|
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: 1048.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSLLH 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 241 ASTLLSAPQHPYTQRLLDSEPSGDPVPLAADSTPLLRVEDLSVSFPIRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGE 320
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 321 SGSGKSTTGLALLRLIASQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGLSAQQ 400
Cdd:PRK15134 321 SGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 401 REQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYI 480
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 658548496 481 FISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSAD 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: 964.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPvSYPQGDILFHGSSLLH 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPA-AHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 241 ASTLLSAPQHPYTQRLLDSEPSGDPVPLAADSTPLLRVEDLSVSFPIRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGE 320
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 321 SGSGKSTTGLALLRLIASQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGLSAQQ 400
Cdd:COG4172 321 SGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 401 REQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYI 480
Cdd:COG4172 401 RRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 658548496 481 FISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 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: 618.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFStqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvSYPQGDILFHGSSLLHAD 82
Cdd:COG1123 2 TPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG--GRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHtlrgIRGNKIAMIFQEPMVSLNPLhSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGER 162
Cdd:COG1123 78 EA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAS 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 243 TLLSAPQHPYTQRLLDSePSGDPVPLAADSTPLLRVEDLSVSFPIRKGilrrivDQNPVLKNIRFSLRPGESLGLVGESG 322
Cdd:COG1123 229 EILAAPQALAAVPRLGA-ARGRAAPAAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 323 SGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpGLSAQQR 401
Cdd:COG1123 302 SGKSTLARLLLGLLrPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHG-LLSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 402 EQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIF 481
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 658548496 482 ISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAA 507
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-528 |
2.71e-153 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 452.00 E-value: 2.71e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSS---- 77
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 78 -LLHADEHTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQ 156
Cdd:PRK10261 89 eLSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 237 EQNTASTLLSAPQHPYTQRLLDSEP-----SGDPVP---------------------LAADSTPLLRVEDLSVSFPIRKG 290
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPqlgamKGLDYPrrfplislehpakqeppieqdTVVDGEPILQVRNLVTRFPLRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 291 ILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPLHRWNRRQMLPVRPRMQVVFQ 369
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 370 DPNSSLNPRLSVLQIIEEGLRVHQ--PGLSAQQReqeVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVHGllPGKAAAAR---VAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
.
gi 658548496 528 A 528
Cdd:PRK10261 566 A 566
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-265 |
2.25e-134 |
|
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: 392.49 E-value: 2.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSypQGDILFHGSSLLHADEH 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGGERQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTL 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 658548496 245 LSAPQHPYTQRLLDSEPSGDP 265
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
269-528 |
2.79e-116 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 346.33 E-value: 2.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFPIRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDM 347
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGlSAQQREQEVMRVMAEVGLDAGTRHRYPAEFS 427
Cdd:COG4608 81 DITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLA-SKAERRERVAELLELVGLRPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260
....*....|....*....|.
gi 658548496 508 GECQRVFSAPTQRYTRQLLSA 528
Cdd:COG4608 240 APRDELYARPLHPYTQALLSA 260
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-528 |
6.37e-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: 6.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA----SQGEIFFDDMPLH 350
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPR-MQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLDAGTRH--RYPAEFS 427
Cdd:COG0444 74 KLSEKELRKIRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHG-GLSKAEARERAIELLERVGLPDPERRldRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260
....*....|....*....|.
gi 658548496 508 GECQRVFSAPTQRYTRQLLSA 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 |
1.08e-105 |
|
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: 315.60 E-value: 1.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWN 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQR 433
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 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 |
3.26e-105 |
|
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: 314.44 E-value: 3.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEH 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK--PTS---GSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRgIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILdCLERTGIRNAAKRLNDFPHQLSGGERQR 164
Cdd:cd03257 76 LRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQN 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-528 |
1.29e-97 |
|
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: 295.56 E-value: 1.29e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPL 349
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKST----LLRALAglerpWSGEVTFDGRPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNRRQMlpvRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHqpGLsaQQREQEVMRVMAEVGLDAGTRHRYPAEFSGG 429
Cdd:COG1124 70 TRRRRKAF---RRRVQMVFQDPYASLHPRHTVDRILAEPLRIH--GL--PDREERIAELLEQVGLPPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 658548496 510 CQRVFSAPTQRYTRQLLSA 528
Cdd:COG1124 223 VADLLAGPKHPYTRELLAA 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-265 |
1.29e-95 |
|
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: 299.90 E-value: 1.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQG-ETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR--PTS---GSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRGnKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRnaAKRLNDFPHQLSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQN 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|....*.
gi 658548496 240 TASTLLSAPQHPYTQRLLDSEPSGDP 265
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-264 |
2.53e-93 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 287.78 E-value: 2.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSypQGDILFHGSSLLH 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI--GGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|....
gi 658548496 241 ASTLLSAPQHPYTQRLLDSEPSGD 264
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLD 269
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-265 |
7.02e-88 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 273.53 E-value: 7.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQG-----ETRTV--VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILF 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PTS---GEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 74 HGSSLLHADEHTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRnaAKRLNDF 153
Cdd:COG4608 78 DGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLG 234
|
250 260 270
....*....|....*....|....*....|..
