlsdfphQLSGGERQRVMIAMALLTRPELLI 179
Cdd:cd03213 90 DDIL----HPTL--TVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 180 ADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSI-VKKLADSVAVMQNGRCV 236
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSeIFELFDKLLLLSQGRVI 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-234 |
1.14e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.32 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 11 LSIAFSKQgetrtvVSDLSLQIQ-----RGETlALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQT 85
Cdd:PRK11144 2 LELNFKQQ------LGDLCLTVNltlpaQGIT-AIFGRSGAGKT-SLINAISGLTRPQ----KGRIVLNGRVLFDAEKGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEpmVSLNPLHTLEKqlyevlSLHRGMRKEAaRGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQRV 165
Cdd:PRK11144 70 CLPPEKRRIGYVFQD--ARLFPHYKVRG------NLRYGMAKSM-VAQFDKIVALLGIEPLLDR---YPGSLSGGEKQRV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK11144 138 AIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-238 |
1.14e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.78 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLH 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIAGFETPD----SGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 AD-EQtlRGVRgnkiaMIFQEpmVSLNPLHTLekqlYEVLSLHRGMRKEAARgEIldcldRTGIRNAAK--RLSDF---- 153
Cdd:PRK09452 81 VPaEN--RHVN-----TVFQS--YALFPHMTV----FENVAFGLRMQKTPAA-EI-----TPRVMEALRmvQLEEFaqrk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNG 233
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
....*
gi 502863011 234 RcVEQ 238
Cdd:PRK09452 222 R-IEQ 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
301-508 |
1.15e-19 |
|
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: 87.97 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDG-----MPLHRWNRRQMLPVrPRMQVVFqd 370
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTT----LLKTLmgllpVKSGSIRLDGeditkLPPHERARAGIAYV-PQGREIF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 pnsslnPRLSILQIIEEGLrvhqptlTALQRENevRRVMAEV-GLDP---ETRHRYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:TIGR03410 88 ------PRLTVEENLLTGL-------AALPRRS--RKIPDEIyELFPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 447 IILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-234 |
1.18e-19 |
|
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: 87.46 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 23 TVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL--PSPPVSypqGDILFHGSSLLHADEQTLRGVRgNKIAMIFQE 100
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKS----TLLKLIykEELPTS---GTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 pmVSLNPLHTLEKQLYEVLSLHRGMRKEAARgEILDCLDRTGIRNaakRLSDFPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03292 87 --FRLLPDRNVYENVAFALEVTGVPPREIRK-RVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 181 DEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
276-503 |
1.32e-19 |
|
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: 85.19 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQGEIlfdgmplhrwnrr 355
Cdd:cd03221 1 IELENLSKTY-----------GGKLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIAGELEP------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 356 qmlpvrprmqvvfqdpnsslnprlsilqiiEEGlrvhqptltalqrenevrrvmaEVGLDPETRHRYPAEFSGGQRQRIA 435
Cdd:cd03221 53 ------------------------------DEG----------------------IVTWGSTVKIGYFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 436 IARALILKPELIILDEPTSSLD-RTVQAqiltLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDlESIEA----LEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-234 |
1.43e-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: 87.22 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 29 SLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTlrgvrgNKIAMIFQEPmvSLNPL 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPA----SGSIKVNDQSHTGLAPYQ------RPVSMLFQEN--NLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 109 HTLEKQLyeVLSLHRGMRKEAARGE-ILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
Cdd:TIGR01277 85 LTVRQNI--GLGLHPGLKLNAEQQEkVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502863011 188 DVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-234 |
1.46e-19 |
|
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: 86.12 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiaFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLlhadEQT 85
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PTS---GRVRLDGADI----SQW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEpmvslnplhtleKQLYEvlslhrgmrkeaarGEILDCLdrtgirnaakrlsdfphqLSGGERQRV 165
Cdd:cd03246 70 DPNELGDHVGYLPQD------------DELFS--------------GSIAENI------------------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVkKLADSVAVMQNGR 234
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-241 |
1.52e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.92 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFhGSSLLHA--DEQTLRGVRgNKIAMIFQEPmvs 104
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKS-TLLQHLNGLLQPT----SGTVTI-GERVITAgkKNKKLKPLR-KKVGIVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 lnplhtlEKQLYE--VLS------LHRGMRKEAARGEILDCLDRTGIrnAAKRLSDFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:PRK13634 95 -------EHQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTA 241
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-240 |
1.63e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAF-SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILF--HGSSLLHA 81
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGVRGNK-----IAMIFQEPMVSLNPlHTLEKQL-YEVLSLhrGMRKEAARGEILDCLDRTGIRNAAkrLSDFPH 155
Cdd:PRK13631 101 TNPYSKKIKNFKelrrrVSMVFQFPEYQLFK-DTIEKDImFGPVAL--GVKKSEAKKLAKFYLNKMGLDDSY--LERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
....*
gi 502863011 236 VEQNT 240
Cdd:PRK13631 255 LKTGT 259
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-245 |
1.95e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAfskqgeTRtvVSDLSLQIQRGETLALVGESGSGKSvSALSILH-LLPSppvsypQGDILFHGSSLLHADEQ 84
Cdd:COG4138 1 LQLNDVAVA------GR--LGPISAQVNAGELIHLIGPNGAGKS-TLLARMAgLLPG------QGEILLNGRPLSDWSAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRgnkiAMIFQEPMvslnPLHTLekQLYEVLSLHR--GMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGER 162
Cdd:COG4138 66 ELARHR----AYLSQQQS----PPFAM--PVFQYLALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 163 QRVMIAMALLT-------RPELLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:COG4138 133 QRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
250
....*....|
gi 502863011 236 VEQNTAAALL 245
Cdd:COG4138 212 VASGETAEVM 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
302-508 |
2.26e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS--------QGEILFDGMPLhrwNRRQMlpvRPRMQVVFQDpns 373
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTT----LMNALAFrspkgvkgSGSVLLNGMPI---DAKEM---RAISAYVQQD--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 SLN-PRLSILQ--IIEEGLRVHQpTLTALQRENEVRRVMAEVGLDP--ETRHRYPAE---FSGGQRQRIAIARALILKPE 445
Cdd:TIGR00955 108 DLFiPTLTVREhlMFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 446 LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
301-509 |
2.36e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILF---DGMPLHRWNR------------------ 354
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlNAL----LLPDTGTIEWifkDEKNKKKTKEkekvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 355 RQMLPVRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPTLTALQReneVRRVMAEVGLDPETRHRYPAEFSGGQRQRI 434
Cdd:PRK13651 98 KKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKR---AAKYIELVGLDESYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 435 AIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-237 |
2.42e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSIL-HllPSPPVSypQGDILFHGSSLLH--AD 82
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgH--PKYEVT--SGSILLDGEDILElsPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRGvrgnkIAMIFQEPM----VSL-NPLHTLekqlyevlslhrgmrKEAARGEILDCLD-RTGIRNAAKRL---SDF 153
Cdd:COG0396 73 ERARAG-----IFLAFQYPVeipgVSVsNFLRTA---------------LNARRGEELSAREfLKLLKEKMKELgldEDF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 PHQ-----LSGGERQRVMIA-MALLtRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHN---LSIVKklA 224
Cdd:COG0396 133 LDRyvnegFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYqriLDYIK--P 208
|
250
....*....|...
gi 502863011 225 DSVAVMQNGRCVE 237
Cdd:COG0396 209 DFVHVLVDGRIVK 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
302-508 |
2.50e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMlpvrpRMQVVFQDPNSSL----- 375
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYdIDEGEILLDGHDLRDYTLASL-----RNQVALVSQNVHLfndti 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 --------NPRLSILQIIEEGLRVHqptltAL----QRENEVRRVMAEVGldpetrhrypAEFSGGQRQRIAIARALILK 443
Cdd:PRK11176 434 anniayarTEQYSREQIEEAARMAY-----AMdfinKMDNGLDTVIGENG----------VLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 444 PELIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQ-KNRTSLV-IAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-302 |
2.55e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.99 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 15 FSKQGETRTVVSDLSLQIQRGETLALVGESGSGKS--VSALS-ILHllPSppvsypQGDILFHGSSLlHADEQTLRgvrg 91
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSttIKMLTgILV--PT------SGEVRVLGYVP-FKRRKEFA---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 92 NKIAMIF---QEPMVSLNPLHTLE--KQLYEV-LSLHRGMRKEAArgEILDcldrtgirnaakrLSDFPH----QLSGGE 161
Cdd:COG4586 95 RRIGVVFgqrSQLWWDLPAIDSFRllKAIYRIpDAEYKKRLDELV--ELLD-------------LGELLDtpvrQLSLGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTA 241
Cdd:COG4586 160 RMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 242 AALLNAPQHPYTQRLLDSEPAgDPVPLQRDsAPLLNVEGLSVSFPIRKG-----ILRRVVDQNAVL 302
Cdd:COG4586 240 EELKERFGPYKTIVLELAEPV-PPLELPRG-GEVIEREGNRVRLEVDPReslaeVLARLLARYPVR 303
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-236 |
2.79e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTqPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLH 80
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPT----SGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRGNKIAMIFQEpmVSLNPlHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGG 160
Cdd:PRK10535 75 LDADALAQLRREHFGFIFQR--YHLLS-HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKlADSVAVMQNGRCV 236
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-236 |
3.16e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 14 AFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVSYpQGDILFHGSSLlHADEQTLRGvrgnk 93
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKT-TLMNALAFRSPKGVKG-SGSVLLNGMPI-DAKEMRAIS----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 94 iAMIFQEPMvsLNPLHTLEKQLY--EVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSDFPHQ---LSGGERQRVMIA 168
Cdd:TIGR00955 102 -AYVQQDDL--FIPTLTVREHLMfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 169 MALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
297-518 |
3.40e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.06 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRWNRRQMlpVRpRMQVVFQDP 371
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKST----LLSMISrllppDSGEVLVDGLDVATTPSREL--AK-RLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NssLNPRLSILQIIEEGlRV--HQPTLTALQREnEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:COG4604 85 H--INSRLTVRELVAFG-RFpySKGRLTAEDRE-IIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 450 DEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-254 |
3.56e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 13 IAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSppvSYP--QGDILFHGSSLlhaDEQTLRGVR 90
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKS----TIANLLTR---FYDidEGEILLDGHDL---RDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 91 gNKIAMIFQEpmVSL------NPLHTLEKQLYEVLSLHRGMRKEAARGEIL---DCLDRTGIRNAAkrlsdfphQLSGGE 161
Cdd:PRK11176 417 -NQVALVSQN--VHLfndtiaNNIAYARTEQYSREQIEEAARMAYAMDFINkmdNGLDTVIGENGV--------LLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTA 241
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTH 562
|
250
....*....|...
gi 502863011 242 AALLnAPQHPYTQ 254
Cdd:PRK11176 563 AELL-AQNGVYAQ 574
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
297-508 |
3.69e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.32 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnrRQMLPVRPRMQ---VVF 368
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAglediTSGDLFIGE--------KRMNDVPPAERgvgMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 369 QdpNSSLNPRLSILQIIEEGLRVHQPTLTAL-QRENEVRRVMAEVGLdpetRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11000 82 Q--SYALYPHLSVAENMSFGLKLAGAKKEEInQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 448 ILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
296-508 |
3.98e-19 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 86.55 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 296 VDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDGMPLHrwnrrQMLP---VRPRMQVVFQ 369
Cdd:TIGR01978 10 VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGQDLL-----ELEPderARAGLFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSlnPRLSILQIIEEGLRVH-----QPTLTALQRENEVRRVMAEVGLDPETRHRYPAE-FSGGQRQRIAIARALILK 443
Cdd:TIGR01978 85 YPEEI--PGVSNLEFLRSALNARrsargEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 444 PELIILDEPTSSLD----RTVQAQIltllKGLQEKHRlAYIFISHDLQVVRALCHQVI-VLRQGEVVEQG 508
Cdd:TIGR01978 163 PKLAILDEIDSGLDidalKIVAEGI----NRLREPDR-SFLIITHYQRLLNYIKPDYVhVLLDGRIVKSG 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
265-518 |
4.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 265 PVPLQRDSapLLNVEGLSVSFPirkgilRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTT------------GLAL 332
Cdd:PRK13631 13 PNPLSDDI--ILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnglikskyGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 333 LRLIASQGEILFDGMPLHRWNRR--QMLPVRPRMQVVFQDPNSSLNpRLSILQIIEEG-LRVHQPTLTALQReneVRRVM 409
Cdd:PRK13631 85 VGDIYIGDKKNNHELITNPYSKKikNFKELRRRVSMVFQFPEYQLF-KDTIEKDIMFGpVALGVKKSEAKKL---AKFYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 410 AEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIfISHDLQVV 489
Cdd:PRK13631 161 NKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHV 239
|
250 260
....*....|....*....|....*....
gi 502863011 490 RALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-245 |
4.83e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.46 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQGETRTVvSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQ 84
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRgvrgNKIAMIFQEPMVSLNPLHTLEKQLYevlslhrGMRKEA-ARGEILDCLDRTGIrnaAKRLSDF----PHQLSG 159
Cdd:PRK13642 78 NLR----RKIGMVFQNPDNQFVGATVEDDVAF-------GMENQGiPREEMIKRVDEALL---AVNMLDFktrePARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQN 239
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
....*.
gi 502863011 240 TAAALL 245
Cdd:PRK13642 223 APSELF 228
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
10-267 |
5.22e-19 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 90.33 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 10 NLSIAFSKQGetrtvVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVsypqGDILFHGSSLLHADEQTLRgv 89
Cdd:TIGR01192 341 TFEFANSSQG-----VFDVSFEAKAGQTVAIVGPTGAGKT-TLINLLQRVYDPTV----GQILIDGIDINTVTRESLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 90 rgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRG------MRKEAARGEILDCLDRTgIRNAAKRLSDFPHQLSGGERQ 163
Cdd:TIGR01192 409 --KSIATVFQDAGL-------FNRSIRENIRLGREgatdeeVYEAAKAAAAHDFILKR-SNGYDTLVGERGNRLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAA 243
Cdd:TIGR01192 479 RLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSFQE 555
|
250 260
....*....|....*....|....*...
gi 502863011 244 LLNAPQHPY----TQRLLDSEPAGDPVP 267
Cdd:TIGR01192 556 LIQKDGRFYkllrRSGLLTNQPATKPLR 583
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-236 |
5.42e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 85.72 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 13 IAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLHADEQTLRGVrgn 92
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS-TLLKLLAGLYKPT----SGSVLLDGTDIRQLDPADLRRN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 93 kIAMIFQEPmvslnplHTLEKQLYEVLSLHRGMRKEAargEILDCLDRTGIRNAAKRLsdfPH-----------QLSGGE 161
Cdd:cd03245 80 -IGYVPQDV-------TLFYGTLRDNITLGAPLADDE---RILRAAELAGVTDFVNKH---PNgldlqigergrGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVkKLADSVAVMQNGRCV 236
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-234 |
5.62e-19 |
|
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: 85.66 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 12 SIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpsppvsypqgdilfhgSSLLHADEQTLRgVRG 91
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLL----------------AGIYPPDSGTVT-VRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 92 NKIAMIfqEPMVSLNPLHTLEKQLYEVLSLHrGMRKEAARGEILDCLDRTGirnaakrLSDFPHQ----LSGGERQRVMI 167
Cdd:cd03220 84 RVSSLL--GLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSE-------LGDFIDLpvktYSSGMKARLAF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 168 AMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
296-485 |
7.51e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 296 VDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLHRWNrrqmlPVRPRMQV--VF 368
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKST----LLKIVASlisptSGTLLFEGEDISTLK-----PEIYRQQVsyCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 369 QDP---NSSLNPRLsilqIIEEGLRVHQPTLTALQREnevrrvMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:PRK10247 88 QTPtlfGDTVYDNL----IFPWQIRNQQPDPAIFLDD------LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502863011 446 LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHD 485
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
301-507 |
8.56e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.98 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnRR--QMLPVRPRMQVVFQdpNS 373
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAgleriTSGEIWIGG-------RVvnELEPADRDIAMVFQ--NY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 SLNPRLSILQIIEEGLRVHQ-PTLTALQRENEVRRVMaEVG--LDpetrhRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:PRK11650 86 ALYPHMSVRENMAYGLKIRGmPKAEIEERVAEAARIL-ELEplLD-----RKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 451 EPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDlQV-VRALCHQVIVLRQGeVVEQ 507
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-QVeAMTLADRVVVMNGG-VAEQ 215
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-249 |
1.64e-18 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 85.02 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHA--DE 83
Cdd:TIGR04406 2 LVAENLIKSYKK----RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILIDGQDITHLpmHE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGvrgnkIAMIFQEPmvSLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLSdfpHQLSGGERQ 163
Cdd:TIGR04406 73 RARLG-----IGYLPQEA--SIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKA---MSLSGGERR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAA 243
Cdd:TIGR04406 143 RVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAE 221
|
....*.
gi 502863011 244 LLNAPQ 249
Cdd:TIGR04406 222 IVANEK 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-254 |
1.70e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.47 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKS--VSALSILHLLPSPpvSYPQGDILFHGSSLLHA 81
Cdd:PRK14258 6 PAIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNELESE--VRVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGVRgnKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhrGMRKEAArgeiLDCLDRTGIRNA------AKRLSDFPH 155
Cdd:PRK14258 80 RVNLNRLRR--QVSMVHPKP--NLFPMSVYDNVAYGVKIV--GWRPKLE----IDDIVESALKDAdlwdeiKHKIHKSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQN--- 232
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnen 229
|
250 260
....*....|....*....|....
gi 502863011 233 --GRCVEQNTAAALLNAPQHPYTQ 254
Cdd:PRK14258 230 riGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-248 |
2.18e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 21 TRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADeqtLRGVRgNKIAMIFQE 100
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK--PTS---GSVLIRGEPITKEN---IREVR-KFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 PMVSLnpLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK13652 87 PDDQI--FSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 181 DEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAP 248
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
301-511 |
2.24e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.20 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEILFDGMPLHRWNRRQMLPVRPRMQVVFQdpNSSL 375
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQiapdhGEILFDGENIPAMSRSRLYTVRKRMSMLFQ--SGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRLSILQIIEEGLRVHQPTLTALQRENEVRRVMAeVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK11831 96 FTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA-VGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 456 LDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQ 511
Cdd:PRK11831 174 QDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
287-511 |
2.35e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 287 IRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI----ASQGEILFDGMPLHRWNR--RQMLPV 360
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGSHIELLGRTVQREGRlaRDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 361 RPRMQVVFQDPNssLNPRLSILQIIEEGLRVHQPT-------LTALQREnEVRRVMAEVGLdPETRHRYPAEFSGGQRQR 433
Cdd:PRK09984 85 RANTGYIFQQFN--LVNRLSVLENVLIGALGSTPFwrtcfswFTREQKQ-RALQALTRVGM-VHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 434 IAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQ 511
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-234 |
2.39e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVsypqGDILFHGSSLLHADEQTLRGVRgNKIAMIFQEP 101
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERPSA----GKIWFSGHDITRLKNREVPFLR-RQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 102 MVslnplhTLEKQLYEVLSLH---RGMRKEAARGEILDCLDRTGIRNAAKrlsDFPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK10908 89 HL------LMDRTVYDNVAIPliiAGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 179 IADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-234 |
2.48e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSK-QGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL--HLLPSppvsypQGDILFHGSSLLH-A 81
Cdd:COG1101 2 LELKNLSKTFNPgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIagSLPPD------SGSILIDGKDVTKlP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQtlrgvRGNKIAMIFQEPMVSLNPLHTLEKQLyeVLSLHRGMRKEAARG----------EILDCLDRtGIRNaakRLS 151
Cdd:COG1101 75 EYK-----RAKYIGRVFQDPMMGTAPSMTIEENL--ALAYRRGKRRGLRRGltkkrrelfrELLATLGL-GLEN---RLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQ 231
Cdd:COG1101 144 TKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMH 223
|
...
gi 502863011 232 NGR 234
Cdd:COG1101 224 EGR 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-230 |
3.02e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpsppvsypqgdilfhgSSLLHADEQTLRGVRGNKIAMIFQEP 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKS----TLLKVL----------------AGVLRPTSGTVRRAGGARVAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 102 MVSlnplHTLEKQLYEVLSL----HRGMRKE---AARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTR 174
Cdd:NF040873 65 EVP----DSLPLTVRDLVAMgrwaRRGLWRRltrDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 175 PELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVkKLADSVAVM 230
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
302-527 |
4.42e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-------LIAS---QGEILFDGMPLHRwNRRQMLPVRPRMQVVFQDP 371
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKST----ILRcfnrlndLIPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSlnPRlSILQIIEEGLRV--HQPTL-----TALQRE---NEVRRVMAEVGLdpetrhrypaEFSGGQRQRIAIARALI 441
Cdd:PRK14243 101 NPF--PK-SIYDNIAYGARIngYKGDMdelveRSLRQAalwDEVKDKLKQSGL----------SLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 442 LKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQVVRALCHQVIVL---------RQGEVVEQGECQR 512
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEK 245
|
250
....*....|....*
gi 502863011 513 VFTAPTQSYTRQLLS 527
Cdd:PRK14243 246 IFNSPQQQATRDYVS 260
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-261 |
4.49e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 83.36 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 30 LQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQTLRGVRGNKIAMIFqepmvSLNPLH 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPA-----KGTVKVAGASPGKGWRHIGYVPQRHEFAWDF-----PISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 110 TLEKQLYEVLSLHRGMRKEAARGeILDCLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
Cdd:TIGR03771 71 TVMSGRTGHIGWLRRPCVADFAA-VRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 190 TVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVaVMQNGRCVEQNTAAALLNAPQHPYTQRLLDSEP 261
Cdd:TIGR03771 147 PTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGVSDSSP 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
274-509 |
4.51e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpirKGIlrrvvdqnAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:PRK15439 10 PLLCARSISKQY---SGV--------EVLKGIDFTLHAGEVHALLGGNGAGKST----LMKIIAgivppDSGTLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRWNrrqmlPVRPR---MQVVFQDPNssLNPRLSILQIIEEGLRVHQPTltalqrENEVRRVMAEVG--LDPETRhryP 423
Cdd:PRK15439 75 CARLT-----PAKAHqlgIYLVPQEPL--LFPNLSVKENILFGLPKRQAS------MQKMKQLLAALGcqLDLDSS---A 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:PRK15439 139 GSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVMRDGT 217
|
....*.
gi 502863011 504 VVEQGE 509
Cdd:PRK15439 218 IALSGK 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
307-518 |
4.57e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.83 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 307 FSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMlpVRPRMQVVFQDPNSSLNPRLSILQIie 386
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAEL--ARHRAYLSQQQTPPFAMPVFQYLTL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 387 eglrvHQPTLTAL-QRENEVRRVMAEVGLDPETrHRYPAEFSGGQRQRIAIARALI-----LKPE--LIILDEPTSSLDR 458
Cdd:PRK03695 93 -----HQPDKTRTeAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 459 TVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFTAPT 518
Cdd:PRK03695 167 AQQAALDRLLSELCQQGI-AVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
301-527 |
5.16e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.11 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRW---NRRQMLPVRPRMQVVFQ------- 369
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRIMIDDCDVAKFgltDLRRVLSIIPQSPVLFSgtvrfni 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSLNprlsilqiiEEGLrvhqptLTALQR---ENEVRRvmAEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PLN03232 1331 DPFSEHN---------DADL------WEALERahiKDVIDR--NPFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 447 IILDEPTSSLDRTVQAQILTLLKglQEKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFTAPTQSYTRQLL 526
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
.
gi 502863011 527 S 527
Cdd:PLN03232 1470 S 1470
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-242 |
1.14e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHGSSllhaDEQTLRGVRgNKIAMIFQEPmvsln 106
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 107 plhtlEKQLYEVLSL--------HRGMRKEAARGEILDCLDRTGIRNAAKRLSdfPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK13643 94 -----ESQLFEETVLkdvafgpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKS--PFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 179 IADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAA 242
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-240 |
1.17e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 8 IDNLSIAFSKQG--ETRTVvSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPPVSYPQGDILfhGSSLLHADEQT 85
Cdd:PRK13645 9 LDNVSYTYAKKTpfEFKAL-NNTSLTFKKNKVTCVIGTTGSGKS----TMIQLTNGLIISETGQTIV--GDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRG--NKIAMIFQEPMVSLNPlHTLEKQLyEVLSLHRGMRKEAARGEILDCLDRTGI-RNAAKRlsdFPHQLSGGER 162
Cdd:PRK13645 82 IKEVKRlrKEIGLVFQFPEYQLFQ-ETIEKDI-AFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-269 |
1.28e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.89 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPS--PPVSypqGDILFHGSSLLHADEQTLRGVRgNKIAMIFQ 99
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGqiAPDH---GEILFDGENIPAMSRSRLYTVR-KRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 100 EP--MVSLNPLHTLEKQLYEvlslHRGMRKEAARGEILDCLDRTGIRNAAKRLsdfPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK11831 92 SGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 178 LIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQhPYTQRLL 257
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFL 243
|
250
....*....|..
gi 502863011 258 DSEPAGdPVPLQ 269
Cdd:PRK11831 244 DGIADG-PVPFR 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-245 |
1.47e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPPVSyPQGDILFHGSSLlh 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKI----QALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRA-TSGRIVFDGKDI-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRGVRgNKIAMIFQEPMVSLNplHTLEKQLyevlslhrgmrkeaARGEILdcLDRTGIRNAAKRLSD-FP----- 154
Cdd:PRK11614 70 TDWQTAKIMR-EAVAIVPEGRRVFSR--MTVEENL--------------AMGGFF--AERDQFQERIKWVYElFPrlher 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 -HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAV 229
Cdd:PRK11614 131 rIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYV 209
|
250
....*....|....*.
gi 502863011 230 MQNGRCVEQNTAAALL 245
Cdd:PRK11614 210 LENGHVVLEDTGDALL 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
297-527 |
1.49e-17 |
|
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: 82.98 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDG-----MPLHRWnrRQMLPVRPRMQVVFQDP 371
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswnsVPLQKW--RKAFGVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 -NSSLNPrlsilqiieeglrvhqptlTALQRENEVRRVMAEVGLDpETRHRYPAE-----------FSGGQRQRIAIARA 439
Cdd:cd03289 93 fRKNLDP-------------------YGKWSDEEIWKVAEEVGLK-SVIEQFPGQldfvlvdggcvLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 440 LILKPELIILDEPTSSLDRTVQAQILTLLKglQEKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFTapTQ 519
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLN--EK 227
|
....*...
gi 502863011 520 SYTRQLLS 527
Cdd:cd03289 228 SHFKQAIS 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-236 |
1.55e-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: 81.55 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 15 FSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYpqGDILFHGSSLlHADEQTLRgvrgnkI 94
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPR-KPDQFQKC------V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 95 AMIFQEPMvsLNPLHTLEKQLY--EVLSLHRGM-----RKEAARGEILDCLDrTGIRNAAKRlsdfphQLSGGERQRVMI 167
Cdd:cd03234 84 AYVRQDDI--LLPGLTVRETLTytAILRLPRKSsdairKKRVEDVLLRDLAL-TRIGGNLVK------GISGGERRRVSI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 168 AMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-248 |
1.78e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.67 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIaFSKQGetRTVVSDLSLQIQRGETLALVGESGSGKS--VSALsiLHLLPsppvsYpQGDILFHGSSLLHADE 83
Cdd:PRK11174 350 IEAEDLEI-LSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTslLNAL--LGFLP-----Y-QGSLKINGIELRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLHRgmrKEAARGEILDCLDRTGIRNAAKRLS---DFPHQ---- 156
Cdd:PRK11174 419 ESWR----KHLSWVGQNP-------QLPHGTLRDNVLLGN---PDASDEQLQQALENAWVSEFLPLLPqglDTPIGdqaa 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLaDSVAVMQNGRC 235
Cdd:PRK11174 485 gLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
250
....*....|...
gi 502863011 236 VEQNTAAALLNAP 248
Cdd:PRK11174 562 VQQGDYAELSQAG 574
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
111-457 |
2.08e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 111 LEKQLYEVLSLHR---------GMRKEAARGEILDCLDRTGirnaakrLSDFPH----QLSGGERQRVMIAMALLTRPEL 177
Cdd:NF033858 85 LGKNLYPTLSVFEnldffgrlfGQDAAERRRRIDELLRATG-------LAPFADrpagKLSGGMKQKLGLCCALIHDPDL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 178 LIADEPTTALDVTVQAQILQLLRELRSEL-NMSLLFIThnlsivkklA--------DSVAVMQNGRCVEQNTAAALLNAP 248
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT---------AymeeaerfDWLVAMDAGRVLATGTPAELLART 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 249 QHP-----YTqRLLDSEPAGD--PV---PLQRDSAPLLNVEGlsvsfpirKGILRRVVDQNAVlKNIRFSLRPGESLGLV 318
Cdd:NF033858 229 GADtleaaFI-ALLPEEKRRGhqPVvipPRPADDDDEPAIEA--------RGLTMRFGDFTAV-DHVSFRIRRGEIFGFL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 319 GESGSGKST-----TGLallrLIASQGEILFDGMPLhrwNRRQMlpvRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQ 393
Cdd:NF033858 299 GSNGCGKSTtmkmlTGL----LPASEGEAWLFGQPV---DAGDI---ATRRRVGYMSQAFSLYGELTVRQNLELHARLFH 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 394 ptLTALQRENEVRRVMAEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:NF033858 369 --LPAAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
274-468 |
2.74e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVsfpIRKGILrrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:PRK13539 1 MMLEGEDLAC---VRGGRV--------LFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLIAgllppAAGTIKLDGGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHrwnrrqmLPvRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQptltalQRENEVRRVMAEVGLDPETrHRYPAEFSG 428
Cdd:PRK13539 66 ID-------DP-DVAEACHYLGHRNAMKPALTVAENLEFWAAFLG------GEELDIAAALEAVGLAPLA-HLPFGYLSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLL 468
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-217 |
3.21e-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: 84.33 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQTLRGVrgnkIAMIFQEPmv 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPVSSLDQDEVRRR----VSVCAQDA-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 slnplHTLEKQLYEVLSLHRGmrkEAARGEILDCLDRTGIRNAAKRLSDFPH--------QLSGGERQRVMIAMALLTRP 175
Cdd:TIGR02868 419 -----HLFDTTVRENLRLARP---DATDEELWAALERVGLADWLRALPDGLDtvlgeggaRLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502863011 176 ELLIADEPTTALDVTVQAQILQLLRELRSELnmSLLFITHNL 217
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-270 |
3.94e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 9 DNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLH-ADEQTLR 87
Cdd:PRK10253 11 EQLTLGYGK----YTVAENLTVEIPDGHFTAIIGPNGCGKS-TLLRTLSRLMTPA----HGHVWLDGEHIQHyASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 88 gvrgnKIAMIFQEPMV--SLNPLHTLEKQLYEVLSLHRGMRKEAARGeILDCLDRTGIRNAAKRLSDfphQLSGGERQRV 165
Cdd:PRK10253 82 -----RIGLLAQNATTpgDITVQELVARGRYPHQPLFTRWRKEDEEA-VTKAMQATGITHLADQSVD---TLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALL 245
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
250 260 270
....*....|....*....|....*....|.
gi 502863011 246 NAP--QHPYTQR--LLDSEPAGDP--VPLQR 270
Cdd:PRK10253 233 TAEliERIYGLRcmIIDDPVAGTPlvVPLGR 263
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
273-527 |
4.29e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 APLLNVEGLSVSFPIRKGilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGM 347
Cdd:PRK10535 2 TALLELKDIRRSYPSGEE-------QVEVLKGISLDIYAGEMVAIVGASGSGKST----LMNILgcldkPTSGTYRVAGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 348 PLHRWNRRQMLPVR-PRMQVVFQdpNSSLNPRLSILQIIEeglrvhQPTLTA----LQRENEVRRVMAEVGLDPETRHRy 422
Cdd:PRK10535 71 DVATLDADALAQLRrEHFGFIFQ--RYHLLSHLTAAQNVE------VPAVYAglerKQRLLRAQELLQRLGLEDRVEYQ- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEK-HRLayIFISHDLQVVrALCHQVIVLRQ 501
Cdd:PRK10535 142 PSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTV--IIVTHDPQVA-AQAERVIEIRD 218
|
250 260 270
....*....|....*....|....*....|....
gi 502863011 502 GEVV--------EQGECQRVFTAPTQSYTRQLLS 527
Cdd:PRK10535 219 GEIVrnppaqekVNVAGGTEPVVNTASGWRQFVS 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
272-516 |
4.87e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFpiRKGilrrvvdqNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLH 350
Cdd:PRK15056 3 QQAGIVVNDVTVTW--RNG--------HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKISILGQPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMLPVRPRMQVVfqdpNSSLnPRLsILQIIEEGLRVHQPTLTALQRENE--VRRVMAEVGLdPETRHRYPAEFSG 428
Cdd:PRK15056 73 QALQKNLVAYVPQSEEV----DWSF-PVL-VEDVVMMGRYGHMGWLRRAKKRDRqiVTAALARVDM-VEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRqGEVVEQG 508
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
....*...
gi 502863011 509 ECQRVFTA 516
Cdd:PRK15056 224 PTETTFTA 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-248 |
5.17e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 80.28 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSiafsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppVSYPQGDILFHGS--SLLHADE 83
Cdd:cd03218 1 LRAENLS----KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-----VKPDSGKILLDGQdiTKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGvrgnkIAMIFQEPMV--SLnplhTLEKQLYEVLSLHRGMRKEAARgEILDCLDRTGIRNAAKRLSDfphQLSGGE 161
Cdd:cd03218 72 RARLG-----IGYLPQEASIfrKL----TVEENILAVLEIRGLSKKEREE-KLEELLEEFHITHLRKSKAS---SLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTA 241
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
....*..
gi 502863011 242 AALLNAP 248
Cdd:cd03218 218 EEIAANE 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-248 |
5.57e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSiaFSKQGetRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL--HLLPSppvsypQGDILFHGSSLLHADEQ 84
Cdd:PRK10575 13 ALRNVS--FRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLgrHQPPS------EGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLrgvrGNKIAMIFQEpmvsLNPLHTLekQLYEVLSLHR-------GMRKEAARGEILDCLDRTGIRNAAKRLSDfphQL 157
Cdd:PRK10575 82 AF----ARKVAYLPQQ----LPAAEGM--TVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD---SL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
250
....*....|.
gi 502863011 238 QNTAAALLNAP 248
Cdd:PRK10575 229 QGTPAELMRGE 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-237 |
6.51e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 79.38 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppVSYPQGDILFHGSSLLHADEQT 85
Cdd:cd03369 7 IEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRF-----LEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRgvrgNKIAMIFQEPMV-------SLNPL-HTLEKQLYEVLSLHRGmrkeaarGEildcldrtgirnaakrlsdfphQL 157
Cdd:cd03369 80 LR----SSLTIIPQDPTLfsgtirsNLDPFdEYSDEEIYGALRVSEG-------GL----------------------NL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLaDSVAVMQNGRCVE 237
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
274-508 |
7.04e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFpirKGilRRVVdqnavlKNIRFSLRPGESLGLVGESGSGKSTT-----GLallrLIASQGEILFDG-- 346
Cdd:COG1137 2 MTLEAENLVKSY---GK--RTVV------KDVSLEVNQGEIVGLLGPNGAGKTTTfymivGL----VKPDSGRIFLDGed 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 ---MPLHRwnRRQM----LPvrprmqvvfQDPnsSLNPRLS-------ILQIIEeglrvhqptLTALQRENEVRRVMAEV 412
Cdd:COG1137 67 ithLPMHK--RARLgigyLP---------QEA--SIFRKLTvednilaVLELRK---------LSKKEREERLEELLEEF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 413 GLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLlkglqeKHRLAYIFIS-HDlq 487
Cdd:COG1137 125 GIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHL------KERGIGVLITdHN-- 195
|
250 260
....*....|....*....|....