gi 658548496 234 RCVEQNTASTLLSAPQHPYTQRLLDSEPSGDP 265
Cdd:COG4608 235 KIVEIAPRDELYARPLHPYTQALLSAVPVPDP 266
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-264 |
1.02e-84 |
|
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: 271.94 E-value: 1.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAF--------STQGETRtVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSppvsypQGDILFHG 75
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrRTVGHVK-AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS------EGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 SSLLHADEHTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHR-GMRKEAARGEILDCLERTGIRNAAkrLNDFP 154
Cdd:COG4172 347 QDLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAA--RHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|
gi 658548496 235 CVEQNTASTLLSAPQHPYTQRLLDSEPSGD 264
Cdd:COG4172 504 VVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-259 |
7.77e-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: 260.12 E-value: 7.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLLHAD 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKS----TLLRALAglERPWS---GEVTFDGRPVTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGirgnKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRNAAkrLNDFPHQLSGGER 162
Cdd:COG1124 74 RKAFRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPSF--LDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAS 242
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250
....*....|....*..
gi 658548496 243 TLLSAPQHPYTQRLLDS 259
Cdd:COG1124 225 DLLAGPKHPYTRELLAA 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
273-528 |
5.57e-80 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 250.91 E-value: 5.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPIRKGILRRIVDQnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDM 347
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRRQQFE--AVKPVSFTLEAGQTLAIIGENGSGKST----LAKMLAgiiepTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRWNRRQmlpvRP---RMqvVFQDPNSSLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLDAGTRHRYPA 424
Cdd:COG4167 76 KLEYGDYKY----RCkhiRM--IFQDPNTSLNPRLNIGQILEEPLRLNT-DLTAEEREERIFATLRLVGLLPEHANFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 658548496 505 VEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTKRLIES 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
268-528 |
7.09e-78 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 247.70 E-value: 7.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 268 LAADSTPLLRVEDLSVSFPIRKGilRRIVDQNPV-LK---NIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEI 342
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDG--KQWFWQPPKtLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 343 FFDDMPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRY 422
Cdd:PRK15079 79 AWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260
....*....|....*....|....*.
gi 658548496 503 EVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSA 264
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-261 |
1.31e-77 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 246.96 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSP-PVSYPQgdILFHGSSLLHADE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgRVMAEK--LEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGGERQ 163
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAST 243
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*...
gi 658548496 244 LLSAPQHPYTQRLLDSEP 261
Cdd:PRK11022 241 IFRAPRHPYTQALLRALP 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
271-528 |
3.30e-77 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 246.03 E-value: 3.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 271 DSTPLLRVEDLSVSFPIRKGILR--RIVDqnpVLKNIRFSLRPGESLGLVGESGSGKSTTGlALLRLI--ASQGEIFFDD 346
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKpeRLVK---ALDGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIetPTGGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPgLSAQQREQEVMRVMAEVGLDAGTRHRYPAEF 426
Cdd:PRK11308 77 QDLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTS-LSAAERREKALAMMAKVGLRPEHYDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260
....*....|....*....|..
gi 658548496 507 QGECQRVFSAPTQRYTRQLLSA 528
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLSA 257
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-265 |
1.21e-67 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 220.99 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQ----GETRTV--VTDLSLQIQPGETLALVGESGSGKSVSAlsilRLLP--SPPVSypqGDIL 72
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKrglfKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLA----RLLTmiETPTG---GELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 73 FHGSSLLHADEHTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIR-NAAKRln 151
Cdd:PRK11308 74 YQGQDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDR-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 dFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQ 231
Cdd:PRK11308 151 -YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMY 229
|
250 260 270
....*....|....*....|....*....|....
gi 658548496 232 NGRCVEQNTASTLLSAPQHPYTQRLLDSEPSGDP 265
Cdd:PRK11308 230 LGRCVEKGTKEQIFNNPRHPYTQALLSATPRLNP 263
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-267 |
4.23e-64 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 212.07 E-value: 4.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLL-PSPPVSypqGDIL-FHGSSLLHA 81
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkDNWHVT---ADRFrWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVL--SLHRGM---RKEAARGEILDCLERTGIRNAAKRLNDFPHQ 156
Cdd:COG4170 79 SPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpsWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250 260 270
....*....|....*....|....*....|..
gi 658548496 237 EQNTASTLLSAPQHPYTQRLLDSEPS-GDPVP 267
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKALLRSMPDfRQPLP 270
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
272-528 |
3.05e-62 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 206.88 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFPIRKGILRRIVDQNpvlknirFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEI----FFDDM 347
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLN-------FSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRWNRRQMLPVRP-RMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGL-DAGTRHR-YPA 424
Cdd:PRK09473 82 EILNLPEKELNKLRAeQISMIFQDPMTSLNPYMRVGEQLMEVLMLHK-GMSKAEAFEESVRMLDAVKMpEARKRMKmYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250 260
....*....|....*....|....
gi 658548496 505 VEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:PRK09473 241 MEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
271-508 |
6.89e-61 |
|
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: 200.21 E-value: 6.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 271 DSTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFD 345
Cdd:COG1127 1 MSEPMIEVRNLTKSF-----------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSV----LLKLIIgllrpDSGEILVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNRRQMLPVRPRMQVVFQDP---NSslnprLSVLQIIEEGLRVHqPGLSAQQREQEVMRVMAEVGLdAGTRHRY 422
Cdd:COG1127 66 GQDITGLSEKELYELRRRIGMLFQGGalfDS-----LTVFENVAFPLREH-TDLSEAEIRELVLEKLELVGL-PGAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
....*.
gi 658548496 503 EVVEQG 508
Cdd:COG1127 219 KIIAEG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-265 |
4.06e-60 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 201.47 E-value: 4.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQG---------ETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILF 73
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-----DGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 74 HGSSLLHADEHTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVL-SLHRGMRKEAARGEILDCLERTGIRnaAKRLND 152
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLL--PNLINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQN 232
Cdd:PRK15079 158 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYL 237
|
250 260 270
....*....|....*....|....*....|...