gi 502863011 488 vVR---ALCHQVIVLRQGEVVEQG 508
Cdd:COG1137 196 -VRetlGICDRAYIISEGKVLAEG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-234 |
9.59e-17 |
|
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: 79.68 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 15 FSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILhllpsppvsypqgdilfhgSSLLHADEQTLRgVRGN-- 92
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKT-TTLKIL-------------------SGLLQPTSGEVR-VAGLvp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 93 ---------KIAMIF-QEPMVS--LNPLHTLE--KQLYEVLSLHRGMRKEaargEILDCLDRTGIRNAAKRlsdfphQLS 158
Cdd:cd03267 86 wkrrkkflrRIGVVFgQKTQLWwdLPVIDSFYllAAIYDLPPARFKKRLD----ELSELLDLEELLDTPVR------QLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-249 |
1.08e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 28 LSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypqGDILFHGSSLLHADEQTLRGVRGnkiAMIFQEPMVSLNP 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS------GSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 108 LhtlekqlYEVLSLHR--GMRKEAARGEILDCLDRTGIrnaAKRLSDFPHQLSGGERQRVMIAMALL-----TRPE--LL 178
Cdd:PRK03695 86 V-------FQYLTLHQpdKTRTEAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 179 IADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLNAPQ 249
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-217 |
1.15e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.74 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFskQGetRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpSPPVSYPQGDILFHGSSLlhADEQ 84
Cdd:PRK11248 1 MLQISHLYADY--GG--KPALEDINLTLESGELLVVLGPSGCGKT----TLLNLI-AGFVPYQHGSITLDGKPV--EGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVrgnkiamIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRlsdFPHQLSGGERQR 164
Cdd:PRK11248 70 AERGV-------VFQNE--GLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502863011 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNL 217
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-234 |
1.29e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.72 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpsppvsypqgdilfhgSSLLHADEQT 85
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI----------------AGELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIfqepmvslnplhtlekqlyevlslhrgmrkeaargeildcldrtgirnaakrlsdfpHQLSGGERQRV 165
Cdd:cd03221 57 VTWGSTVKIGYF---------------------------------------------------------EQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelnmSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
290-492 |
1.55e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 290 GILRRVVDQNaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIasqgeilfdgmplhrWNRRQMLPVrprmQVVFQ 369
Cdd:COG2401 35 GVELRVVERY-VLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL---------------AGALKGTPV----AGCVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSLNPRLSILQIIeeglrvhqptlTALQRENEVRRVMAEVGL-DPETRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:COG2401 91 VPDNQFGREASLIDAI-----------GRKGDFKDAVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502863011 449 LDEPTSSLDRTVqAQIL--TLLKgLQEKHRLAYIFISHDLQVVRAL 492
Cdd:COG2401 160 IDEFCSHLDRQT-AKRVarNLQK-LARRAGITLVVATHHYDVIDDL 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
302-506 |
1.69e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglalLRLIAS--------QGEILFDGMPLHrwnrrqmlpvrprmqvvFQDPNS 373
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST-----LMKVLSgvyphgsyEGEILFDGEVCR-----------------FKDIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 S-------------LNPRLSILQIIEEGlrvHQPTLTAL----QRENEVRRVMAEVGLD--PETRhryPAEFSGGQRQRI 434
Cdd:NF040905 75 SealgiviihqelaLIPYLSIAENIFLG---NERAKRGVidwnETNRRARELLAKVGLDesPDTL---VTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 435 AIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEkHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-498 |
1.80e-16 |
|
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: 82.52 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 33 QRGETLALVGESGSGKSvSALSIL--HLLP-----SPPVSYPqgDIL--FHGSSLlhadeQT-LRGVRGNKIAmifqepm 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKS-TALKILsgELKPnlgdyDEEPSWD--EVLkrFRGTEL-----QDyFKKLANGEIK------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 103 VSLNPlhtlekQLYEVLS-LHRG-----MRKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTRPE 176
Cdd:COG1245 162 VAHKP------QYVDLIPkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDIS---ELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMqngrcveqntaaallnapqhpYtqrl 256
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL---------------------Y---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 257 ldsepaGDPvplqrdsapllNVEGLsVSFP--IRKGIlrrvvdqNAVLK------NIRF--------------------- 307
Cdd:COG1245 287 ------GEP-----------GVYGV-VSKPksVRVGI-------NQYLDgylpeeNVRIrdepiefevhaprrekeeetl 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 308 --------------------SLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEIlfdgmplhrwnrrqmlpvrprmqvv 367
Cdd:COG1245 342 veypdltksyggfsleveggEIREGEVLGIVGPNGIGKTT----FAKILA--GVL------------------------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 368 fqDPNS-SLNPRLSIL---QII--------EEGLR-VHQPTLTALQRENEVRRVMaevGLDPeTRHRYPAEFSGGQRQRI 434
Cdd:COG1245 391 --KPDEgEVDEDLKISykpQYIspdydgtvEEFLRsANTDDFGSSYYKTEIIKPL---GLEK-LLDKNVKDLSGGELQRV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 435 AIARALILKPELIILDEPTSSLD---RTVQAQIltlLKGLQEKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDveqRLAVAKA---IRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-248 |
2.75e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFhg 75
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKT----TVFNCLtgfykPT------GGTILL-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 76 ssllhaDEQTLRGVRGNKIAM-----------IFQEPMVSLNPLHTLEKQLYEvlSLHRGMRKEAA----RGEILD---- 136
Cdd:PRK11300 65 ------RGQHIEGLPGHQIARmgvvrtfqhvrLFREMTVIENLLVAQHQQLKT--GLFSGLLKTPAfrraESEALDraat 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 137 CLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHN 216
Cdd:PRK11300 137 WLERVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
250 260 270
....*....|....*....|....*....|..
gi 502863011 217 LSIVKKLADSVAVMQNGRCVEQNTAAALLNAP 248
Cdd:PRK11300 214 MKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-246 |
2.93e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.01 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 28 LSLQIQRGETLALVGESGSGKSVSalsILHL----LPSppvsypQGDILFHGSSLLHADEQTLRgvrgNKIAMIFQEPMV 103
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTL---LLHLngiyLPQ------RGRVKVMGREVNAENEKWVR----SKVGLVFQDPDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNPLHTLEKQLYEVLSLhrGMRKEaargEILDcldRTGIRNAAKRLSDF----PHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK13647 91 QVFSSTVWDDVAFGPVNM--GLDKD----EVER---RVEEALKAVRMWDFrdkpPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 180 ADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALLN 246
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
302-515 |
3.03e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.28 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFD--GMPLHRWNRRQMLPVRPRMQVVFQDPNSS 374
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqltNGL----IISETGQTIVGdyAIPANLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LnprlsILQIIEEGLRVHQPTLTALQRE--NEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK13645 103 L-----FQETIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 453 TSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFT 515
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-247 |
3.04e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQpLLSIDNLSIAF------------------SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpsp 62
Cdd:COG1134 1 MSS-MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKS----TLLKLI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 63 pvsypqgdilfhgSSLLHADEQTLRgVRGnKIAMIFqEPMVSLNPLHTLEKQLYEVLSLHrGMRKEaargEILDCLDRtg 142
Cdd:COG1134 73 -------------AGILEPTSGRVE-VNG-RVSALL-ELGAGFHPELTGRENIYLNGRLL-GLSRK----EIDEKFDE-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 143 IRNAAkRLSDFPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLS 218
Cdd:COG1134 130 IVEFA-ELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMG 207
|
250 260
....*....|....*....|....*....
gi 502863011 219 IVKKLADSVAVMQNGRCVEQNTAAALLNA 247
Cdd:COG1134 208 AVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
275-508 |
3.13e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 275 LLNVEGLSVSFpirKGilRRVVDqnavlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDG-----MP 348
Cdd:PRK10895 3 TLTAKNLAKAY---KG--RRVVE------DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDedislLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRwnrrqmlpvRPRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQpTLTALQRENEVRRVMAEVGLDpETRHRYPAEFSG 428
Cdd:PRK10895 72 LHA---------RARRGIGYLPQEASIFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHIE-HLRDSMGQSLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEkHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK10895 141 GERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
301-508 |
3.96e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 77.70 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--------GEILFDGMPLHRWNrrqmlpVRPRMQVVFQDPN 372
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTT----LLDAISGRvegggttsGQILFNGQPRKPDQ------FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 --SSLNPRLSILQIIEEGLRVHQPtltalqreNEVRRVMAEVGL-----DPETRHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:cd03234 92 llPGLTVRETLTYTAILRLPRKSS--------DAIRKKRVEDVLlrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 446 LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFIshdlqvvralcHQ-----------VIVLRQGEVVEQG 508
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI-----------HQprsdlfrlfdrILLLSSGEIVYSG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-508 |
4.08e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRqmlpVRPRMQVVFQD 370
Cdd:PRK13537 13 VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARH----ARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 PNssLNPRLSIlqiiEEGLRVHQP--TLTALQRENEVRRVMAEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPELII 448
Cdd:PRK13537 89 DN--LDPDFTV----RENLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 449 LDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-248 |
4.58e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 7 SIDNLSiafsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL-HLLPSPpvsypQGDILFHGSSLLHADEQT 85
Cdd:COG4604 3 EIKNVS----KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD-----SGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LrgvrGNKIAMIFQEPMVSLNpLhTLEkqlyEVLSL-----HRGMRKEAARGEI---LDCLDRTGIRNAakrlsdFPHQL 157
Cdd:COG4604 73 L----AKRLAILRQENHINSR-L-TVR----ELVAFgrfpySKGRLTAEDREIIdeaIAYLDLEDLADR------YLDEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVA 216
|
250
....*....|.
gi 502863011 238 QNTAAALLNAP 248
Cdd:COG4604 217 QGTPEEIITPE 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-233 |
4.77e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFsKQGETrtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppVSYPQGDILFHGSSllh 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTW-RNGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-----VRLASGKISILGQP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 adeqTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRG-MRKEAARgeildclDRTGIRNAAKR--LSDFPH-- 155
Cdd:PRK15056 71 ----TRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGwLRRAKKR-------DRQIVTAALARvdMVEFRHrq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADsVAVMQNG 233
Cdd:PRK15056 140 igELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
297-528 |
5.01e-16 |
|
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: 81.50 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMP-----LHRWnrRQMLPVRPRMQVVFQDP 371
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSwnsvtLQTW--RKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 -NSSLNPRlsilqiieeglrvhqptltALQRENEVRRVMAEVGLDpETRHRYPAE-----------FSGGQRQRIAIARA 439
Cdd:TIGR01271 1308 fRKNLDPY-------------------EQWSDEEIWKVAEEVGLK-SVIEQFPDKldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 440 LILKPELIILDEPTSSLDrTVQAQILTllKGLQEKHRLAYIFISHdlQVVRAL--CHQVIVLRQGEVVEQGECQRVFTap 517
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD-PVTLQIIR--KTLKQSFSNCTVILSE--HRVEALleCQQFLVIEGSSVKQYDSIQKLLN-- 1440
|
250
....*....|.
gi 502863011 518 TQSYTRQLLSA 528
Cdd:TIGR01271 1441 ETSLFKQAMSA 1451
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-215 |
5.24e-16 |
|
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: 75.65 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAfskQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL-HLLPsppvsYPQGDILFHgssllhadeq 84
Cdd:cd03223 1 IELENLSLA---TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKS-SLFRALaGLWP-----WGSGRIGMP---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 tlrgvRGNKIAMIFQEPMVslnPLHTLEKQLYevlslhrgmrkeaargeildcldrtgirnaakrlsdFP--HQLSGGER 162
Cdd:cd03223 62 -----EGEDLLFLPQRPYL---PLGTLREQLI------------------------------------YPwdDVLSGGEQ 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRselnMSLLFITH 215
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
297-491 |
6.19e-16 |
|
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: 76.24 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmLPVRPRMQVVFQDP 371
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTT----LLRILAgllrpDSGEVRWNGTPLAE------QRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSLNPRLSILqiieEGLRVHQPTLTALQREneVRRVMAEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:TIGR01189 81 LPGLKPELSAL----ENLHFWAAIHGGAQRT--IEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
302-505 |
6.76e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEILFD-GmplhRWNRRQMLPVrPRMQvvfQDPnsslnPRL- 379
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKST----LMKILN--GEVLLDdG----RIIYEQDLIV-ARLQ---QDP-----PRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 --SILQIIEEGL--------RVHQ-----------PTLTALQR-------------ENEVRRVMAEVGLDPETRHrypAE 425
Cdd:PRK11147 80 egTVYDFVAEGIeeqaeylkRYHDishlvetdpseKNLNELAKlqeqldhhnlwqlENRINEVLAQLGLDPDAAL---SS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
206-529 |
7.70e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.53 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 206 LNMSLLFITHNLSIVKKladsvAVMQNGRCVEqntaaaLLNAPQHPYtqrlldsepAGDPVPLQRDSAPLLNVeglsvSF 285
Cdd:PRK10790 294 LNEPLIELTTQQSMLQQ-----AVVAGERVFE------LMDGPRQQY---------GNDDRPLQSGRIDIDNV-----SF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 286 PIRkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtgLALLRL---IASQGEILFDGMPLHRWNRRQMlpvRP 362
Cdd:PRK10790 349 AYR--------DDNLVLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyyPLTEGEIRLDGRPLSSLSHSVL---RQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 363 RMQVVFQDP---------NSSLNPRLSilqiiEEglRVHQpTLTALQRENEVRRVmaevgldPETRHRYPAE----FSGG 429
Cdd:PRK10790 416 GVAMVQQDPvvladtflaNVTLGRDIS-----EE--QVWQ-ALETVQLAELARSL-------PDGLYTPLGEqgnnLSVG 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLayIFISHDLQ-VVRAlcHQVIVLRQGEVVEQG 508
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLStIVEA--DTILVLHRGQAVEQG 556
|
330 340
....*....|....*....|....
gi 502863011 509 ECQRVFTAPT---QSYTRQLLSAD 529
Cdd:PRK10790 557 THQQLLAAQGrywQMYQLQLAGEE 580
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-236 |
7.74e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGET---RTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLL-----PSppvsypQGDILFHGSS 77
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLnglhvPT------QGSVRVDDTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 LL-HADEQTLRGVRgNKIAMIFQEPmvslnplhtlEKQLYEVLSL--------HRGMRKEAARGEILDCLDRTGIrnAAK 148
Cdd:PRK13649 71 ITsTSKNKDIKQIR-KKVGLVFQFP----------ESQLFEETVLkdvafgpqNFGVSQEEAEALAREKLALVGI--SES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 149 RLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVA 228
Cdd:PRK13649 138 LFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVY 216
|
....*...
gi 502863011 229 VMQNGRCV 236
Cdd:PRK13649 217 VLEKGKLV 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
274-510 |
8.87e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKGilrrvvdqnavLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDGMP 348
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKA-----------LSGAALNVYPGRVMALVGENGAGKSTmmkvlTGI----YTRDAGSILYLGKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 lhrwnrrqmlpvrprmqVVFQDPNSSLNPRLSIlqiieeglrVHQ-----PTLTA-----LQRE--------------NE 404
Cdd:PRK10762 68 -----------------VTFNGPKSSQEAGIGI---------IHQelnliPQLTIaenifLGREfvnrfgridwkkmyAE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 405 VRRVMAEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISH 484
Cdd:PRK10762 122 ADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISH 199
|
250 260
....*....|....*....|....*.
gi 502863011 485 DLQVVRALCHQVIVLRQGEVVeqGEC 510
Cdd:PRK10762 200 RLKEIFEICDDVTVFRDGQFI--AER 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-249 |
9.36e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsyP-QGDILFHGSSL---- 78
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK------PdSGRIFLDGEDIthlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 79 LHadeqtLRGVRGnkIAMIFQEPMV--SLnplhTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRLSDfphQ 156
Cdd:COG1137 72 MH-----KRARLG--IGYLPQEASIfrKL----TVEDNILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAY---S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALD-VTVqAQILQLLRELRsELNMSLLfIT-HN----LSIVkklaDSVAVM 230
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretLGIC----DRAYII 209
|
250
....*....|....*....
gi 502863011 231 QNGRCVEQNTAAALLNAPQ 249
Cdd:COG1137 210 SEGKVLAEGTPEEILNNPL 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
1.07e-15 |
|
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: 75.58 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAF-SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSIL--------HLLPSPPVSY-PQGDILFHG 75
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgeleklsgSVSVPGSIAYvSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 76 SsllhadeqtlrgVRGNkiaMIFQEPMvslnplhtlEKQLYE-VL---SLHRGMrkeaargEILDCLDRTGIrnAAKRLS 151
Cdd:cd03250 81 T------------IREN---ILFGKPF---------DEERYEkVIkacALEPDL-------EILPDGDLTEI--GEKGIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 dfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQ--LLRELRseLNMSLLFITHNLSIVKKlADSVAV 229
Cdd:cd03250 128 -----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLL--NNKTRILVTHQLQLLPH-ADQIVV 199
|
....*
gi 502863011 230 MQNGR 234
Cdd:cd03250 200 LDNGR 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-248 |
1.17e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 25 VSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsyPQ-GDILFHGSSLlhADEQTLRGVRgNKIAMIFQEPmv 103
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR------PQkGKVLVSGIDT--GDFSKLQGIR-KLVGIVFQNP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 slnplhtlEKQLyevlsLHRGMRKEAARGEILDCLDRTGIRNAAKR------LSDF----PHQLSGGERQRVMIAMALLT 173
Cdd:PRK13644 87 --------ETQF-----VGRTVEEDLAFGPENLCLPPIEIRKRVDRalaeigLEKYrhrsPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 174 RPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVkKLADSVAVMQNGRCVEQNTAAALLNAP 248
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
156-457 |
1.33e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.29 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 236 VEQNTAAALLnapQHPYTQRLLDSEPAGDpVPLQRDSAPLLNVEGLSVSFPIrkgILRRVV---DQNAVLKNIRFSLRPG 312
Cdd:PRK10938 214 AETGEREEIL---QQALVAQLAHSEQLEG-VQLPEPDEPSARHALPANEPRI---VLNNGVvsyNDRPILHNLSWQVNPG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 313 ESLGLVGESGSGKSTtglaLLRLIAS---QGE----ILFD---GMPLHRWN-RRQMLPVRPRMQvvfQDPNSSLNPRLSI 381
Cdd:PRK10938 287 EHWQIVGPNGAGKST----LLSLITGdhpQGYsndlTLFGrrrGSGETIWDiKKHIGYVSSSLH---LDYRVSTSVRNVI 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 382 LQIIEEGLRVHQPTLTALQRenEVRRVMAEVGLDPETRHRYPAEFSGGQrQRIA-IARALILKPELIILDEPTSSLD 457
Cdd:PRK10938 360 LSGFFDSIGIYQAVSDRQQK--LAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
274-513 |
1.45e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKGilrrvvdqnavLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMP 348
Cdd:PRK09700 4 PYISMAGIGKSFGPVHA-----------LKSVNLTVYPGEIHALLGENGAGKST----LMKVLSgihepTKGTITINNIN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 349 LHRWNRRqmLPVRPRMQVVFQDpnSSLNPRLSILQIIEEG-LRVHQPTLTALQRENEVRRVMAE----VGL--DPETRhr 421
Cdd:PRK09700 69 YNKLDHK--LAAQLGIGIIYQE--LSVIDELTVLENLYIGrHLTKKVCGVNIIDWREMRVRAAMmllrVGLkvDLDEK-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 422 yPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK09700 143 -VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKD 220
|
250
....*....|..
gi 502863011 502 GEVVEQGECQRV 513
Cdd:PRK09700 221 GSSVCSGMVSDV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-486 |
2.15e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 32 IQRGETLALVGESGSGKSvSALSIL--HLLP-----SPPVSYPqgDIL--FHGSSLlhadeQT-LRGVRGNKIAMIFQEP 101
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKT-TAVKILsgELIPnlgdyEEEPSWD--EVLkrFRGTEL-----QNyFKKLYNGEIKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 102 MVSLNPlhtleKQL----YEVLslhrgmRKEAARGEILDCLDRTGIRNAAKRlsDFpHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK13409 168 YVDLIP-----KVFkgkvRELL------KKVDERGKLDEVVERLGLENILDR--DI-SELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 178 LIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLADSVAVMqngrcveqntaaallnapqhpYtqrll 257
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA---------------------Y----- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 258 dSEPAGDPVplqrdsapllnveglsVSFP--IRKGIlrrvvdqNAVLK------NIR----------------------- 306
Cdd:PRK13409 286 -GEPGAYGV----------------VSKPkgVRVGI-------NEYLKgylpeeNMRirpepiefeerpprdeseretlv 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 307 -----------FSL-------RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDgmplhrwnrrqmLPVRPR 363
Cdd:PRK13409 342 eypdltkklgdFSLeveggeiYEGEVIGIVGPNGIGKTT----FAKLLAgvlkpDEGEVDPE------------LKISYK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 364 MQVVFQDPNSSlnprlsilqiIEEGLRVHQPTLTALQRENEVRRVMaevGLDP--EtrhRYPAEFSGGQRQRIAIARALI 441
Cdd:PRK13409 406 PQYIKPDYDGT----------VEDLLRSITDDLGSSYYKSEIIKPL---QLERllD---KNVKDLSGGELQRVAIAACLS 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 502863011 442 LKPELIILDEPTSSLDrtVQAQILT--LLKGLQEKHRLAYIFISHDL 486
Cdd:PRK13409 470 RDADLYLLDEPSAHLD--VEQRLAVakAIRRIAEEREATALVVDHDI 514
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
421-508 |
3.38e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:PRK11144 124 RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLE 203
|
....*...
gi 502863011 501 QGEVVEQG 508
Cdd:PRK11144 204 QGKVKAFG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
301-497 |
3.63e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILfdgmplhrwnrrqmlpVRPRMQVVFQDPNSSL 375
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKST----LLKVLAgvlrpTSGTVR----------------RAGGARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRL--SILQIIEEGLRVHQPTLTALQREN--EVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:NF040873 67 PDSLplTVRDLVAMGRWARRGLWRRLTRDDraAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVL 190
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
292-457 |
4.34e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.05 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQN-AVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILF-DGMplhrwnRRQMLPvrprm 364
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkdFNGEARPqPGI------KVGYLP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 365 qvvfQDPnsSLNPRLSILQIIEEGLrvhQPTLTALQRENEVRRVMAEV----------------------GLDPETR--- 419
Cdd:TIGR03719 75 ----QEP--QLDPTKTVRENVEEGV---AEIKDALDRFNEISAKYAEPdadfdklaaeqaelqeiidaadAWDLDSQlei 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502863011 420 ----HRYP------AEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:TIGR03719 146 amdaLRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-508 |
7.36e-15 |
|
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: 73.33 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSfpirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDG-----M 347
Cdd:cd03217 1 LEIKDLHVS-----------VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGeditdL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 348 PLHRWNRRQMLpvrprmqVVFQDPnsslnPRLsilqiieEGLRVhqptltalqrENEVRRVmaEVGldpetrhrypaeFS 427
Cdd:cd03217 70 PPEERARLGIF-------LAFQYP-----PEI-------PGVKN----------ADFLRYV--NEG------------FS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVI-VLRQGEVVE 506
Cdd:cd03217 107 GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVhVLYDGRIVK 185
|
..
gi 502863011 507 QG 508
Cdd:cd03217 186 SG 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
297-491 |
1.03e-14 |
|
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: 72.91 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwnrrqmlpVRPRMQ--VVFQ 369
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTT----LLRILAglsppLAGRVLLNGGPLDF--------QRDSIArgLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSLNPRLSILqiieEGLRVhqptLTALQRENEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03231 79 GHAPGIKTTLSVL----ENLRF----WHADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502863011 450 DEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
272-508 |
1.16e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSfpirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEILF 344
Cdd:CHL00131 4 NKPILEIKNLHAS-----------VNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAGhpaykilEGDILF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 345 DGmplhrwnrRQMLPVRPRMQ------VVFQDP----------------NS--------SLNPrLSILQIIEEGLRVhqp 394
Cdd:CHL00131 69 KG--------ESILDLEPEERahlgifLAFQYPieipgvsnadflrlayNSkrkfqglpELDP-LEFLEIINEKLKL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 395 tltalqrenevrrvmaeVGLDPETRHRYPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILTLLK 469
Cdd:CHL00131 137 -----------------VGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMT 199
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 502863011 470 glQEKhrlAYIFISHdLQvvRALCH----QVIVLRQGEVVEQG 508
Cdd:CHL00131 200 --SEN---SIILITH-YQ--RLLDYikpdYVHVMQNGKIIKTG 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
294-509 |
1.17e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 294 RVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGeilFDGMPLHRwNRRQMLPVRPRMQVVFQDpnS 373
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILAN-NRKPTKQILKRTGFVTQD--D 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 374 SLNPRLSILQ--IIEEGLRVHQpTLTALQRENEVRRVMAEVGL----DPETRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PLN03211 150 ILYPHLTVREtlVFCSLLRLPK-SLTKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 448 ILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
272-508 |
1.19e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSFpirKGILrrvvdqnAVlKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEILFDG 346
Cdd:PRK11300 2 SQPLLSVSGLMMRF---GGLL-------AV-NNVNLEVREQEIVSLIGPNGAGKTTvfnclTGF----YKPTGGTILLRG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNRRQMlpvrPRMQVV--FQdpnsslNPRLSILQIIEEGLRVHQ------PTLTALQRENEVRRVMAE------- 411
Cdd:PRK11300 67 QHIEGLPGHQI----ARMGVVrtFQ------HVRLFREMTVIENLLVAQhqqlktGLFSGLLKTPAFRRAESEaldraat 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 412 ----VGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQ 487
Cdd:PRK11300 137 wlerVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMK 215
|
250 260
....*....|....*....|.
gi 502863011 488 VVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK11300 216 LVMGISDRIYVVNQGTPLANG 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
274-501 |
2.41e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 274 PLLNVEGLSVSFPIRKgilrrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILfdgmplhrw 352
Cdd:PRK09544 3 SLVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIK--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 353 nRRQMLPVRPRMQVVFQDPNSSLNprLSILQIIEEGLRvHQPTLTALqrenevRRVMAEVGLDPETRhrypaEFSGGQRQ 432
Cdd:PRK09544 63 -RNGKLRIGYVPQKLYLDTTLPLT--VNRFLRLRPGTK-KEDILPAL------KRVQAGHLIDAPMQ-----KLSGGETQ 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 433 RIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK09544 128 RVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-241 |
2.43e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAFSkqgeTRTVVSDLSLQIQRGETLALVGESGSGKSVSALSIL-HllpsPPVSYPQGDILFHGSSLL 79
Cdd:CHL00131 3 KNKPILEIKNLHASVN----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgH----PAYKILEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 80 HAdEQTLRGVRGnkIAMIFQEPM----VS--------------------LNPLhtlekQLYEVLSlhrgmrkeaargEIL 135
Cdd:CHL00131 75 DL-EPEERAHLG--IFLAFQYPIeipgVSnadflrlaynskrkfqglpeLDPL-----EFLEIIN------------EKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 136 DCLDRTgirnaakrlSDFPHQ-----LSGGERQRVMI-AMALLtRPELLIADEPTTALDVTVQAQILQLLRELRSELNmS 209
Cdd:CHL00131 135 KLVGMD---------PSFLSRnvnegFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSEN-S 203
|
250 260 270
....*....|....*....|....*....|....*
gi 502863011 210 LLFITHN---LSIVKklADSVAVMQNGRCVEQNTA 241
Cdd:CHL00131 204 IILITHYqrlLDYIK--PDYVHVMQNGKIIKTGDA 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-246 |
3.96e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.71 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSIAF---SKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpSPPVsypqGDIlfhgsS 77
Cdd:PRK13536 30 KASIPGSMSTVAIDLagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-SPDA----GKI-----T 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 78 LLHADEQTLRGVRGNKIAMIFQepMVSLNPLHTLEKQLYeVLSLHRGMRKEAARGEILDCLDRTGIRNAAK-RLSDfphq 156
Cdd:PRK13536 100 VLGVPVPARARLARARIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADaRVSD---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSeLNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
250
....*....|
gi 502863011 237 EQNTAAALLN 246
Cdd:PRK13536 252 AEGRPHALID 261
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-201 |
4.03e-14 |
|
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: 71.24 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAfskQGEtRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpSPPVSypqGDILFHGSSLlhadeQT 85
Cdd:TIGR01189 1 LAARNLACS---RGE-RMLFEGLSFTLNAGEALQVTGPNGIGKT-TLLRILAGL-LRPDS---GEVRWNGTPL-----AE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLHRGmrkeaARGEILDCLDRTGIRNAAKRLSdfpHQLSGGERQRV 165
Cdd:TIGR01189 67 QRDEPHENILYLGHLP--GLKPELSALENLHFWAAIHGG-----AQRTIEDALAAVGLTGFEDLPA---AQLSAGQQRRL 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRE 201
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-234 |
4.21e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSiafskqGETrtvVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpSPPVSypqGDILFHGssllhad 82
Cdd:PRK15439 266 APVLTVEDLT------GEG---FRNISLEVRAGEILGLAGVVGAGRTELAETLYGL--RPARG---GRIMLNG------- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 eqtlRGVRGNKIAMIFQEPMVSL------NPLHtLEKQLY-EVLSLHRGMR-------KEAARgeildcLDR-------- 140
Cdd:PRK15439 325 ----KEINALSTAQRLARGLVYLpedrqsSGLY-LDAPLAwNVCALTHNRRgfwikpaRENAV------LERyrralnik 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 141 -TGIRNAAKRLSdfphqlsGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSI 219
Cdd:PRK15439 394 fNHAEQAARTLS-------GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEE 465
|
250
....*....|....*
gi 502863011 220 VKKLADSVAVMQNGR 234
Cdd:PRK15439 466 IEQMADRVLVMHQGE 480
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
300-508 |
4.42e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 300 AVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRqmlpVRPRMQVVFQDPNssLNPR 378
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARL----ARARIGVVPQFDN--LDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 379 LSIlqiiEEGLRVHQPTLTALQRENE--VRRVMAEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13536 129 FTV----RENLLVFGRYFGMSTREIEavIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502863011 457 DRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-247 |
5.03e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 1 MTQPLLSIDNLSiafsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSaLSILHLLPSPPVsypqGDILFHGSSLLH 80
Cdd:PRK13537 3 MSVAPIDFRNVE----KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTT-LRMLLGLTHPDA----GSISLCGEPVPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 81 ADEQTLRgvrgnKIAMIFQepMVSLNPLHTLEKQLyEVLSLHRGMRKEAARGEILDCLDRTGIRNAAK-RLSDfphqLSG 159
Cdd:PRK13537 74 RARHARQ-----RVGVVPQ--FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADaKVGE----LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQN 239
Cdd:PRK13537 142 GMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
....*...
gi 502863011 240 TAAALLNA 247
Cdd:PRK13537 221 APHALIES 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
288-508 |
5.69e-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: 74.98 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 288 RKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMlpvRPRMQV 366
Cdd:TIGR00957 1288 RNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDL---RFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 367 VFQDP---NSSLNPRLSILQIIEEglrvhQPTLTALqrenEVRRVMAEVGLDPETRHRYPAE----FSGGQRQRIAIARA 439
Cdd:TIGR00957 1365 IPQDPvlfSGSLRMNLDPFSQYSD-----EEVWWAL----ELAHLKTFVSALPDKLDHECAEggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 440 LILKPELIILDEPTSSL----DRTVQAQILTLLKG---LQEKHRLAYIfishdLQVVRalchqVIVLRQGEVVEQG 508
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVdletDNLIQSTIRTQFEDctvLTIAHRLNTI-----MDYTR-----VIVLDKGEVAEFG 1501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
301-506 |
6.90e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHR---WNRRQMLPVRPRMQVVFQ------- 369
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKfglMDLRKVLGIIPQAPVLFSgtvrfnl 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSLNPrlsiLQIIEEGLRVHqptLTALQRENEVrrvmaevGLDPETrhrypAE----FSGGQRQRIAIARALILKPE 445
Cdd:PLN03130 1334 DPFNEHND----ADLWESLERAH---LKDVIRRNSL-------GLDAEV-----SEagenFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 446 LIILDEPTSSLDRTVQAQIltlLKGLQEKHR-LAYIFISHDLQVVRAlCHQVIVLRQGEVVE 506
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALI---QKTIREEFKsCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
292-457 |
7.00e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.00 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQN-AVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGE-ILFDGMplhrwnRRQMLPvrprm 364
Cdd:PRK11819 12 VSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkeFEGEaRPAPGI------KVGYLP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 365 qvvfQDPnsSLNPRLSILQIIEEGLrvhQPTLTALQRENEVRRVMAEV----------------------GLDPETR--- 419
Cdd:PRK11819 77 ----QEP--QLDPEKTVRENVEEGV---AEVKAALDRFNEIYAAYAEPdadfdalaaeqgelqeiidaadAWDLDSQlei 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502863011 420 ----HRYP------AEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK11819 148 amdaLRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-250 |
7.18e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYP---QGDILFHGSSLLHADEQTLRGVRgnkiAMIF 98
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGarvTGDVTLNGEPLAAIDAPRLARLR----AVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 99 Q--EPMVSLNplhtlekqLYEVLSL------HRGMRKEAARGEILDC-LDRTGIRNAAKRlsDFPhQLSGGERQRVMIAM 169
Cdd:PRK13547 90 QaaQPAFAFS--------AREIVLLgryphaRRAGALTHRDGEIAWQaLALAGATALVGR--DVT-TLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 170 AL---------LTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNT 240
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250
....*....|
gi 502863011 241 AAALLNaPQH 250
Cdd:PRK13547 239 PADVLT-PAH 247
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
301-506 |
7.44e-14 |
|
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: 71.48 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDG-----MPLHrwnrrqmlPVRPRMQVVFQDP--- 371
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVdIFDGKIVIDGidiskLPLH--------TLRSRLSIILQDPilf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 ----NSSLNPRLSIL-QIIEEGLRVHQPTLTALQRENEVRRVMAEVGldpetrhrypAEFSGGQRQRIAIARALILKPEL 446
Cdd:cd03288 108 sgsiRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502863011 447 IILDEPTSSLD----RTVQAQILTLLKG---LQEKHRLAYIFIShdlqvvralcHQVIVLRQGEVVE 506
Cdd:cd03288 178 LIMDEATASIDmateNILQKVVMTAFADrtvVTIAHRVSTILDA----------DLVLVLSRGILVE 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
302-508 |
7.57e-14 |
|
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: 70.37 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--------GEILFDGMPLHRWNRrqmlpvRPRMQVVF---QD 370
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCST----LLKALANRtegnvsveGDIHYNGIPYKEFAE------KYPGEIIYvseED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 pnsslnprlsilqiieeglrVHQPTLTalqreneVRRVmaevgLDPETR---HRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:cd03233 93 --------------------VHFPTLT-------VRET-----LDFALRckgNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 448 ILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIF-ISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
301-528 |
8.12e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDPnsslnprl 379
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVeVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDP-------- 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 silqIIEEGlRVHQ---PTLTAlqRENEVRRVMAEVGLdpetRHRYPAE--------------FSGGQRQRIAIARALIL 442
Cdd:PTZ00243 1394 ----VLFDG-TVRQnvdPFLEA--SSAEVWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 443 KPE-LIILDEPTSS----LDRTVQAQILTLLKglqekhrlAY--IFISHDLQVVrALCHQVIVLRQGEVVEQGEcQRVFT 515
Cdd:PTZ00243 1463 KGSgFILMDEATANidpaLDRQIQATVMSAFS--------AYtvITIAHRLHTV-AQYDKIIVMDHGAVAEMGS-PRELV 1532
|
250
....*....|...
gi 502863011 516 APTQSYTRQLLSA 528
Cdd:PTZ00243 1533 MNRQSIFHSMVEA 1545
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-234 |
1.28e-13 |
|
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: 73.24 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQT 85
Cdd:COG4618 331 LSVENLTVVP--PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP--PTA---GSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LrgvrGNKIAMIFQEPmvslnplhtlekQLYEvlslhrGMRKEA-ARgeiLDCLDRTGIRNAAK---------------- 148
Cdd:COG4618 404 L----GRHIGYLPQDV------------ELFD------GTIAENiAR---FGDADPEKVVAAAKlagvhemilrlpdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 149 -RLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVkKLADSV 227
Cdd:COG4618 459 tRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKL 536
|
....*..
gi 502863011 228 AVMQNGR 234
Cdd:COG4618 537 LVLRDGR 543
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
279-505 |
1.31e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 279 EGLSVSFPIRKGilrrvvdqnavLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEILFDGMPLHRWNRRQM 357
Cdd:PRK10982 2 SNISKSFPGVKA-----------LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkDSGSILFQGKEIDFKSSKEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 358 LPVRPRMqvVFQDPNSSLnpRLSILQII------EEGLRVHQPTLTalqreNEVRRVMAEVGLDPETRHRYpAEFSGGQR 431
Cdd:PRK10982 71 LENGISM--VHQELNLVL--QRSVMDNMwlgrypTKGMFVDQDKMY-----RDTKAIFDELDIDIDPRAKV-ATLSVSQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK10982 141 QMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-236 |
1.42e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.60 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 10 NLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVSyPQGDILFHGSSLLHADEQTLRGV 89
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCS-TLLKALANRTEGNVS-VEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 90 rgnkiamIFqepmVSLNPLH----TLEKQLYEVLSLhRGmrKEAARGeildcldrtgirnaakrlsdfphqLSGGERQRV 165
Cdd:cd03233 86 -------IY----VSEEDVHfptlTVRETLDFALRC-KG--NEFVRG------------------------ISGGERKRV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 166 MIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLS-IVKKLADSVAVMQNGRCV 236
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-237 |
2.45e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSvsAL--SILHLLPsppvsyPQGDILFHGSSLlha 81
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS--TLlkLLAGELE------PDSGTVKLGETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 deqtlrgvrgnKIAMIFQEPMvSLNPlhtlEKQLYEVLS-LHRGMRKEAARGeILDCLDRTGIRnAAKRLSDfphqLSGG 160
Cdd:COG0488 379 -----------KIGYFDQHQE-ELDP----DKTVLDELRdGAPGGTEQEVRG-YLGRFLFSGDD-AFKPVGV----LSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVtvqaqilqllrELRSELNMSL-------LFITHNLSIVKKLADSVAVMQNG 233
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDI-----------ETLEALEEALddfpgtvLLVSHDRYFLDRVATRILEFEDG 505
|
....