gi 658548496 233 GRCVEQNTASTLLSAPQHPYTQRLLDSEPSGDP 265
Cdd:PRK15079 238 GHAVELGTYDEVYHNPLHPYTKALMSAVPIPDP 270
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-528 |
5.15e-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: 198.88 E-value: 5.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFpiRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWN 353
Cdd:TIGR02769 2 LLEVRDVTHTY--RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRvHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQR 433
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250
....*....|....*
gi 658548496 514 FSApTQRYTRQLLSA 528
Cdd:TIGR02769 239 LSF-KHPAGRNLQSA 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
273-528 |
4.65e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 196.45 E-value: 4.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFpiRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHR 351
Cdd:PRK10419 1 MTLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRvHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQR 431
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ---G 508
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvG 237
|
250 260
....*....|....*....|
gi 658548496 509 ECQRvFSAPTqryTRQLLSA 528
Cdd:PRK10419 238 DKLT-FSSPA---GRVLQNA 253
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
3-259 |
5.75e-59 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 196.19 E-value: 5.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKS--VSALSiLRLLPSppvsypQGDILFHGS---- 76
Cdd:COG4107 6 QPLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKStlLKCLY-FDLAPT------SGSVYYRDRdggp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 77 -SLLHADEHTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLsLHRGMRK-EAARGEILDCLERTGIrnAAKRLNDFP 154
Cdd:COG4107 79 rDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERL-MAAGERHyGDIRARALEWLERVEI--PLERIDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250 260
....*....|....*....|....*
gi 658548496 235 CVEQNTASTLLSAPQHPYTQRLLDS 259
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYTQLLVSS 260
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
276-517 |
2.60e-58 |
|
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: 193.32 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:COG1122 1 IELENLSFSYP----------GGTPALDDVSLSIEKGEFVAIIGPNGSGKST----LLRLLNgllkpTSGEVLVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQmlpVRPRMQVVFQDPNSslnprlsvlQIIEE--------GLRvhQPGLSAQQREQEVMRVMAEVGLdAGTRHRY 422
Cdd:COG1122 67 KKNLRE---LRRKVGLVFQNPDD---------QLFAPtveedvafGPE--NLGLPREEIRERVEEALELVGL-EHLADRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDG 210
|
250
....*....|....*
gi 658548496 503 EVVEQGECQRVFSAP 517
Cdd:COG1122 211 RIVADGTPREVFSDY 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-259 |
3.94e-58 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 193.76 E-value: 3.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAfstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsPPVSYPQGDILFHGSSLLHADeht 85
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGVRQTAGRVLLDGKPVAPCA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 lrgIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLslhRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQLSGGERQRV 165
Cdd:PRK10418 76 ---LRGRKIATIMQNPRSAFNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLL 245
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....
gi 658548496 246 SAPQHPYTQRLLDS 259
Cdd:PRK10418 230 NAPKHAVTRSLVSA 243
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-259 |
6.93e-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: 6.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQG-----ETRTVVTDLSLQIQPGETLALVGESGSGKSVSAlsilRLLPS--PPVSypqGDILFHGS 76
Cdd:COG4167 3 ALLEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLA----KMLAGiiEPTS---GEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 77 SLLHADEHTlrgiRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRnaAKRLNDFPHQ 156
Cdd:COG4167 76 KLEYGDYKY----RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLL--PEHANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 658548496 237 EQNTASTLLSAPQHPYTQRLLDS 259
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIES 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
276-527 |
4.61e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 193.76 E-value: 4.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLH 350
Cdd:COG1135 2 IELENLSKTFPTKGG-------PVTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInllerPTSGSVLVDGVDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQ 430
Cdd:COG1135 71 ALSERELRAARRKIGMIFQHFN--LLSSRTVAENVALPLEIA--GVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250
....*....|....*..
gi 658548496 511 QRVFSAPTQRYTRQLLS 527
Cdd:COG1135 226 LDVFANPQSELTRRFLP 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-507 |
2.00e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 188.33 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDM 347
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRWNRRQMLPVRpRMQV--VFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAE 425
Cdd:COG1136 71 DISSLSERELARLR-RRHIgfVFQFFN--LLPELTALENVALPLLLA--GVSRKERRERARELLERVGL-GDRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVV 505
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
..
gi 658548496 506 EQ 507
Cdd:COG1136 224 SD 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
275-528 |
4.75e-56 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 188.85 E-value: 4.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKGILRRivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWN 353
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 ---RRQmlpvrpRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQ 430
Cdd:PRK15112 82 ysyRSQ------RIRMIFQDPSTSLNPRQRISQILDFPLRLNT-DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*...
gi 658548496 511 QRVFSAPTQRYTRQLLSA 528
Cdd:PRK15112 235 ADVLASPLHELTKRLIAG 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-517 |
4.68e-54 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 182.40 E-value: 4.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKGILrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPL 349
Cdd:cd03258 1 MIELKNVSKVFGDTGGKV-------TALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCInglerPTSGSVLVDGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGG 429
Cdd:cd03258 70 TLLSGKELRKARRRIGMIFQHFN--LLSSRTVFENVALPLEIA--GVPKAEIEERVLELLELVGL-EDKADAYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
....*...