gi 502863011 234 RCVE 237
Cdd:COG0488 506 GVRE 509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-232 |
2.64e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSLLhaDEQTLRGVRgNKIAMIFQEPMV 103
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPT----EGDIIINDSHNL--KDINLKWWR-SKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 --------------SLNPLHTLEKQL-------YEVLSLHRGMRKEAAR--GEILDCLDRTGIRNAAKR----------- 149
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEALSNYYnedgndsQENKNKRNSCRAKCAGdlNDMSNTTDSNELIEMRKNyqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 150 ------LSDF---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNM 208
Cdd:PTZ00265 552 vskkvlIHDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|....
gi 502863011 209 SLLFITHNLSIVkKLADSVAVMQN 232
Cdd:PTZ00265 632 ITIIIAHRLSTI-RYANTIFVLSN 654
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-234 |
2.71e-13 |
|
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: 72.38 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAfsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsYPQGDILFHGSSLLHADEQT 85
Cdd:TIGR01842 317 LSVENVTIV--PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDGADLKQWDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LrgvrGNKIAMIFQEpmvslnplhtlekqlyevLSLHRGMRKE-AARGEilDCLDRTGIRNAAKrLSD-------FPH-- 155
Cdd:TIGR01842 390 F----GKHIGYLPQD------------------VELFPGTVAEnIARFG--ENADPEKIIEAAK-LAGvhelilrLPDgy 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 ---------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVkKLADS 226
Cdd:TIGR01842 445 dtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDK 522
|
....*...
gi 502863011 227 VAVMQNGR 234
Cdd:TIGR01842 523 ILVLQDGR 530
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
297-515 |
2.87e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKST---------TGLALLRLIASQGEILFDGMPLHRWNRRQMlpvrPRMQVV 367
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTllkalagdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRL----ARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 368 FQDPNSSLNPrLSILQIIEEGLRVHQPTLTALQRENE--VRRVMAEVGLDPETRhRYPAEFSGGQRQRIAIARAL----- 440
Cdd:PRK13547 88 LPQAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGeiAWQALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 441 ----ILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFT 515
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
297-468 |
3.64e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEILFDGMPLHRwnrrqmlpVRPrmqvvfqDP 371
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTS----LLRILAGlarpdAGEVLWQGEPIRR--------QRD-------EY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 NSSL---------NPRLSIlqiiEEGLRVHQPtLTALQRENEVRRVMAEVGLdpETRHRYPAE-FSGGQRQRIAIARALI 441
Cdd:PRK13538 73 HQDLlylghqpgiKTELTA----LENLRFYQR-LHGPGDDEALWEALAQVGL--AGFEDVPVRqLSAGQQRRVALARLWL 145
|
170 180
....*....|....*....|....*..
gi 502863011 442 LKPELIILDEPTSSLDRTVQAQILTLL 468
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-200 |
3.65e-13 |
|
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: 68.29 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpSPPVSypqGDILFHGSSLlhaDEQtlRGVRGNKIAMIFQEP 101
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKT-TLLRILAGL-SPPLA---GRVLLNGGPL---DFQ--RDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 102 MVslnplhtleKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNaakrLSDFP-HQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03231 83 GI---------KTTLSVLENLRFWHADHSDEQVEEALARVGLNG----FEDRPvAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180
....*....|....*....|
gi 502863011 181 DEPTTALDVTVQAQILQLLR 200
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMA 169
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-248 |
5.26e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.28 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 14 AFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLPSPpVSYPQGDILFHGSSLLHADEQTLRGvrgnK 93
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRH-FDVSEGDIRFHDIPLTKLQLDSWRS----R 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 94 IAMIFQEPM---------VSLNPLHTLEKQLYEV----------LSLHRGMRKEAA-RGEILdcldrtgirnaakrlsdf 153
Cdd:PRK10789 391 LAVVSQTPFlfsdtvannIALGRPDATQQEIEHVarlasvhddiLRLPQGYDTEVGeRGVML------------------ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 154 phqlSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElnMSLLFITHNLSIVKKlADSVAVMQNG 233
Cdd:PRK10789 453 ----SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHG 525
|
250
....*....|....*
gi 502863011 234 RCVEQNTAAALLNAP 248
Cdd:PRK10789 526 HIAQRGNHDQLAQQS 540
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-230 |
5.48e-13 |
|
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: 68.93 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 35 GETLALVGESGSGKSvSALSIL--HLLP------SPPvSYPqgDIL--FHGSSLlhadEQTLRGVRGNKIAMIFQEPMVS 104
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALKILagKLKPnlgkfdDPP-DWD--EILdeFRGSEL----QNYFTKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 105 LNPlHTLEKQLYEVLSlhrgmrKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:cd03236 98 LIP-KAVKGKVGELLK------KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502863011 185 TALDVTVQAQILQLLRELRSELNmSLLFITHNLSIVKKLADSVAVM 230
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
297-490 |
7.72e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIrfslrpgESLGLVGESGSGKSTTglallrLIASQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQDPnssLN 376
Cdd:PTZ00265 1247 EQNVGMKNV-------NEFSLTKEGGSGEDST------VFKNSGKILLDGVDICDYNLKDL---RNLFSIVSQEP---ML 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIEEGlrvhqptltalqREN----EVRRVMAEVGLD------PETRHR----YPAEFSGGQRQRIAIARALIL 442
Cdd:PTZ00265 1308 FNMSIYENIKFG------------KEDatreDVKRACKFAAIDefieslPNKYDTnvgpYGKSLSGGQKQRIAIARALLR 1375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502863011 443 KPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVR 490
Cdd:PTZ00265 1376 EPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-249 |
9.64e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLP--SPPVSYPQGDIlfhgsSLLHAD 82
Cdd:PRK10895 3 TLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrdAGNIIIDDEDI-----SLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRGV-RGNKIAMIFQEPMVSLNPLHTLEKQLyevlSLHRGMRKEAARgEILDCLDRTGIRNaakrlsDFPHQLSGGE 161
Cdd:PRK10895 74 ARARRGIgYLPQEASIFRRLSVYDNLMAVLQIRD----DLSAEQREDRAN-ELMEEFHIEHLRD------SMGQSLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTA 241
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
....*...
gi 502863011 242 AALLNAPQ 249
Cdd:PRK10895 222 TEILQDEH 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-238 |
1.00e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSILHLL-PSppvsypQGDILFHGSSLLHAdEQTLRGVRgNKIAMIFQEPm 102
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ------KGAVLWQGKPLDYS-KRGLLALR-QQVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 103 vslnplhtlEKQLYEV-------LSLhRGMrkEAARGEILDCLDRTGIRNAAKRLSDFPHQ-LSGGERQRVMIAMALLTR 174
Cdd:PRK13638 87 ---------EQQIFYTdidsdiaFSL-RNL--GVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 175 PELLIADEPTTALDVTVQAQILQLLRELRSELNmSLLFITHNLSIVKKLADSVAVMQNGRCVEQ 238
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
276-503 |
1.40e-12 |
|
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: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFPirkgilRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILfdgmplhrwnr 354
Cdd:cd03250 1 ISVEDASFTWD------SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVS----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 355 rqmlpVRPRMQVVFQDP---NSSLnpRLSIL---QIIEEglRVHQpTLTALQRENEVRRV----MAEVG-----Ldpetr 419
Cdd:cd03250 64 -----VPGSIAYVSQEPwiqNGTI--RENILfgkPFDEE--RYEK-VIKACALEPDLEILpdgdLTEIGekginL----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 420 hrypaefSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILT-LLKGLQEKHRlAYIFISHDLQVVRAlCHQVIV 498
Cdd:cd03250 129 -------SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNK-TRILVTHQLQLLPH-ADQIVV 199
|
....*
gi 502863011 499 LRQGE 503
Cdd:cd03250 200 LDNGR 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-236 |
1.41e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSypqGDILFHGSSLlhaD 82
Cdd:PLN03211 62 KRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT---GTILANNRKP---T 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRgvrgnKIAMIFQEPMvsLNPLHTLEKQLY--EVLSLHRGMRKEAARGEILDCLDRTGIRNAAKRL--SDFPHQLS 158
Cdd:PLN03211 136 KQILK-----RTGFVTQDDI--LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
301-505 |
3.38e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNR----RQMLPVRPRMQVVFQdp 371
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLcgdprATSGRIVFDGKDITDWQTakimREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 nsslnpRLSIlqiiEEGLRVHQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK11614 94 ------RMTV----EENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 452 PTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRaLCHQVIVLRQGEVV 505
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALK-LADRGYVLENGHVV 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-231 |
4.11e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNlsIAFskQGETRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPVsypqGDILFHGSSLLHADE 83
Cdd:PRK10247 6 PLLQLQN--VGY--LAGDAKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPTS----GTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRGMRKEAA-RGEILDCLDRTGIRNA--AKRLSDfphqLSGG 160
Cdd:PRK10247 77 EIYR----QQVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPdPAIFLDDLERFALPDTilTKNIAE----LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKlADSVAVMQ 231
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
157-247 |
6.12e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSVAVMQNGRC- 235
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIs 474
|
90
....*....|....*.
gi 502863011 236 ----VEQNTAAALLNA 247
Cdd:PRK10762 475 geftREQATQEKLMAA 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-234 |
6.89e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSiAFSKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHllpsppvSYP---QGDILFHGSSLlhA 81
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-------AYPgkfEGNVFINGKPV--D 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 82 DEQTLRGVRgNKIAMIFQE-------PMVSLNPLHTLEKqlyevlslhrgMRKEAARGEILDCLDRTGIRNAAKRLS--- 151
Cdd:TIGR02633 327 IRNPAQAIR-AGIAMVPEDrkrhgivPILGVGKNITLSV-----------LKSFCFKMRIDAAAELQIIGSAIQRLKvkt 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 ---DFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLADSV 227
Cdd:TIGR02633 395 aspFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRV 473
|
....*..
gi 502863011 228 AVMQNGR 234
Cdd:TIGR02633 474 LVIGEGK 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-485 |
8.14e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 22 RTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL---------HLLPSP--PVSY----PQGDilfhgssllhaDEQTL 86
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkdfngEARPQPgiKVGYlpqePQLD-----------PTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 87 RGV-------------RGNKIAMIFQEPMVSLNPLhtLEKQlyevlslhrgmrkeaarGEILDCLDRTGIRNAAKRLS-- 151
Cdd:TIGR03719 86 RENveegvaeikdaldRFNEISAKYAEPDADFDKL--AAEQ-----------------AELQEIIDAADAWDLDSQLEia 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 ---------DFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelnmSLLFITHNLSIVK 221
Cdd:TIGR03719 147 mdalrcppwDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHDRYFLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 222 KLADSVAVMQNGRCV-------------------EQNTAAALLNAPQ-----------------------------HPYT 253
Cdd:TIGR03719 223 NVAGWILELDRGRGIpwegnysswleqkqkrleqEEKEESARQKTLKrelewvrqspkgrqakskarlaryeellsQEFQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSE---PAGdpvplQRDSAPLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtgl 330
Cdd:TIGR03719 303 KRNETAEiyiPPG-----PRLGDKVIEAENLTKAF-----------GDKLLIDDLSFKLPPGGIVGVIGPNGAGKST--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 331 aLLRLIASQ-----GEIlfdgmplhrwnrrqmlPVRPRMQVVFQDPN-SSLNPRLSILQIIEEGLRVhqptLTALQRENE 404
Cdd:TIGR03719 364 -LFRMITGQeqpdsGTI----------------EIGETVKLAYVDQSrDALDPNKTVWEEISGGLDI----IKLGKREIP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 405 VRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAqiltLLKGLQEKHRLAYIfIS 483
Cdd:TIGR03719 423 SRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDvETLRA----LEEALLNFAGCAVV-IS 497
|
..
gi 502863011 484 HD 485
Cdd:TIGR03719 498 HD 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-489 |
1.15e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSKQgetrTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL--------------------HLLPSPPv 64
Cdd:PRK11147 3 LISIHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKS-TLMKILngevllddgriiyeqdlivaRLQQDPP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 65 SYPQGDI-------LFHGSSLLHADEQTLRgvrgnkiaMIFQEPMVS-LNPLhtleKQLYEVLSLHRGMRKEAargEILD 136
Cdd:PRK11147 77 RNVEGTVydfvaegIEEQAEYLKRYHDISH--------LVETDPSEKnLNEL----AKLQEQLDHHNLWQLEN---RINE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 137 CLDRTGIrNAAKRLSDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelnmSLLFITHN 216
Cdd:PRK11147 142 VLAQLGL-DPDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 217 LSIVKKLADSVAVMQNGRCV--------------EQNTAAALLNApqhpytqrLLDSEPAGDPV---------------- 266
Cdd:PRK11147 213 RSFIRNMATRIVDLDRGKLVsypgnydqyllekeEALRVEELQNA--------EFDRKLAQEEVwirqgikarrtrnegr 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 267 -----PLQRDSAPLLNVEG---LSVSFPIRKG-ILRRV------VDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtgla 331
Cdd:PRK11147 285 vralkALRRERSERREVMGtakMQVEEASRSGkIVFEMenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTT---- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 332 LLRLIAsqGEILFDGMPLHrwnrrqmlpVRPRMQVVFQDP-NSSLNPRLSILQIIEEGlrvhqptltalQRENEV----R 406
Cdd:PRK11147 361 LLKLML--GQLQADSGRIH---------CGTKLEVAYFDQhRAELDPEKTVMDNLAEG-----------KQEVMVngrpR 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 407 RVMAEVG--LDPETRHRYPAE-FSGGQRQRIAIARaLILKP-ELIILDEPTSSLDrtvqAQILTLLKGLQEKHRLAYIFI 482
Cdd:PRK11147 419 HVLGYLQdfLFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLV 493
|
....*..
gi 502863011 483 SHDLQVV 489
Cdd:PRK11147 494 SHDRQFV 500
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
301-490 |
1.67e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILF-DGMPLHRWNRRQMlpvRPRMQVVFQDP--- 371
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIInDSHNLKDINLKWW---RSKIGVVSQDPllf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 372 -NSSLNP------RLSILQIIEEGLrvHQPTLTALQRENEVRRVMAEVGLD-------------PETRHRY--------- 422
Cdd:PTZ00265 473 sNSIKNNikyslySLKDLEALSNYY--NEDGNDSQENKNKRNSCRAKCAGDlndmsnttdsnelIEMRKNYqtikdsevv 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 423 --------------------------PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHR 476
Cdd:PTZ00265 551 dvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
250
....*....|....
gi 502863011 477 LAYIFISHDLQVVR 490
Cdd:PTZ00265 631 RITIIIAHRLSTIR 644
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
287-513 |
3.12e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 287 IRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ---------GEILFDGMPLHRWNRRQm 357
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCST----LLKTIASNtdgfhigveGVITYDGITPEEIKKHY- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 358 lpvrpRMQVVFQDPNSSLNPRLSILQIIEEGLRVHQPT-----LTALQRENEVRRV-MAEVGLDPETRHRYPAEF----S 427
Cdd:TIGR00956 137 -----RGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrpdgVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 428 GGQRQRIAIARALILKPELIILDEPTSSLDrtvQAQILTLLKGLQEKHRL----AYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLD---SATALEFIRALKTSANIldttPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
250
....*....|
gi 502863011 504 VVEQGECQRV 513
Cdd:TIGR00956 289 QIYFGPADKA 298
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-246 |
3.75e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.19 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQGetRTVVSDLSLQIQRGETLALVGESGSGKSVSaLSILHLLpSPPVSypqGDILFHGSSLlhadE 83
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTGL-LPPTS---GTVLVGGKDI----E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRgNKIAMIFQEPMVsLNPLHTLEKQLYevLSLHRGMRKEAARGEILDCLDRTGIRNaaKRlSDFPHQLSGGERQ 163
Cdd:TIGR01257 996 TNLDAVR-QSLGMCPQHNIL-FHHLTVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTGLHH--KR-NEEAQDLSGGMQR 1068
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAA 243
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLF 1146
|
...
gi 502863011 244 LLN 246
Cdd:TIGR01257 1147 LKN 1149
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-233 |
3.83e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGETRTVvsdlSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSYPQGDILFHgssLLHAD 82
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAV----DLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGR---TVQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRGVRGNK--IAMIFQEPMVsLNPLHTLEKQLYEVLSLHRGMR------KEAARGEILDCLDRTGirnaakrLSDFP 154
Cdd:PRK09984 75 GRLARDIRKSRanTGYIFQQFNL-VNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVG-------MVHFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVM 230
Cdd:PRK09984 147 HQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
...
gi 502863011 231 QNG 233
Cdd:PRK09984 227 RQG 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-201 |
5.45e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLsiAFSKqGEtRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpSPPVSypqGDILFHGSSLLHADEQ 84
Cdd:PRK13538 1 MLEARNL--ACER-DE-RILFSGLSFTLNAGELVQIEGPNGAGKT-SLLRILAGL-ARPDA---GEVLWQGEPIRRQRDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRgvrgnkiAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRKEAargeILDCLDRTGIRnaakRLSDFP-HQLSGGERQ 163
Cdd:PRK13538 72 YHQ-------DLLYLGHQPGIKTELTALENLRFYQRLHGPGDDEA----LWEALAQVGLA----GFEDVPvRQLSAGQQR 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 502863011 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRE 201
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-234 |
6.38e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 23 TVVS-DLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppvsypqGDI----LFHGSSLLHADEQTLRGVrgnkiAMI 97
Cdd:PRK11000 16 VVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL----------EDItsgdLFIGEKRMNDVPPAERGV-----GMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 98 FQEpmvslnplhtleKQLYEVLSLHRGMR-----KEAARGEILDCLDRTG-IRNAAKRLSDFPHQLSGGERQRVMIAMAL 171
Cdd:PRK11000 81 FQS------------YALYPHLSVAENMSfglklAGAKKEEINQRVNQVAeVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 172 LTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-230 |
6.64e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 21 TRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPPVSyPQGDILfhgssllhadeqtlrgvrgnkiamifqe 100
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA-GCVDVP---------------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 101 pmvslnplhtlEKQLYEVLSlhrgmrkeaargeILDCLDRTGIRNAAKR------LSDF------PHQLSGGERQRVMIA 168
Cdd:COG2401 93 -----------DNQFGREAS-------------LIDAIGRKGDFKDAVEllnavgLSDAvlwlrrFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 169 MALLTRPELLIADEPTTALDVTVqAQILQL-LRELRSELNMSLLFITHNLSIVKKLADSVAVM 230
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-236 |
9.34e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.80 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 10 NLSIAFSKQGETR-TVVSDLSLQIQRGETLALVGESGSGKS--VSALSILhLLPSppvsypQGDILFhgsslLHADEQTl 86
Cdd:PRK13651 7 NIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPD------TGTIEW-----IFKDEKN- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 87 rgvrgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-----------------------------GMRKEAARGEILDC 137
Cdd:PRK13651 74 -----KKKTKEKEKVLEKLVIQKTRFKKIKKIKEIRRrvgvvfqfaeyqlfeqtiekdiifgpvsmGVSKEEAKKRAAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 138 LDRTGIrnAAKRLSDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNL 217
Cdd:PRK13651 149 IELVGL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDL 225
|
250
....*....|....*....
gi 502863011 218 SIVKKLADSVAVMQNGRCV 236
Cdd:PRK13651 226 DNVLEWTKRTIFFKDGKII 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-238 |
1.17e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKS-----VSALSilhllpsppvSYPQGDILFhGSSLLHADEQTLRGvrgnkIAMIF 98
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKStllrmVAGLE----------RITSGEIWI-GGRVVNELEPADRD-----IAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 99 QEpmVSLNPLHTLEKQLYEVLSLhRGMRK--------EAARG-EILDCLDRTgirnaakrlsdfPHQLSGGERQRVMIAM 169
Cdd:PRK11650 83 QN--YALYPHMSVRENMAYGLKI-RGMPKaeieervaEAARIlELEPLLDRK------------PRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 170 ALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGRcVEQ 238
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQ 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
150-504 |
1.31e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 150 LSDFphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVTVqaqILQLLRELRSeLNMSLLFITHNLSIVKKLADSVAV 229
Cdd:PRK10636 147 VSDF----SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKS-YQGTLILISHDRDFLDPIVDKIIH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 230 MQ---------NGRCVEQNTAA------ALLNAPQH--PYTQRLLDSEPAGDPVPLQRDS-------------------- 272
Cdd:PRK10636 219 IEqqslfeytgNYSSFEVQRATrlaqqqAMYESQQErvAHLQSYIDRFRAKATKAKQAQSrikmlermeliapahvdnpf 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 273 -----------APLLNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS--- 338
Cdd:PRK10636 299 hfsfrapeslpNPLLKMEKVSAGY-----------GDRIILDSIKLNLVPGSRIGLLGRNGAGKST----LIKLLAGela 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 339 --QGEI-LFDGMPLHRWNRRQmlpvrprmqvvfqdpnsslnprLSILQIIEEGLRvHQPTLTALQRENEVRRVMAEVGLD 415
Cdd:PRK10636 364 pvSGEIgLAKGIKLGYFAQHQ----------------------LEFLRADESPLQ-HLARLAPQELEQKLRDYLGGFGFQ 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 416 PETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQILTLLKGlqekhrlAYIFISHDLQVVRAL 492
Cdd:PRK10636 421 GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmRQALTEALIDFEG-------ALVVVSHDRHLLRST 493
|
410
....*....|..
gi 502863011 493 CHQVIVLRQGEV 504
Cdd:PRK10636 494 TDDLYLVHDGKV 505
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-262 |
1.64e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpsppVSYPQGDILFHGSSLLHADEQTLRGVrgnkIAMIFQEPMV 103
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKS-SMLNALFRI----VELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 -------SLNPL--HTlEKQLYEVLSlhrgmrkeaaRGEILDCLDRTGIRNAAKrLSDFPHQLSGGERQRVMIAMALLTR 174
Cdd:PLN03232 1322 fsgtvrfNIDPFseHN-DADLWEALE----------RAHIKDVIDRNPFGLDAE-VSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 175 PELLIADEPTTALDVTVQAQILQLLR-ELRSelnMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAALLNAPQHPYT 253
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIReEFKS---CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
....*....
gi 502863011 254 QRLLDSEPA 262
Cdd:PLN03232 1466 RMVHSTGPA 1474
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-504 |
2.81e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 27 DLSLQIQRGETLALVGESGSGKSvSALSILHLLPSPPvsypQGDILFHGSSL-LHADEQTLRgvrgNKIAMIFQEpmvsL 105
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKS-TLLKCLFGIYQKD----SGSILFQGKEIdFKSSKEALE----NGISMVHQE----L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 106 NplHTLEKQLYEVLSL-----------HRGMRKEAARgeILDCLDrtgIR-NAAKRLSDfphqLSGGERQRVMIAMALLT 173
Cdd:PRK10982 83 N--LVLQRSVMDNMWLgryptkgmfvdQDKMYRDTKA--IFDELD---IDiDPRAKVAT----LSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 174 RPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCVEQNTAAALlNAPQ---- 249
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL-TMDKiiam 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 250 ---HPYTQRLldsePAGDPVPLQrdsaPLLNVEGLSVSfpirkgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSgKS 326
Cdd:PRK10982 230 mvgRSLTQRF----PDKENKPGE----VILEVRNLTSL-------------RQPSIRDVSFDLHKGEILGIAGLVGA-KR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 327 TTGLALLRLI--ASQGEILFDGMPLHrwNRRQMLPVRPRMQVVFQDPNSS---------LNPRLSILQIIEEGLRVhqpt 395
Cdd:PRK10982 288 TDIVETLFGIreKSAGTITLHGKKIN--NHNANEAINHGFALVTEERRSTgiyayldigFNSLISNIRNYKNKVGL---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 396 LTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKH 475
Cdd:PRK10982 362 LDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD 441
|
490 500
....*....|....*....|....*....
gi 502863011 476 RlAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK10982 442 K-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
308-457 |
3.47e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 308 SLRPGESLGLVGESGSGKSTtglaLLRLIASQGeilFDGMPlhrwNRRQMLPVRprmQVVFQDPNSSL----NPRLSILQ 383
Cdd:PLN03073 199 TLAFGRHYGLVGRNGTGKTT----FLRYMAMHA---IDGIP----KNCQILHVE---QEVVGDDTTALqcvlNTDIERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 384 IIEEGLRVHQ-------PTLTAL---------------QRENEVRR----------------VMAEVGLDPETRHRYPAE 425
Cdd:PLN03073 265 LLEEEAQLVAqqrelefETETGKgkgankdgvdkdavsQRLEEIYKrlelidaytaearaasILAGLSFTPEMQVKATKT 344
|
170 180 190
....*....|....*....|....*....|..
gi 502863011 426 FSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
302-471 |
5.78e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-------GEILFDGMPLHRWNRRQMLPVrprmqvvfqdpnss 374
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGRktagvitGEILINGRPLDKNFQRSTGYV-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 lnprlsilqiieEGLRVHQPTLTalqreneVRRVMaevgldpetrhRYPA---EFSGGQRQRIAIARALILKPELIILDE 451
Cdd:cd03232 85 ------------EQQDVHSPNLT-------VREAL-----------RFSAllrGLSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|
gi 502863011 452 PTSSLDRTVQAQILTLLKGL 471
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKL 154
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
302-515 |
2.15e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnRRQMLPVrprmqvvfqdpNSSLN 376
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST----LSNLIAgvtmpNKGTVDIKG-------SAALIAI-----------SSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIE-EGLRVhqpTLTALQRENEVRRVM--AEVGldpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:PRK13545 98 GQLTGIENIElKGLMM---GLTKEKIKEIIPEIIefADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 454 SSLDRTVQAQILTLLKGLQEKHRLAYiFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFT 515
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-237 |
2.91e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSilhLLPSPPVSYPQGDILFHGSSLLHADEQ 84
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGvrgNKIAMIFQEPMvslnPLHTLEKQLYEVLSLH--RGMRKEAArgeiLDCLDRTGIRNAAKRLSDFPHQL----- 157
Cdd:PRK09580 74 DRAG---EGIFMAFQYPV----EIPGVSNQFFLQTALNavRSYRGQEP----LDRFDFQDLMEEKIALLKMPEDLltrsv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 158 ----SGGERQRVMI-AMALLtRPELLIADEPTTALDVTVQAQILQLLRELRSElNMSLLFITHNLSIVKKLA-DSVAVMQ 231
Cdd:PRK09580 143 nvgfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLY 220
|
....*.
gi 502863011 232 NGRCVE 237
Cdd:PRK09580 221 QGRIVK 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-232 |
3.27e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSIL----------HLLPSPPVS-------YPQGD---------------- 70
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKS-TVMSLLmrfydlkndhHIVFKNEHTndmtneqDYQGDeeqnvgmknvnefslt 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 71 ---------ILFHGSSLLHAD-----EQTLRGVRgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRgmrKEAARGEILD 136
Cdd:PTZ00265 1262 keggsgedsTVFKNSGKILLDgvdicDYNLKDLR-NLFSIVSQEPML-------FNMSIYENIKFGK---EDATREDVKR 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 137 CLDRTGIRNAAKRLSD--------FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNM 208
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADK 1410
|
250 260
....*....|....*....|....
gi 502863011 209 SLLFITHNLSIVKKlADSVAVMQN 232
Cdd:PTZ00265 1411 TIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
156-243 |
3.41e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGRC 235
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
....*...
gi 502863011 236 VEQNTAAA 243
Cdd:PRK09700 488 TQILTNRD 495
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-245 |
3.49e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpsppVSYPQGDILFHGSSLLHADEQTLRGVRGnkiaMIFQEPMV 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKS-SMLNALFRI----VELERGRILIDGCDISKFGLMDLRKVLG----IIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 -------SLNPL--HTlEKQLYEvlSLHRGMRKEAARgeildcldrtgiRNAA---KRLSDFPHQLSGGERQRVMIAMAL 171
Cdd:PLN03130 1325 fsgtvrfNLDPFneHN-DADLWE--SLERAHLKDVIR------------RNSLgldAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 172 LTRPELLIADEPTTALDVTVQAQILQLLR-ELRSelnMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAALL 245
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIReEFKS---CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
156-504 |
3.57e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDV----------TVQAQILQLLRELRSELNMSLLFITH----NLSIVK 221
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLhavlwletylLKWPKTFIVVSHAREFLNTVVTDILHlhgqKLVTYK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 222 KLADSVAVMQNGRCVEQNTAAALlNAPQHPYTQRLLDS-------------------------EPAGDP-------VPLQ 269
Cdd:PLN03073 424 GDYDTFERTREEQLKNQQKAFES-NERSRSHMQAFIDKfrynakraslvqsrikaldrlghvdAVVNDPdykfefpTPDD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 270 RDSAPLLNVEGLSVSFPirKGILrrvvdqnaVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEILFDGMPL 349
Cdd:PLN03073 503 RPGPPIISFSDASFGYP--GGPL--------LFKNLNFGIDLDSRIAMVGPNGIGKST----ILKLIS--GELQPSSGTV 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 350 HRwnrrqmlPVRPRMQVVFQDP----NSSLNPRLSILQ----IIEEGLRVHQPTLTalqrenevrrVMAEVGLDPETrhr 421
Cdd:PLN03073 567 FR-------SAKVRMAVFSQHHvdglDLSSNPLLYMMRcfpgVPEQKLRAHLGSFG----------VTGNLALQPMY--- 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 422 ypaEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAQI--LTLLKGlqekhrlAYIFISHDLQVVRALCHQVIV 498
Cdd:PLN03073 627 ---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIqgLVLFQG-------GVLMVSHDEHLISGSVDELWV 696
|
....*.
gi 502863011 499 LRQGEV 504
Cdd:PLN03073 697 VSEGKV 702
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-247 |
9.88e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQTLRgvrgNKIAMIFQEPMV 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGLNIAKIGLHDLR----FKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 -------SLNPLHTL-EKQLYEVLSLHRGMRKEAARGEILDCLDRTGIRNaakrlsdfphqLSGGERQRVMIAMALLTRP 175
Cdd:TIGR00957 1372 fsgslrmNLDPFSQYsDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN-----------LSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 176 ELLIADEPTTALDVTVQAQILQLLRELRSELnmSLLFITHNLSIVKKLAdSVAVMQNGRCVEQNTAAALLNA 247
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-233 |
1.23e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.41 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 19 GETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPpvsypQGDILFHGSSLLHADEQTLRGVRGNKIAMIF 98
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL-----EGKVHWSNKNESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 99 QEPMVsLNPlhTLE----------KQLYEVLSLHRGMRKEAargEILDCLDRTGIRNAAKrlsdfphQLSGGERQRVMIA 168
Cdd:cd03290 86 QKPWL-LNA--TVEenitfgspfnKQRYKAVTDACSLQPDI---DLLPFGDQTEIGERGI-------NLSGGQRQRICVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 169 MALLTRPELLIADEPTTALDV-----TVQAQILQLLRELRSelnmSLLFITHNLSIVKKlADSVAVMQNG 233
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
311-492 |
1.42e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 311 PGESLGLVGESGSGKSTTGLALLRLIASQGEilfdgmplhrwnrrqmlpvrprmQVVFQDPNSSLNPRLSILQIIEeglr 390
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-----------------------GVIYIDGEDILEEVLDQLLLII---- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 391 vhqptltalqrenevrrvmaevgldpetRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL----- 465
Cdd:smart00382 54 ----------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180
....*....|....*....|....*..
gi 502863011 466 TLLKGLQEKHRLAYIFISHDLQVVRAL 492
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-201 |
1.59e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAfskQGEtRTVVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpSPPVSypqGDILFHGssllhaDE 83
Cdd:PRK13539 1 MMLEGEDLACV---RGG-RVLFSGLSFTLAAGEALVLTGPNGSGKT-TLLRLIAGL-LPPAA---GTIKLDG------GD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVR------GNKIAMifqepmvslNPLHTLEkqlyEVLSLHRGMRKeAARGEILDCLDRTGIRNAAkrlsDFPHQ- 156
Cdd:PRK13539 66 IDDPDVAeachylGHRNAM---------KPALTVA----ENLEFWAAFLG-GEELDIAAALEAVGLAPLA----HLPFGy 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRE 201
Cdd:PRK13539 128 LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
284-524 |
2.55e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 284 SFPIRKGIlrRVVdqnavLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRW-NRRQMLPV 360
Cdd:PRK10636 6 SLQIRRGV--RVL-----LDNATATINPGQKVGLVGKNGCGKSTL-LALLKneISADGGSYTFPGNWQLAWvNQETPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 361 RPRMQVVFQDPNS--SLNPRLSILQIIEEG-----LRVHQPTLTALQRENEVRRVMAEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:PRK10636 78 QPALEYVIDGDREyrQLEAQLHDANERNDGhaiatIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 434 IAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGEVVEqgecqrv 513
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSLFE------- 226
|
250
....*....|.
gi 502863011 514 FTAPTQSYTRQ 524
Cdd:PRK10636 227 YTGNYSSFEVQ 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
301-491 |
2.91e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPLHRwNRRQMlpvrpRMQVVFQDPNSSL 375
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTT----LLKLIAgllnpEKGEILFERQSIKK-DLCTY-----QKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRLSILqiiEEGLRVHQPTLTALQRENEVRRVMAEVGLDpetrhrYPAEF-SGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK13540 86 NPYLTLR---ENCLYDIHFSPGAVGITELCRLFSLEHLID------YPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502863011 455 SLDrtvQAQILTLLKGLQEkHRL---AYIFISH-DLQVVRA 491
Cdd:PRK13540 157 ALD---ELSLLTIITKIQE-HRAkggAVLLTSHqDLPLNKA 193
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
292-521 |
2.96e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 292 LRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEILFDGmplhrwnrRQMLPVRPRMQ--- 365
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgreDYEVTGGTVEFKG--------KDLLELSPEDRage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 366 ---VVFQDPNSSlnPRLS---ILQIIEEGLRV--HQPTLTALQRENEVRRVMAEVGLDPETRHRYPAE-FSGGQRQRIAI 436
Cdd:PRK09580 79 gifMAFQYPVEI--PGVSnqfFLQTALNAVRSyrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 437 ARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQ-VIVLRQGEVVEQGECQRVFT 515
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKPDyVHVLYQGRIVKSGDFTLVKQ 235
|
....*.
gi 502863011 516 APTQSY 521
Cdd:PRK09580 236 LEEQGY 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
302-490 |
3.38e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.48 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTTglaLLRLIASQGEILFDGMplhrwnrrqmLPVRPRMQVVFQDpnsslnprlsi 381
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---VNEGLYASGKARLISF----------LPKFSRNKLIFID----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 382 lqiieeglrvhqptltALQRenevrrvMAEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPE--LIILDEPTSSLDRT 459
Cdd:cd03238 67 ----------------QLQF-------LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|..
gi 502863011 460 VQAQILTLLKGL-QEKHRLayIFISHDLQVVR 490
Cdd:cd03238 124 DINQLLEVIKGLiDLGNTV--ILIEHNLDVLS 153
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
299-503 |
4.21e-08 |
|
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: 54.86 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 299 NAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILFDGmplhrwnrrqmlpvrprmQVVFQDPNSSLNP 377
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSG------------------RISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 378 RlSILQIIEEGLRV----HQPTLTALQRENEVRR-------VMAEVGLDpetrhrypaeFSGGQRQRIAIARALILKPEL 446
Cdd:cd03291 112 G-TIKENIIFGVSYdeyrYKSVVKACQLEEDITKfpekdntVLGEGGIT----------LSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 447 IILDEPTSSLDRTVQAQIL--TLLKGLQEKHRlayIFISHDLQVVRAlCHQVIVLRQGE 503
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFesCVCKLMANKTR---ILVTSKMEHLKK-ADKILILHEGS 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
300-487 |
4.85e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.87 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 300 AVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEILFDGMPLHRWNRRQMLPVRPRMQVVFqdpnSSLNPRL 379
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAY----AAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 380 sILQIIEEGLRVHQPTltALQRENEVR---RVMAEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPELIILDEP 452
Cdd:cd03290 91 -LNATVEENITFGSPF--NKQRYKAVTdacSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 502863011 453 TSSLDRTVQAQILT--LLKGLQEKHRlAYIFISHDLQ 487
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQ 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-221 |
6.84e-08 |
|
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: 55.14 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSvSALSILHLLpsppvsYPqgdiLFHGssllhadeqTLRGVRGNKIAMIFQEPMV 103
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKS-SLFRILGEL------WP----VYGG---------RLTKPAKGKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 104 SLNplhTLEKQ-LYEVLSLH---RGMRkEAARGEILDCLDRTGI--RNAA-KRLSDFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:TIGR00954 527 TLG---TLRDQiIYPDSSEDmkrRGLS-DKDLEQILDNVQLTHIleREGGwSAVQDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502863011 177 LLIADEPTTALDVTVQAQILQLLRelrsELNMSLLFITHNLSIVK 221
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSLWK 643
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
307-484 |
8.79e-08 |
|
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: 54.75 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIasqGEI--LFDG-MPLHRWNRRQMLPVRPRM-------QVVFQDpnssln 376
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSS----LFRIL---GELwpVYGGrLTKPAKGKLFYVPQRPYMtlgtlrdQIIYPD------ 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 prlSILQIIEEGLR--VHQPTLTALQRENEVRRvmaEVGLDpeTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:TIGR00954 540 ---SSEDMKRRGLSdkDLEQILDNVQLTHILER---EGGWS--AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 502863011 455 SLDRTVQAQILTLLKglqeKHRLAYIFISH 484
Cdd:TIGR00954 612 AVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-253 |
1.10e-07 |
|
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: 52.99 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppVSYPQGDILFHGSSLLHADEQT 85
Cdd:cd03288 20 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM-----VDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRgvrgNKIAMIFQEPMV-------SLNPLHTL-EKQLYEVLSLH--RGMRKEAARGeiLDCLDRTGIRNaakrlsdfph 155
Cdd:cd03288 93 LR----SRLSIILQDPILfsgsirfNLDPECKCtDDRLWEALEIAqlKNMVKSLPGG--LDAVVTEGGEN---------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 qLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQaQILQLLrELRSELNMSLLFITHNLSIVKKlADSVAVMQNGRC 235
Cdd:cd03288 157 -FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGIL 232
|
250
....*....|....*...