gi 658548496 510 CQRVFSAP 517
Cdd:cd03258 225 VEEVFANP 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-278 |
1.77e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.13 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCInllerPT------SGSVLVDGVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGnKIAMIFQepmvSLNPLHS----------LEkqlyevlslHRGMRKEAARGEILDCLERTGIrnaAKRL 150
Cdd:COG1135 72 LSERELRAARR-KIGMIFQ----HFNLLSSrtvaenvalpLE---------IAGVPKAEIRKRVAELLELVGL---SDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 151 NDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVM 230
Cdd:COG1135 135 DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 231 QNGRCVEQNTASTLLSAPQHPYTQRLLDSEPSGDP-------VPLAADSTPLLRV 278
Cdd:COG1135 215 ENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELpeellarLREAAGGGRLVRL 269
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-527 |
2.22e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 177.88 E-value: 2.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPL 349
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINlleepDSGTITVDGEDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRwNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGG 429
Cdd:COG1126 66 TD-SKKDINKLRRKVGMVFQQFN--LFPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLD-RTVqAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDpELV-GEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
250
....*....|....*....
gi 658548496 509 ECQRVFSAPTQRYTRQLLS 527
Cdd:COG1126 219 PPEEFFENPQHERTRAFLS 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
276-508 |
4.56e-52 |
|
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: 176.92 E-value: 4.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEIFFDDMPLH 350
Cdd:cd03261 1 IELRGLTKSF-----------GGRTVLKGVDLDVRRGEILAIIGPSGSGKST----LLRLIVGLlrpdsGEVLIDGEDIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPRMQVVFQDpnSSLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQ 430
Cdd:cd03261 66 GLSEAELYRLRRRMGMLFQS--GALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
270-506 |
5.94e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 177.59 E-value: 5.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 270 ADSTPLLRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFF 344
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIAglekpTSGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 345 DDMPLHRwnrrqmlpVRPRMQVVFQDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPA 424
Cdd:COG1116 71 DGKPVTG--------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELR--GVPKAERRERARELLELVGL-AGFEDAYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLkglqEKHRLAYIFISHDLQ--VvrALCHQVIV 498
Cdd:COG1116 138 QLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLW----QETGKTVLFVTHDVDeaV--FLADRVVV 211
|
250
....*....|
gi 658548496 499 L--RQGEVVE 506
Cdd:COG1116 212 LsaRPGRIVE 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
8.74e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 176.00 E-value: 8.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLL--PSppvsypQGDILFHGSSLLH 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPT------SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGNKIAMIFQEPmvslnplhslekQLYEVLS---------LHRGMRKEAARGEILDCLERTGIrnaAKRLN 151
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF------------NLLPELTalenvalplLLAGVSRKERRERARELLERVGL---GDRLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRkLADNVAVMQ 231
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLR 218
|
....*..
gi 658548496 232 NGRCVEQ 238
Cdd:COG1136 219 DGRIVSD 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-267 |
2.68e-51 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 178.07 E-value: 2.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlPSPPVSYPQGDILFHGSSLLHADE 83
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVL--SLHRGM-------RKEAArgeiLDCLERTGIRNAAKRLNDFP 154
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGRwwqrfgwRKRRA----IELLHRVGIKDHKDAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260 270
....*....|....*....|....*....|....
gi 658548496 235 CVEQNTASTLLSAPQHPYTQRLLDSEPS-GDPVP 267
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALIRAIPDfGSAMP 270
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
272-521 |
3.25e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 178.37 E-value: 3.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDD 346
Cdd:COG3842 2 AMPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAgfetpDSGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 mplhrwnrRQMLPVRP---RMQVVFQDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYP 423
Cdd:COG3842 67 --------RDVTGLPPekrNVGMVFQDY--ALFPHLTVAENVAFGLRMR--GVPKAEIRARVAELLELVGLE-GLADRYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
250
....*....|....*...
gi 658548496 504 VVEQGECQRVFSAPTQRY 521
Cdd:COG3842 214 IEQVGTPEEIYERPATRF 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-518 |
4.94e-51 |
|
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: 182.31 E-value: 4.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVsALSILRLLPS-PPVSypqGDILFH---------- 74
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV-LMHVLRGMDQyEPTS---GRIIYHvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 75 -------------GSSL-------LHADEHTLRGIRgNKIAMIFQ-------EPMVSLNPLHSLEKQLYEvlslhrgmrK 127
Cdd:TIGR03269 73 erpskvgepcpvcGGTLepeevdfWNLSDKLRRRIR-KRIAIMLQrtfalygDDTVLDNVLEALEEIGYE---------G 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 128 EAARGEILDCLERTgirNAAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELN 207
Cdd:TIGR03269 143 KEAVGRAVDLIEMV---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 208 MSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSApqhpYTQRLldSEPSGDPVPLAADstPLLRVEDLSVSF-P 286
Cdd:TIGR03269 220 ISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV----FMEGV--SEVEKECEVEVGE--PIIKVRNVSKRYiS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 287 IRKGILrRIVDqnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFD------DMPLHRWNRRQMlp 359
Cdd:TIGR03269 292 VDRGVV-KAVD------NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVRvgdewvDMTKPGPDGRGR-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 360 VRPRMQVVFQDpnSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVM------AEVGLDagtrhRYPAEFSGGQRQR 433
Cdd:TIGR03269 363 AKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVgfdeekAEEILD-----KYPDELSEGERHR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 434 IAIARALILKPELIILDEPTSSLD----RTVQAQILALLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*....
gi 658548496 510 CQRVFSAPT 518
Cdd:TIGR03269 512 PEEIVEELT 520
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-528 |
5.60e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 177.24 E-value: 5.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKGILRrIVDqnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIF-----FDDMPL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-AVD------RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekleFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWN---RRQMlpVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGlSAQQREQEVMRVMAEVGL-DAGTR-HRYPA 424
Cdd:PRK11022 76 QRISekeRRNL--VGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKKTRRQRAIDLLNQVGIpDPASRlDVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
250 260
....*....|....*....|....
gi 658548496 505 VEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:PRK11022 233 VETGKAHDIFRAPRHPYTQALLRA 256
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
276-504 |
6.20e-51 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 173.44 E-value: 6.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03255 1 IELKNLSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVRVDGTDIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPR-MQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGG 429
Cdd:cd03255 70 KLSEKELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLA--GVPKKERRERAEELLERVGLGD-RLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRaLCHQVIVLRQGEV 504
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-518 |
8.77e-51 |
|
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: 174.08 E-value: 8.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPL 349
Cdd:COG1120 1 MLEAENLSVGY-----------GGRPVLDDVSLSLPPGEVTALLGPNGSGKST----LLRALAgllkpSSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNRRQmlpVRPRMQVVFQDPNSSLNprLSVLQIIEEGLRVHQPGLSAQQRE--QEVMRVMAEVGLdAGTRHRYPAEFS 427
Cdd:COG1120 66 ASLSRRE---LARRIAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSAEdrEAVEEALERTGL-EHLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
250
....*....|.
gi 658548496 508 GECQRVFSAPT 518
Cdd:COG1120 220 GPPEEVLTPEL 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
277-503 |
9.36e-51 |
|
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: 172.65 E-value: 9.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHR 351
Cdd:cd03225 1 ELKNLSFSYP---------DGARPALDDISLTIKKGEFVLIVGPNGSGKST----LLRLLNgllgpTSGEVLVDGKDLTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQmlpVRPRMQVVFQDPNSSL-NPRlsvlqIIEE---GLRvhQPGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFS 427
Cdd:cd03225 68 LSLKE---LRRKVGLVFQNPDDQFfGPT-----VEEEvafGLE--NLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-513 |
5.96e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 171.78 E-value: 5.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMP 348
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNglvepTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHQPGL-------SAQQReQEVMRVMAEVGLdAGTRHR 421
Cdd:COG3638 67 VTALRGRALRRLRRRIGMIFQQFN--LVPRLSVLTNVLAGRLGRTSTWrsllglfPPEDR-ERALEALERVGL-ADKAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 422 YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 658548496 502 GEVVEQGECQRV 513
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-505 |
7.33e-50 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 178.67 E-value: 7.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKS--VSALS-ILrllpsPPVSypqGDILFHGSsl 78
Cdd:COG1129 1 AEPLLEMRGISKSF---GGVK-ALDGVSLELRPGEVHALLGENGAGKStlMKILSgVY-----QPDS---GEILLDGE-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 lhadEHTLRGIR---GNKIAMIFQEPmvslnplhSLEKQL--YEVLSL-----------HRGMRKEAARgeildCLERTG 142
Cdd:COG1129 67 ----PVRFRSPRdaqAAGIAIIHQEL--------NLVPNLsvAENIFLgreprrgglidWRAMRRRARE-----LLARLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 143 IR-NAAKRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVR 221
Cdd:COG1129 130 LDiDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 222 KLADNVAVMQNGRCVEQNTASTLlsapqhpyTQ---------RLLDSEpsgDPVPLAADSTPLLRVEDLSVsfpirkgil 292
Cdd:COG1129 205 EIADRVTVLRDGRLVGTGPVAEL--------TEdelvrlmvgRELEDL---FPKRAAAPGEVVLEVEGLSV--------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 293 rrivdqNPVLKNIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEIFFDDMPLHRWNRRQ-------MLPV 360
Cdd:COG1129 265 ------GGVVRDVSFSVRAGEILGIAGLVGAGRT----ELARALfgadpADSGEIRLDGKPVRIRSPRDairagiaYVPE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 361 RPRMQVVFQDPNSSLNPRLSVLQiieeglRVHQPGLSAQQREQE-VMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARA 439
Cdd:COG1129 335 DRKGEGLVLDLSIRENITLASLD------RLSRGGLLDRRRERAlAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKW 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 440 LILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-257 |
1.60e-49 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 170.55 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpsPPVSypqGDILFHGSSLLH 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL--RPDS---GEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRgNKIAMIFQEPMV--SLNPLHSLEKQLYEvlslHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLS 158
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGALfdSLTVFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---MPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VTVqAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250 260
....*....|....*....|
gi 658548496 238 QNTASTLLSAPqHPYTQRLL 257
Cdd:COG1127 223 EGTPEELLASD-DPWVRQFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-507 |
2.83e-49 |
|
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: 169.19 E-value: 2.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIAglerpTSGEVLVDGEPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RwnrrqmlpVRPRMQVVFQDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQ 430
Cdd:cd03293 70 G--------PGPDRGYVFQQD--ALLPWLTVLDNVALGLELQ--GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL--RQGEVVEQ 507
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
276-508 |
4.70e-49 |
|
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: 168.47 E-value: 4.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03259 1 LELKGLSKTY-----------GSVRALDDLSLTVEPGEFLALLGPSGCGKTT----LLRLIAglerpDSGEILIDGRDVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RwnrrqmLPVRPR---MqvVFQDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFS 427
Cdd:cd03259 66 G------VPPERRnigM--VFQDY--ALFPHLTVAENIAFGLKLR--GVPKAEIRARVRELLELVGLE-GLLNRYPHELS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03259 133 GGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
.
gi 658548496 508 G 508
Cdd:cd03259 213 G 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-265 |
1.74e-48 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 177.35 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGE-----TRTV--VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHG 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-----GGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 SSLLHADEHTLRGIRGNkIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIR-NAAKRlndFP 154
Cdd:PRK10261 386 QRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWR---YP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
250 260 270
....*....|....*....|....*....|.