gi 502863011 236 VEQNTAAALLNAPQHPYT 253
Cdd:cd03288 233 VECDTPENLLAQEDGVFA 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
301-477 |
1.13e-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: 54.92 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILFDGM----PLHRWnrrqMLPVRPRMQVVFQDPNSSL 375
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRisfsPQTSW----IMPGTIKDNIIFGLSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRlSILQI--IEEGLRVHqptltalqrENEVRRVMAEVGLdpetrhrypaEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:TIGR01271 517 RYT-SVIKAcqLEEDIALF---------PEKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180
....*....|....*....|....*.
gi 502863011 454 SSLDRTVQAQIL--TLLKGLQEKHRL 477
Cdd:TIGR01271 577 THLDVVTEKEIFesCLCKLMSNKTRI 602
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
427-503 |
1.30e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.22 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 427 SGGQRQ------RIAIARALILKPELIILDEPTSSLDR-TVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 502863011 500 RQGE 503
Cdd:cd03240 197 KDGR 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
309-502 |
1.35e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 309 LRPGESLGLVGESGSGKSTTGLALL-RLIASQGEILFDGMPlhrwnrrqmlpVRPRMQVVFQdpNSSLNPRLSILQIIEE 387
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTgDTTVTSGDATVAGKS-----------ILTNISDVHQ--NMGYCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 388 GlRVHQPTLTALQ--RENEVRRV----MAEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQ 461
Cdd:TIGR01257 2029 G-REHLYLYARLRgvPAEEIEKVanwsIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502863011 462 AQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:TIGR01257 2107 RMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-236 |
1.61e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 125 MRKEAARGEILDCLDRTGIRNAAKRLSdfpHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRS 204
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAA---AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110
....*....|....*....|....*....|..
gi 502863011 205 ElNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:NF000106 193 D-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
287-513 |
1.79e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 287 IRKGILRrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALlrliasQGE-ILFDGMPLHRWNRRQMLPVRPRMQ 365
Cdd:PRK10938 6 ISQGTFR--LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARAL------AGElPLLSGERQSQFSHITRLSFEQLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 366 VV---FQDPNSSL------NPRLSILQIIEEGlrVHQPTLTAlqrenevrRVMAEVGLDP--ETRHRYpaeFSGGQRQRI 434
Cdd:PRK10938 78 LVsdeWQRNNTDMlspgedDTGRTTAEIIQDE--VKDPARCE--------QLAQQFGITAllDRRFKY---LSTGETRKT 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 435 AIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-221 |
2.92e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.48 E-value: 2.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 157 LSGGERQRVMIAMALLTR---PELLIADEPTTAL---DVtvqAQILQLLRELRSELNmSLLFITHNLSIVK 221
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVIK 896
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-192 |
3.23e-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: 53.38 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGetRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSppvsypQGDILFHGSSLLHADEQT 85
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LR---GVRGNKIAMIFQEPMVSLNPLHTLEKQlyevlslhrgmrkeaargEILDCLDRTGIRNAAKR--------LSDFP 154
Cdd:TIGR01271 1290 WRkafGVIPQKVFIFSGTFRKNLDPYEQWSDE------------------EIWKVAEEVGLKSVIEQfpdkldfvLVDGG 1351
|
170 180 190
....*....|....*....|....*....|....*....
gi 502863011 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VTVQ 192
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-231 |
3.51e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 3.51e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQ 231
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-230 |
3.83e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 155 HQLSGGERQRVMIAMAL----LTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMsLLFITHNLsIVKKLADSVAVM 230
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLP-ELAELADKLIHI 153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
264-511 |
3.92e-07 |
|
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: 53.03 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 264 DPVPLQRDSAPllnvEGLSVSFPIRKGILRRVVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEI 342
Cdd:TIGR00957 620 EPDSIERRTIK----PGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 343 LFDG----MPLHRWNRRQMLpvrpRMQVVFQDPnssLNPRlSILQIIEEGLRVhqPTLTALQRENevRRVMAEVGLDpet 418
Cdd:TIGR00957 696 HMKGsvayVPQQAWIQNDSL----RENILFGKA---LNEK-YYQQVLEACALL--PDLEILPSGD--RTEIGEKGVN--- 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 419 rhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKG----LQEKHRlayIFISHDLQVVRALcH 494
Cdd:TIGR00957 761 -------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHGISYLPQV-D 829
|
250
....*....|....*..
gi 502863011 495 QVIVLRQGEVVEQGECQ 511
Cdd:TIGR00957 830 VIIVMSGGKISEMGSYQ 846
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
254-514 |
4.43e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 254 QRLLDSEPagdpvPLQrDSAPLLNVEGLSVSFPIRKgilrrvvdQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL 333
Cdd:PLN03232 599 ERILAQNP-----PLQ-PGAPAISIKNGYFSWDSKT--------SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 334 rliasqGEIlfDGMPLHRWNRRQMLPVRPRMQVVFqdpNSSLNPRLSILQIIEEGLRVHQPTLTALQRENEV--RRVMAE 411
Cdd:PLN03232 665 ------GEL--SHAETSSVVIRGSVAYVPQVSWIF---NATVRENILFGSDFESERYWRAIDVTALQHDLDLlpGRDLTE 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 412 VGldpetrhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILT--LLKGLQEKHRlayIFISHDLQVV 489
Cdd:PLN03232 734 IG-------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTR---VLVTNQLHFL 803
|
250 260
....*....|....*....|....*
gi 502863011 490 rALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PLN03232 804 -PLMDRIILVSEGMIKEEGTFAELS 827
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
308-509 |
4.70e-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: 51.25 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 308 SLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGMPlhrwnrrqmlpVRPRMQVVFQDPNSSLNPRL-SI 381
Cdd:cd03237 21 SISESEVIGILGPNGIGKTT----FIKMLAgvlkpDEGDIEIELDT-----------VSYKPQYIKADYEGTVRDLLsSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 382 LQIIeeglrvhqptLTALQRENEVrrvMAEVGLDPETRHRYPaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQ 461
Cdd:cd03237 86 TKDF----------YTHPYFKTEI---AKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502863011 462 AQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLrQGEVVEQGE 509
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
305-370 |
5.51e-07 |
|
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: 52.11 E-value: 5.51e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 305 IRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEILFDGMPLHRWNR---RQMlpvrprMQVVFQD 370
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKST----LAKLLtglyrPESGEILLDGQPVTADNReayRQL------FSAVFSD 414
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
302-513 |
7.46e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDGmplhrwnrrqmlpvrprmQVVFQDPNSSLN 376
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKST----LSNIIGgslspTVGKVDRNG------------------EVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 377 PRLSILQIIEEGLrvhqptLTALQRENEVRRVM------AEVGldpETRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:PRK13546 98 GQLTGIENIEFKM------LCMGFKRKEIKAMTpkiiefSELG---EFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 451 EPTSSLDRTVQAQILTLLKGLQEKHRLAYiFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQNKTIF-FVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
310-488 |
9.38e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 310 RPGESLGLVGESGSGKSTTglalLRLIASQ--------------GEIL--FDGMPLHRWNRR----QMLPVRpRMQVVFQ 369
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTA----LKILAGKlkpnlgkfddppdwDEILdeFRGSELQNYFTKllegDVKVIV-KPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSSLNPRLSILQIIEEglrvhqptltalqrENEVRRVMAEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03236 99 IPKAVKGKVGELLKKKDE--------------RGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 502863011 450 DEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQV 488
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAV 201
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
417-515 |
1.04e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 417 ETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIFISHDLQVVRALCHQV 496
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHEL 214
|
90
....*....|....*....
gi 502863011 497 IVLRQGEVVEQGECQRVFT 515
Cdd:NF000106 215 TVIDRGRVIADGKVDELKT 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
157-247 |
1.09e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVKKLADSVAVMQNGRCV 236
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
90
....*....|....*.
gi 502863011 237 -----EQNTAAALLNA 247
Cdd:PRK11288 476 gelarEQATERQALSL 491
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
157-229 |
1.34e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAV 229
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
219-471 |
1.36e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 219 IVKKLADSVAVMQNGRCVEQNTAAALLNAPQHPYTQRLLDSEPAGDPVPLQRDSA-PLLNVEGLSVSFPIRKGILRrvvd 297
Cdd:TIGR00956 702 ILVFRRGSLKRAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESGeDIFHWRNLTYEVKIKKEKRV---- 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 298 qnaVLKNIRFSLRPGESLGLVGESGSGKsTTGLALL--RL---IASQGEILFDGMPLHRWNRRQMLPVRPrmqvvfQDPN 372
Cdd:TIGR00956 778 ---ILNNVDGWVKPGTLTALMGASGAGK-TTLLNVLaeRVttgVITGGDRLVNGRPLDSSFQRSIGYVQQ------QDLH 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 373 SslnPRLSILQIIEEGLRVHQPTLTALQRENE-VRRVM----------AEVGLdpetrhryPAE-FSGGQRQRIAIARAL 440
Cdd:TIGR00956 848 L---PTSTVRESLRFSAYLRQPKSVSKSEKMEyVEEVIkllemesyadAVVGV--------PGEgLNVEQRKRLTIGVEL 916
|
250 260 270
....*....|....*....|....*....|..
gi 502863011 441 ILKPELII-LDEPTSSLDRTVQAQILTLLKGL 471
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-225 |
1.38e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 1.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 157 LSGGERQRVMIA--MALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNmSLLFITHNLSIVkKLAD 225
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVL-SSAD 156
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-215 |
1.81e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKqgetRTVVSDLSLQIQRGETLALVGESGSGKSvSALSIL---HllpspPVSYPQGDILF------ 73
Cdd:PRK10938 258 EPRIVLNNGVVSYND----RPILHNLSWQVNPGEHWQIVGPNGAGKS-TLLSLItgdH-----PQGYSNDLTLFgrrrgs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 74 ------------HGSSLLHADEQTLRGVRGNKIAMIFQepmvSLNplhtlekqLYEVLSlhrgmrkEAARGEILDCLDRT 141
Cdd:PRK10938 328 getiwdikkhigYVSSSLHLDYRVSTSVRNVILSGFFD----SIG--------IYQAVS-------DRQQKLAQQWLDIL 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 142 GIrnaAKRLSDFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITH 215
Cdd:PRK10938 389 GI---DKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
157-221 |
2.03e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.15 E-value: 2.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 157 LSGGERQRVMIAMALL---TRPELLIADEPTTALDVTVQAQILQLLRELRSELNmSLLFITHNLSIVK 221
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-275 |
2.17e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSIL-HLLPSppvsypQGDILFHGssllhadeqtlrgvrgnKIAMIFQEP- 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPS------EGKIKHSG-----------------RISFSPQTSw 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 102 ----MVSLNPLHTLEKQLYEVLSLHRGMRKEAargeildclDRTGIRNAAKR-LSDFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:TIGR01271 498 impgTIKDNIIFGLSYDEYRYTSVIKACQLEE---------DIALFPEKDKTvLGEGGITLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 177 LLIADEPTTALDVTVQAQILQ-LLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRCVEQNTAAAlLNAPQHPYTQR 255
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFEsCLCKLMS--NKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSE-LQAKRPDFSSL 644
|
250 260
....*....|....*....|
gi 502863011 256 LLDSEpAGDPVPLQRDSAPL 275
Cdd:TIGR01271 645 LLGLE-AFDNFSAERRNSIL 663
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-236 |
2.81e-06 |
|
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: 50.40 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 5 LLSIDNLSIAFSkqGETRTVVSDLSLQIQRGETLALVGESGSGKSVSalsiLHLLpSPPVSYPQGDILFHGSSLLhadeQ 84
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKML-TGDTTVTSGDATVAGKSIL----T 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 85 TLRGVRGNkiaMIFQEPMVSLNPLHTLEKQLYEVLSLhRGMRKEAARGEILDCLDRTGIRNAAKRLSDfphQLSGGERQR 164
Cdd:TIGR01257 2006 NISDVHQN---MGYCPQFDAIDDLLTGREHLYLYARL-RGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRK 2078
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 165 VMIAMALLTRPELLIADEPTTALDVTVQAQ----ILQLLRELRselnmSLLFITHNLSIVKKLADSVAVMQNG--RCV 236
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGafQCL 2151
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
427-508 |
3.09e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL-TLLKG-LQEKHRLAYIFISHDLQVVralcHQVIVLRQGEV 504
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDeLRGKTRVLVTNQLHFLSQV----DRIILVHEGMI 817
|
....
gi 502863011 505 VEQG 508
Cdd:PLN03130 818 KEEG 821
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-295 |
3.09e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 28 LSLQIQRGETLALVGESGSGKSvSALSILhLLPSPPVsypQGDILFHGSSLLHADEQTLRG--VRGNkiaMIFQEPmvsL 105
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKS-SLLSAL-LAEMDKV---EGHVHMKGSVAYVPQQAWIQNdsLREN---ILFGKA---L 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 106 NPLHTleKQLYEVLSLHRGMrkeaargEILDCLDRTGIRNAAKrlsdfphQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:TIGR00957 726 NEKYY--QQVLEACALLPDL-------EILPSGDRTEIGEKGV-------NLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 186 ALDVTVQAQILQLLRELRSEL-NMSLLFITHNLSIVKKLaDSVAVMQNGRCVEQNTAAALLNAP--------QHPYTQRL 256
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDgafaeflrTYAPDEQQ 868
|
250 260 270
....*....|....*....|....*....|....*....
gi 502863011 257 LDSEPAGDPVPLQRDSAPLLNVEGLSVSFPIRKGILRRV 295
Cdd:TIGR00957 869 GHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQL 907
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-241 |
4.33e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFsKQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSIlhllpsppvsypQGDIlfHGSSLLHAD 82
Cdd:TIGR00956 56 KILTRGFRKLKKF-RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTI------------ASNT--DGFHIGVEG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRGVRGNKIAMIFQEPMV--SLNPLHTLEKQLYEVLSLHRGMRKEAARGEILDCLDR----TGIRNAAKRLS----- 151
Cdd:TIGR00956 121 VITYDGITPEEIKKHYRGDVVynAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYakhiADVYMATYGLShtrnt 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 152 ----DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSI-VKKLADS 226
Cdd:TIGR00956 201 kvgnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDK 280
|
250
....*....|....*
gi 502863011 227 VAVMQNGRCVEQNTA 241
Cdd:TIGR00956 281 VIVLYEGYQIYFGPA 295
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-263 |
5.20e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 3 QPLLSIDNLSIAFSKQGEtRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPSPP---------VSY-PQGDIL 72
Cdd:PLN03130 612 LPAISIKNGYFSWDSKAE-RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirgtVAYvPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 73 FHGSsllhadeqtlrgVRGNkiaMIFQEPmvslnplhtLEKQLYE----VLSLHRGMrkeaargEILDCLDRTGI--RNA 146
Cdd:PLN03130 691 FNAT------------VRDN---ILFGSP---------FDPERYEraidVTALQHDL-------DLLPGGDLTEIgeRGV 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 147 akrlsdfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQ--LLRELRSELNMSLLFITHNLSIVkkla 224
Cdd:PLN03130 740 ---------NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTRVLVTNQLHFLSQV---- 806
|
250 260 270
....*....|....*....|....*....|....*....
gi 502863011 225 DSVAVMQNGRCVEQNTAAALLNapQHPYTQRLLdsEPAG 263
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSN--NGPLFQKLM--ENAG 841
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-225 |
8.24e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.87 E-value: 8.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVtvqAQILQLLRELRSELNmSLLFITHNLSIVkKLAD 225
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVI-KTAD 896
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
150-227 |
9.80e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 150 LSDFPHQLSGGERQ------RVMIAMALLTRPELLIADEPTTALDV-TVQAQILQLLRELRSELNMSLLFITHNLSiVKK 222
Cdd:cd03240 109 LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEE-LVD 187
|
....*
gi 502863011 223 LADSV 227
Cdd:cd03240 188 AADHI 192
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-227 |
1.01e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863011 157 LSGGERQRVMIAMALLT---RPELLIADEPTTALDVTVQAQILQLLRELrSELNMSLLFITHNLSIVkKLADSV 227
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVV-KVADYV 881
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-501 |
1.10e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.81 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863011 427 SGGQRQRIAIARALIL---KPE-LIILDEPTSSLDRTVQAQILTLLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
302-457 |
1.16e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.20 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEI-LFDG-MPLHRWNRRqmlpVRPRMQVVFQDPNSS 374
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAgarkiQQGRVeVLGGdMADARHRRA----VCPRIAYMPQGLGKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 375 LNPRLSIlqiiEEGLRVHQpTL---TALQRENEVRRVMAEVGLDPeTRHRyPA-EFSGGQRQRIAIARALILKPELIILD 450
Cdd:NF033858 89 LYPTLSV----FENLDFFG-RLfgqDAAERRRRIDELLRATGLAP-FADR-PAgKLSGGMKQKLGLCCALIHDPDLLILD 161
|
....*..
gi 502863011 451 EPTSSLD 457
Cdd:NF033858 162 EPTTGVD 168
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-265 |
1.45e-05 |
|
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: 42.77 E-value: 1.45e-05
10 20 30
....*....|....*....|....*....|
gi 502863011 236 VEQNTAAALLNAPQHPYTQRLLDSEPAGDP 265
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-244 |
1.64e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFSKQGETRTVvSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPsppvsypqgdilfhgssllHAdE 83
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSKPTL-SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-------------------HA-E 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 84 QTLRGVRGNkIAMIFQEPMVsLNPlhTLEKQL-----YEVLSLHRGMRKEAARGEiLDCL---DRTGIRNAAKrlsdfph 155
Cdd:PLN03232 672 TSSVVIRGS-VAYVPQVSWI-FNA--TVRENIlfgsdFESERYWRAIDVTALQHD-LDLLpgrDLTEIGERGV------- 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQ--LLRELRSElnmSLLFITHNLSIVkKLADSVAVMQNG 233
Cdd:PLN03232 740 NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGK---TRVLVTNQLHFL-PLMDRIILVSEG 815
|
250
....*....|.
gi 502863011 234 RCVEQNTAAAL 244
Cdd:PLN03232 816 MIKEEGTFAEL 826
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
157-229 |
1.66e-05 |
|
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: 46.25 E-value: 1.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQLLRELRSELNMSLLFITHNLSIVKKLADSVAV 229
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-224 |
1.81e-05 |
|
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: 44.67 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 34 RGETLALVGESGSGKSVSALSILHLLPSPpvsypqgdilfhgssllhadeqtlrgvrgnkiamifQEPMVSLNPLHTLEK 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP------------------------------------GGGVIYIDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 114 QLYEVLSLHRGMRKeaargeildcldrtgirnaakrlsdfpHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQA 193
Cdd:smart00382 45 VLDQLLLIIVGGKK---------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190
....*....|....*....|....*....|....*.
gi 502863011 194 QILQLLR-----ELRSELNMSLLFITHNLSIVKKLA 224
Cdd:smart00382 98 LLLLLEElrlllLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
157-221 |
1.85e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 1.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 157 LSGGERQRVMIAMALLTRP---ELLIADEPTTAL---DVtvqAQILQLLRELRSELNmSLLFITHNLSIVK 221
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVIK 897
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-192 |
2.49e-05 |
|
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: 46.00 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFSKQGETrtVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLpsppvsYPQGDILFHGSSLLHADEQT 85
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LR---GVRGNKIaMIFQEPM-VSLNPLHTLEKQlyevlslhrgmrkeaargEILDCLDRTGIRNAakrLSDFPHQ----- 156
Cdd:cd03289 75 WRkafGVIPQKV-FIFSGTFrKNLDPYGKWSDE------------------EIWKVAEEVGLKSV---IEQFPGQldfvl 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502863011 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALD-VTVQ 192
Cdd:cd03289 133 vdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
297-485 |
2.68e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEILFDGMPLHRWNRRQMlpvRPRMQVVFQD----- 370
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTAEQPEDY---RKLFSAVFTDfhlfd 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 371 ---------PNSSL-NPRLSILQiIEEGLRVHQPTLTALQrenevrrvmaevgldpetrhrypaeFSGGQRQRIAIARAL 440
Cdd:PRK10522 411 qllgpegkpANPALvEKWLERLK-MAHKLELEDGRISNLK-------------------------LSKGQKKRLALLLAL 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502863011 441 ILKPELIILDEPTSSLD---RTVQAQIltLLKGLQEKHRLayIF-ISHD 485
Cdd:PRK10522 465 AEERDILLLDEWAADQDphfRREFYQV--LLPLLQEMGKT--IFaISHD 509
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
302-508 |
2.71e-05 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 302 LKNIRFSLRPGESLGLVGESGSGKSTtgLAlLRLIASQGEilfdgmplHRWNR------RQMLPVRPRMQVvfqDPNSSL 375
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSS--LA-FDTIYAEGQ--------RRYVEslsayaRQFLGQMDKPDV---DSIEGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 376 NPRLSILQ-IIEEGLRVHQPTLTAL--------QRENEVRRV--MAEVGLDPETRHRYPAEFSGGQRQRIAIARAL--IL 442
Cdd:cd03270 77 SPAIAIDQkTTSRNPRSTVGTVTEIydylrllfARVGIRERLgfLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502863011 443 KPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVRALCHQVIV-----LRQGEVVEQG 508
Cdd:cd03270 157 TGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
157-188 |
3.19e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.19e-05
10 20 30
....*....|....*....|....*....|..
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALD 188
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-234 |
3.46e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 4 PLLSIDNLSIAFskqGEtRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpSPPVSYPQGDI-LFHGSSLLHAD 82
Cdd:PRK10636 311 PLLKMEKVSAGY---GD-RIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLL-AGELAPVSGEIgLAKGIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 83 EQTLRGVRGNKIAMifqEPMVSLNPlHTLEKQLYEVLSlhrgmrkeaargeildcldrtGIRNAAKRLSDFPHQLSGGER 162
Cdd:PRK10636 382 QHQLEFLRADESPL---QHLARLAP-QELEQKLRDYLG---------------------GFGFQGDKVTEETRRFSGGEK 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863011 163 QRVMIAMALLTRPELLIADEPTTALDVTVQaqilQLLRELRSELNMSLLFITHNLSIVKKLADSVAVMQNGR 234
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMR----QALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-237 |
4.17e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 17 KQGETRTVVSDLSLQIQRGETLALVGESGSGKSVSALSILHLLPspPVSypqGDILFHGSSLLHADEQTLRGvrgnkiam 96
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS--PTV---GKVDRNGEVSVIAISAGLSG-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 97 ifqepmvslnPLHTLEKQLYEVLSLhrGM-RKE--AARGEILDcldrtgirnaAKRLSDFPHQ----LSGGERQRVMIAM 169
Cdd:PRK13546 99 ----------QLTGIENIEFKMLCM--GFkRKEikAMTPKIIE----------FSELGEFIYQpvkkYSSGMRAKLGFSI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 170 ALLTRPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKKLADSVAVMQNGRCVE 237
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
425-499 |
4.36e-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: 44.10 E-value: 4.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
272-457 |
5.76e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 272 SAPLLNVEGLSVSfpirkgilrrvVDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEILFDG 346
Cdd:PRK13543 8 APPLLAAHALAFS-----------RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTT----LLRVLAgllhvESGQIQIDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 347 MPLHRWNRRQMLPVRPRMqvvfqdpnSSLNPRLSILQIIE-----EGLRVHQPTLTALqrenevrrvmAEVGL----DPE 417
Cdd:PRK13543 73 KTATRGDRSRFMAYLGHL--------PGLKADLSTLENLHflcglHGRRAKQMPGSAL----------AIVGLagyeDTL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502863011 418 TRHrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK13543 135 VRQ-----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
301-509 |
5.82e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQGEILFDGMplhrWNRRQMLPVRPRMQVVfqdpNSSLnpRLS 380
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKST----LLQSLLSQFEISEGRV----WAERSIAYVPQQAWIM----NATV--RGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 381 ILQIIEEGLRVHQPTLTALQRENEVRRVMAevGLDPETRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD--- 457
Cdd:PTZ00243 741 ILFFDEEDAARLADAVRVSQLEADLAQLGG--GLETEIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDahv 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502863011 458 --RTVQAQILTLLKGlqeKHRlayIFISHDLQVVrALCHQVIVLRQGEVVEQGE 509
Cdd:PTZ00243 818 geRVVEECFLGALAG---KTR---VLATHQVHVV-PRADYVVALGDGRVEFSGS 864
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-235 |
7.56e-05 |
|
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: 44.85 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSIL-HLLPSPPVSYPQGDILFhgssllhadeqtlrgvrGNKIAMIFqEPM 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISF-----------------SSQFSWIM-PGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 103 VSLNPLHTLEKQLYEVLSLHRGMRKEaargeildcldrtgirnaaKRLSDFPHQ-----------LSGGERQRVMIAMAL 171
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVVKACQLE-------------------EDITKFPEKdntvlgeggitLSGGQRARISLARAV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502863011 172 LTRPELLIADEPTTALDVTVQAQILQ-LLRELRSelNMSLLFITHNLSIVKKlADSVAVMQNGRC 235
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSS 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
425-499 |
9.99e-05 |
|
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: 45.16 E-value: 9.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQiltLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVL 499
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVAR---LIRELAEEGK-YVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-499 |
1.55e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALltRPELL----IADEPTTALDVTVQAQILQLLRELRSELNmSLLFITHNLSIVKkLADSV----- 227
Cdd:PRK00635 477 LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMIS-LADRIidigp 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 228 -AVMQNGRCVEQNTAAALLNApQHPYTQRLLDSEPAgDPVPLQRDSAPllnvEGLSVSfpirkgilrRVVDQNavLKNIR 306
Cdd:PRK00635 553 gAGIFGGEVLFNGSPREFLAK-SDSLTAKYLRQELT-IPIPEKRTNSL----GTLTLS---------KATKHN--LKDLT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 307 FSLRPGESLGLVGESGSGKS-----TTGLALLRLIASQGE--ILFDGMPLHRW---NR---------------------R 355
Cdd:PRK00635 616 ISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFCsnLSIQWGAISRLvhiTRdlpgrsqrsipltyikafddlR 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 356 QMLPVRPRMQVV--------FQDPNSS------------LNPRLSILQIIEEGLRVHQPTL---------------TALQ 400
Cdd:PRK00635 696 ELFAEQPRSKRLgltkshfsFNTPLGAcaecqglgsittTDNRTSIPCPSCLGKRFLPQVLevrykgkniadilemTAYE 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 401 REN---------EVRRVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALIL---KPELIILDEPTSSL-DRTVQAQILTL 467
Cdd:PRK00635 776 AEKffldepsihEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhTHDIKALIYVL 855
|
410 420 430
....*....|....*....|....*....|..
gi 502863011 468 LKGLQEKHRLayIFISHDLQVVRaLCHQVIVL 499
Cdd:PRK00635 856 QSLTHQGHTV--VIIEHNMHVVK-VADYVLEL 884
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-508 |
1.57e-04 |
|
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: 44.62 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 316 GLVGESGSGKSTTgLALLR--LIASQGEILFDGMPLHRW--NRRQMLPVRPRMQVVFQDpnsslnprlsiLQIIEEGLRV 391
Cdd:TIGR01257 960 AFLGHNGAGKTTT-LSILTglLPPTSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHH-----------LTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 392 HQPTLTALQREN-EVRRVMAEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILTLLkg 470
Cdd:TIGR01257 1028 AQLKGRSWEEAQlEMEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-- 1104
|
170 180 190
....*....|....*....|....*....|....*...
gi 502863011 471 LQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
276-505 |
1.75e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 276 LNVEGLSVSFpirkgilrrvvDQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEIlfdgmplh 350
Cdd:PRK15064 320 LEVENLTKGF-----------DNGPLFKNLNLLLEAGERLAIIGENGVGKTT----LLRTLVGelepdSGTV-------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 351 RWNRRQMLPVRPrmqvvfQDPNSSLNPRLSIL----QIIEEGlrvhqptltalQRENEVRRVMAEVGLDPETRHRYPAEF 426
Cdd:PRK15064 377 KWSENANIGYYA------QDHAYDFENDLTLFdwmsQWRQEG-----------DDEQAVRGTLGRLLFSQDDIKKSVKVL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 427 SGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAQILTLlkglqEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDmESIESLNMAL-----EKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
425-499 |
2.33e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502863011 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQiltLLKGLQEKHrlAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqRLNVAR---LIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-224 |
2.37e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 6 LSIDNLSIAFskqgETRTVVSDLSLQIQRGETLALVGESGSGKSvsalSILHLLpsppvsypQGDilfhgsslLHADEQT 85
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKT----TLLRTL--------VGE--------LEPDSGT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 86 LRGVRGNKIAMIFQEPmvslnplhtlEKQLYEVLSLHRGMRKEAARGEildclDRTGIRNAAKRL----SDFPHQ---LS 158
Cdd:PRK15064 376 VKWSENANIGYYAQDH----------AYDFENDLTLFDWMSQWRQEGD-----DEQAVRGTLGRLlfsqDDIKKSvkvLS 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863011 159 GGERQRVMIAMALLTRPELLIADEPTTALDVtvqaqilqllrELRSELNM-------SLLFITHNLSIVKKLA 224
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM-----------ESIESLNMalekyegTLIFVSHDREFVSSLA 502
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
156-193 |
5.83e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 5.83e-04
10 20 30
....*....|....*....|....*....|....*....
gi 502863011 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDV-TVQA 193
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVeTLRA 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
407-508 |
7.01e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 407 RVMAEVGLDPETRHRYPAEFSGGQRQRIAIARALiLKPE----LIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAyIFI 482
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTV-VVI 228
|
90 100 110
....*....|....*....|....*....|..
gi 502863011 483 SHDLQVVRAlCHQVIVL------RQGEVVEQG 508
Cdd:cd03271 229 EHNLDVIKC-ADWIIDLgpeggdGGGQVVASG 259
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
297-457 |
8.87e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 297 DQNAVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEILFDGMPlhrwnRRQMLPVRPRMQVVFQ 369
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTT----LMDVLAGrktggyiEGDIRISGFP-----KKQETFARISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 370 DPNSslnPRLSILQ--IIEEGLRVHQpTLTALQRENEVRRVM----------AEVGLDPETrhrypaEFSGGQRQRIAIA 437
Cdd:PLN03140 962 DIHS---PQVTVREslIYSAFLRLPK-EVSKEEKMMFVDEVMelveldnlkdAIVGLPGVT------GLSTEQRKRLTIA 1031
|
170 180
....*....|....*....|
gi 502863011 438 RALILKPELIILDEPTSSLD 457
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLD 1051
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
157-248 |
1.31e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILQ--LLRELRSElnmSLLFITHNLSIVkKLADSVAVMQNGR 234
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGK---TRVLATHQVHVV-PRADYVVALGDGR 858
|
90
....*....|....
gi 502863011 235 CVEQNTAAALLNAP 248
Cdd:PTZ00243 859 VEFSGSSADFMRTS 872
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-249 |
1.52e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 24 VVSDLSLQIQRGETLALVGESGSGKSVSALSILHLlpsppVSYPQGDILFHGSSLlhaDEQTLRGVRgNKIAMIFQEPM- 102
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-----VEVCGGEIRVNGREI---GAYGLRELR-RQFSMIPQDPVl 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 103 ----VSLNPLHTLEKQLYEV---LSLhRGMRKE-AARGEILDCLDRTGIRNaakrlsdfphqLSGGERQRVMIAMALLTR 174
Cdd:PTZ00243 1396 fdgtVRQNVDPFLEASSAEVwaaLEL-VGLRERvASESEGIDSRVLEGGSN-----------YSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502863011 175 PELLI-ADEPTTALDVTVQAQILQLLRELRSelNMSLLFITHNLSIVKKLaDSVAVMQNGRCVEQNTAAALLNAPQ 249
Cdd:PTZ00243 1464 GSGFIlMDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
157-202 |
1.62e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 1.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 502863011 157 LSGGERQRVMIAMALLTRPELLI-ADEPTTALDVTVQAQILQLLREL 202
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-280 |
2.24e-03 |
|
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: 37.34 E-value: 2.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 502863011 236 VEQNTAAALLNAPQHPYTQRLLDSEpagdPVPLQRDSaPLLNVEG 280
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAI----PTIKKRDR-KLISIPG 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
427-508 |
2.35e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 427 SGGQRQRIAIARALILK---PELIILDEPTSSLDRTVQAQILTLLKGLQEKHRLAyIFISHDLQVVRALCHqVIVL---- 499
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVIEHNLDVIKTADY-IIDLgpeg 908
|
90
....*....|.
gi 502863011 500 --RQGEVVEQG 508
Cdd:TIGR00630 909 gdGGGTVVASG 919
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
411-525 |
4.81e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 411 EVGLdPETRHRYP-AEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqaqILTL--LKGLQEKHRLAYIFISHDLQ 487
Cdd:PRK15064 141 GVGI-PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD------INTIrwLEDVLNERNSTMIIISHDRH 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 502863011 488 VVRALCHQVIVLRQGEVveqgecqRVF--------TAPTQSYTRQL 525
Cdd:PRK15064 214 FLNSVCTHMADLDYGEL-------RVYpgnydeymTAATQARERLL 252
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-327 |
5.77e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 157 LSGGERQRVMIAMAL---LTrPELLIADEPTTALDVTVQAQILQLLRELRsELNMSLLFITHNLSIVKkLADSV------ 227
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgLT-GVLYVLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVEHDEDTIR-AADYVidigpg 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 228 AVMQNGRCVEQNTAAALLNAPQHPYTQRLldSEPAGDPVPLQRdsaplLNVEGlsvsfpiRKGILRRVVDQNavLKNIRF 307
Cdd:TIGR00630 566 AGEHGGEVVASGTPEEILANPDSLTGQYL--SGRKKIEVPAER-----RPGNG-------KFLTLKGARENN--LKNITV 629
|
170 180
....*....|....*....|
gi 502863011 308 SLRPGESLGLVGESGSGKST 327
Cdd:TIGR00630 630 SIPLGLFTCITGVSGSGKST 649
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
282-526 |
8.16e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 282 SVSFPIRKGILrrvvdqNAVLKNIRFSLRPGESL--GLVGESGSGKSTTGLALLRLIAS-QGE--ILFDGMPLHRWNR-- 354
Cdd:PRK00635 363 TLTHKVWRGVL------NEIGEKVRYSNKPSRYLpkGTSATSCPRCQGTGLGDYANAATwHGKtfAEFQQMSLQELFIfl 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 355 RQMLPVRPRMQVVFQdpnsSLNPRLSILqiIEEGLrvhqPTLTalqrenevrrvmaevgldPEtrhRYPAEFSGGQRQRI 434
Cdd:PRK00635 437 SQLPSKSLSIEEVLQ----GLKSRLSIL--IDLGL----PYLT------------------PE---RALATLSGGEQERT 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863011 435 AIARAliLKPELI----ILDEPTSSLDRTVQAQILTLLKGLQEKHRlAYIFISHDLQVVrALCHQVIVLRQ------GEV 504
Cdd:PRK00635 486 ALAKH--LGAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRIIDIGPgagifgGEV 561
|
250 260
....*....|....*....|..
gi 502863011 505 VEQGECQRvFTAPTQSYTRQLL 526
Cdd:PRK00635 562 LFNGSPRE-FLAKSDSLTAKYL 582
|
|
| |