gi 658548496 235 CVEQNTASTLLSAPQHPYTQRLLDSEPSGDP 265
Cdd:PRK10261 542 IVEIGPRRAVFENPQHPYTRKLMAAVPVADP 572
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
1.94e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 164.20 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLpSPPVSypqGDILFHGSSLLHADEHT 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGL-DRPTS---GEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGNKIAMIFQEpmvslnplHSLEKQL--YEVLSL---HRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGG 160
Cdd:cd03255 76 LAAFRRRHIGFVFQS--------FNLLPDLtaLENVELpllLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRkLADNVAVMQNGR 234
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
1.61e-46 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 163.17 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKS--VSALSiLRLLPSppvsypQGDILFHG--- 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTtlLNALS-ARLAPD------AGEVHYRMrdg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 --SSLLHADEHTLRGIRGNKIAMIFQEPMVSLNPLHS----LEKQLYEVLSLHRGMRKEAArgeiLDCLERTGIrnAAKR 149
Cdd:PRK11701 71 qlRDLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSaggnIGERLMAVGARHYGDIRATA----GDWLERVEI--DAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 150 LNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAV 229
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|
gi 658548496 230 MQNGRCVEQNTASTLLSAPQHPYTQRLLDS 259
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
276-509 |
1.62e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 161.76 E-value: 1.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:COG2884 2 IRFENVSKRYP----------GGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQVLVNGQDLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQ 430
Cdd:COG2884 68 RLKRREIPYLRRRIGVVFQDFR--LLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqekHRL--AYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI---NRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
.
gi 658548496 509 E 509
Cdd:COG2884 220 A 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
276-508 |
1.63e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.16 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEIFFDDMPLH 350
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRMLLgllrpTSGEVRVLGEDVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRqmlpVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQ 430
Cdd:COG1131 66 RDPAE----VRRRIGYVPQEPA--LYPDLTVRENLRFFARLY--GLPRKEARERIDELLELFGLT-DAADRKVGTLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFIS-HDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT--VLLStHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-249 |
2.97e-46 |
|
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: 161.59 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLL 79
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS----TLIRCInglerPT------SGSVLVDGTDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRgNKIAMIFQEpmvsLNPLHSleKQLYEVLSL---HRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQ 156
Cdd:cd03258 71 LLSGKELRKAR-RRIGMIFQH----FNLLSS--RTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADA---YPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
250
....*....|...
gi 658548496 237 EQNTASTLLSAPQ 249
Cdd:cd03258 221 EEGTVEEVFANPQ 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
271-518 |
1.67e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.87 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 271 DSTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFD 345
Cdd:COG1121 2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKAILgllppTSGTVRLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNRR-----QMLPVRPRMqvvfqdpnsslnPrLSVLQIIEEGLRVHQP---GLSAQQREQeVMRVMAEVGLdAG 417
Cdd:COG1121 67 GKPPRRARRRigyvpQRAEVDWDF------------P-ITVRDVVLMGRYGRRGlfrRPSRADREA-VDEALERVGL-ED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVI 497
Cdd:COG1121 132 LADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVL 210
|
250 260
....*....|....*....|.
gi 658548496 498 VLRQGeVVEQGECQRVFSAPT 518
Cdd:COG1121 211 LLNRG-LVAHGPPEEVLTPEN 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
276-526 |
8.35e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.08 E-value: 8.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:COG1118 3 IEVRNISKRFG-----------SFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAgletpDSGRIVLNGRDLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWnrrqmLPVRPRmQV--VFQDPnsSLNPRLSVLQIIEEGLRVHQPglSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSG 428
Cdd:COG1118 68 TN-----LPPRER-RVgfVFQHY--ALFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQLE-GLADRYPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....*...
gi 658548496 509 ECQRVFSAPTQRYTRQLL 526
Cdd:COG1118 217 TPDEVYDRPATPFVARFL 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
270-526 |
2.55e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 157.40 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 270 ADSTPLLRVEDLSVSFPIRKGilrrivdqnpvLKNIRFSLRPGESLGLVGESGSGKSTTgLALL--RLIASQGEIFFDD- 346
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG-----------CRDVSFDLYPGEVLGIVGESGSGKTTL-LNALsaRLAPDAGEVHYRMr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 ----MPLHRWN--RRQMLpVRPRMQVVFQDPNSSLNPRLSVlqiieeGLRVHQPGLSAQQR-----EQEVMRVMAEVGLD 415
Cdd:PRK11701 69 dgqlRDLYALSeaERRRL-LRTEWGFVHQHPRDGLRMQVSA------GGNIGERLMAVGARhygdiRATAGDWLERVEID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 416 AGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQ 495
Cdd:PRK11701 142 AARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHR 221
|
250 260 270
....*....|....*....|....*....|.
gi 658548496 496 VIVLRQGEVVEQGECQRVFSAPTQRYTrQLL 526
Cdd:PRK11701 222 LLVMKQGRVVESGLTDQVLDDPQHPYT-QLL 251
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
5.21e-44 |
|
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: 155.57 E-value: 5.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSiaFSTQGETRtVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLlh 80
Cdd:COG1122 1 IELENLS--FSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKS----TLLRLLngllkPT------SGEVLVDGKDI-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 aDEHTLRGIRgNKIAMIFQEPmvslnplhslEKQLYE--VLS------LHRGMRKEAARGEILDCLERTGIRNAAKRlnd 152
Cdd:COG1122 66 -TKKNLRELR-RKVGLVFQNP----------DDQLFAptVEEdvafgpENLGLPREEIRERVEEALELVGLEHLADR--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 153 FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQN 232
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD 209
|
250
....*....|....*..
gi 658548496 233 GRCVEQNTASTLLSAPQ 249
Cdd:COG1122 210 GRIVADGTPREVFSDYE 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-252 |
5.29e-44 |
|
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: 155.74 E-value: 5.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHT 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--PDS---GEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRgNKIAMIFQEPMV--SLNPLHSLEKQLYEvlslHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQ 163
Cdd:cd03261 72 LYRLR-RRMGMLFQSGALfdSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAST 243
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 658548496 244 LLsAPQHPY 252
Cdd:cd03261 224 LR-ASDDPL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-505 |
6.08e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 162.50 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTqgetrtVV--TDLSLQIQPGETLALVGESGSGKS--VSalsilrllpsppvsypqgdILFhGs 76
Cdd:COG3845 1 MMPPALELRGITKRFGG------VVanDDVSLTVRPGEIHALLGENGAGKStlMK-------------------ILY-G- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 77 sLLHADEHTLRgIRGNK-------------IAMIFQEPMvslnplhslekqLYEVLS------------LHRGMRKEAAR 131
Cdd:COG3845 54 -LYQPDSGEIL-IDGKPvrirsprdaialgIGMVHQHFM------------LVPNLTvaenivlgleptKGGRLDRKAAR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 132 GEILDCLERTGIR-NAAKRLndfpHQLSGGERQRVMIAMALLTRPELLIADEPTTALdvTVQ--AQILTLLRELRDElNM 208
Cdd:COG3845 120 ARIRELSERYGLDvDPDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 209 SLLFITHNLSIVRKLADNVAVMQNGRCV-EQNTASTllsapqhpytqrlldSEPS------GDPVPLAADSTP------L 275
Cdd:COG3845 193 SIIFITHKLREVMAIADRVTVLRRGKVVgTVDTAET---------------SEEElaelmvGREVLLRVEKAPaepgevV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVsfPIRKGIlrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSttglALLRLIA-----SQGEIFFDDMPLH 350
Cdd:COG3845 258 LEVENLSV--RDDRGV--------PALKDVSLEVRAGEILGIAGVAGNGQS----ELAEALAglrppASGSIRLDGEDIT 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLpvrpRMQVVF--QDPNSS-LNPRLSV-----LQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRY 422
Cdd:COG3845 324 GLSPRERR----RLGVAYipEDRLGRgLVPDMSVaenliLGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALL-KGlqekhrLAYIFISHDLQVVRALCHQVI 497
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRdAG------AAVLLISEDLDEILALSDRIA 473
|
....*...
gi 658548496 498 VLRQGEVV 505
Cdd:COG3845 474 VMYEGRIV 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-279 |
1.94e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 157.27 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHAD 82
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS----TLIRCInllerPT------SGRVLVDGQDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGIRgNKIAMIFQEpmvsLNPLHSleKQLYEVLSLH---RGMRKEAARGEILDCLERTGIrnAAKRlNDFPHQLSG 159
Cdd:PRK11153 74 EKELRKAR-RQIGMIFQH----FNLLSS--RTVFDNVALPlelAGTPKAEIKARVTELLELVGL--SDKA-DRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQN 239
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 658548496 240 TASTLLSAPQHPYTQRLLDS-EPSGDP--------VPLAADSTPLLRVE 279
Cdd:PRK11153 224 TVSEVFSHPKHPLTREFIQStLHLDLPedylarlqAEPTTGSGPLLRLE 272
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-247 |
2.08e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL--RLLPSppvsypQGDILFHGSSLLHADE 83
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIRMLlgLLRPT------SGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRgirgnKIAMIFQEPmvslnplhSLEKQL--YEVLSLH---RGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:COG1131 70 EVRR-----RIGYVPQEP--------ALYPDLtvRENLRFFarlYGLPRKEARERIDELLELFGLTDAADRK---VGTLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:COG1131 134 GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
....*....
gi 658548496 239 NTASTLLSA 247
Cdd:COG1131 213 GTPDELKAR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-257 |
3.63e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 153.61 E-value: 3.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFstqGETrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLl 79
Cdd:COG1126 1 MIEIENLHKSF---GDL-EVLKGISLDVEKGEVVVIIGPSGSGKS----TLLRCInlleePD------SGTITVDGEDL- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRGnKIAMIFQE----P-M-----VSLNPLHslekqlyevlslHRGMRKEAARGEILDCLERTGIrnaAKR 149
Cdd:COG1126 66 TDSKKDINKLRR-KVGMVFQQfnlfPhLtvlenVTLAPIK------------VKKMSKAEAEERAMELLERVGL---ADK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 150 LNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAV 229
Cdd:COG1126 130 ADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVF 208
|
250 260
....*....|....*....|....*...
gi 658548496 230 MQNGRCVEQNTASTLLSAPQHPYTQRLL 257
Cdd:COG1126 209 MDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
297-524 |
5.15e-43 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 153.95 E-value: 5.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLHRWNRRQMLPVR-PRMQVVFQd 370
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKST----LLRCInrliePTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQ- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 pNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03294 110 -SFALLPHRTVLENVAFGLEVQ--GVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQ 524
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
269-528 |
9.34e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 153.03 E-value: 9.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIF 343
Cdd:COG4598 2 TDTAPPALEVRDLHKSF-----------GDLEVLKGVSLTARKGDVISIIGSSGSGKST----FLRCInlletPDSGEIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 344 FDDMPLhRW-----------NRRQMLPVRPRMQVVFQDPNssLNPRLSVLQ-IIEEGLRVHqpGLSAQQREQEVMRVMAE 411
Cdd:COG4598 67 VGGEEI-RLkpdrdgelvpaDRRQLQRIRTRLGMVFQSFN--LWSHMTVLEnVIEAPVHVL--GRPKAEAIERAEALLAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 412 VGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRA 491
Cdd:COG4598 142 VGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARD 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 658548496 492 LCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:COG4598 220 VSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
297-508 |
1.14e-42 |
|
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: 161.93 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDP 371
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKST----LLKLLLglyepTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 ---NSSlnprlsvlqiIEEGLRVHQPGLSaqqrEQEVMRVMAEVGLDAGTRHRyP-----------AEFSGGQRQRIAIA 437
Cdd:COG2274 559 flfSGT----------IRENITLGDPDAT----DEEIIEAARLAGLHDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 438 RALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGEVVEQG 508
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
276-503 |
1.80e-42 |
|
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: 149.64 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03229 1 LELKNVSKRYG-----------QKTVLNDVSLNIEAGEIVALLGPSGSGKST----LLRCIAgleepDSGSILIDGEDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RwNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLrvhqpglsaqqreqevmrvmaevgldagtrhrypaefSGGQ 430
Cdd:cd03229 66 D-LEDELPPLRRRIGMVFQDFA--LFPHLTVLENIALGL-------------------------------------SGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
275-509 |
3.82e-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: 150.78 E-value: 3.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPL 349
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTT----LLRMLAgllkpDSGSILIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNRRqmlpVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGG 429
Cdd:COG4555 66 RKEPRE----ARRQIGVLPDERG--LYDRLTVRENIRYFAELY--GLFDEELKKRIEELIELLGLE-EFLDRRVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-233 |
4.66e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.01 E-value: 4.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQ--PLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILF 73
Cdd:COG1116 1 MSAaaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIaglekPT------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 74 HGSSLLHAdehtlrgirGNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndF 153
Cdd:COG1116 71 DGKPVTGP---------GPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---Y 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLS-IVRkLADNVAVMQN 232
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSA 214
|
.
gi 658548496 233 G 233
Cdd:COG1116 215 R 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-506 |
5.48e-42 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 157.53 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhgSSLLHADEHTLR 87
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKIL----------------AGELEPDSGEVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 88 GIRGNKIAMIFQEP------------MVSLNPLHSLEKQLYEVLSLHRGMRKEAAR-GEILDCLERTG-------IRNAA 147
Cdd:COG0488 57 IPKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERlAELQEEFEALGgweaearAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 148 KRLN--DFPHQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALDVtvqAQILTLLRELRDElNMSLLFITHNLSIV 220
Cdd:COG0488 137 SGLGfpEEDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNY-PGTVLVVSHDRYFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 221 RKLADNVAVMQNGRCVE--------------------------QNTASTLL------SAPQHPYTQ-----------RLL 257
Cdd:COG0488 213 DRVATRILELDRGKLTLypgnysayleqraerleqeaaayakqQKKIAKEEefirrfRAKARKAKQaqsrikaleklERE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 258 DSEPSGDPVPLAADSTP-----LLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaL 332
Cdd:COG0488 293 EPPRRDKTVEIRFPPPErlgkkVLELEGLSKSY-----------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKST----L 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 333 LRLIA-----SQGEIffddmplhRWNrrqmlpvrPRMQVVF--QDpNSSLNPRLSVLQIIEEGlrvhqpglSAQQREQEV 405
Cdd:COG0488 358 LKLLAgelepDSGTV--------KLG--------ETVKIGYfdQH-QEELDPDKTVLDELRDG--------APGGTEQEV 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 406 MRVMAEVGLDaGTRHRYPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAQILALL--KGlqekhrlAYIF 481
Cdd:COG0488 413 RGYLGRFLFS-GDDAFKPVGvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDiETLEALEEALDdfPG-------TVLL 484
|
570 580
....*....|....*....|....*
gi 658548496 482 ISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:COG0488 485 VSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
297-521 |
6.61e-42 |
|
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: 149.69 E-value: 6.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmLPVRPR-MQVVFQd 370
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIAgfetpTSGEILLDGKDITN------LPPHKRpVNTVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 pNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03300 80 -NYALFPHLTVFENIAFGLRLK--KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
274-528 |
1.04e-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: 149.98 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPIRKGilrrivdqnpvLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEIFFDD------ 346
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKG-----------CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYIMrsgael 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 --MPLHRWNRRQMLpvRPRMQVVFQDPNSSLNPRLSVLQIIEEGLrvhqpgLSAQQREQEVMRVMA-----EVGLDAGTR 419
Cdd:TIGR02323 71 elYQLSEAERRRLM--RTEWGFVHQNPRDGLRMRVSAGANIGERL------MAIGARHYGNIRATAqdwleEVEIDPTRI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:TIGR02323 143 DDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
250 260
....*....|....*....|....*....
gi 658548496 500 RQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:TIGR02323 223 QQGRVVESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
1.48e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKS--VSAlsILRLLPspPVSypqGDILFHGSSL 78
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKStlLKA--ILGLLP--PTS---GTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHAdehtlrgirGNKIAMIFQEPMVSLN-PLHslekqLYEVLSL----HRGMRK---EAARGEILDCLERTGIRNAAKRl 150
Cdd:COG1121 71 RRA---------RRRIGYVPQRAEVDWDfPIT-----VRDVVLMgrygRRGLFRrpsRADREAVDEALERVGLEDLADR- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 151 ndfP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAV 229
Cdd:COG1121 136 ---PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLL 211
|
250
....*....|....*....
gi 658548496 230 MqNGRCVEQNTASTLLSAP 248
Cdd:COG1121 212 L-NRGLVAHGPPEEVLTPE 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
292-504 |
5.30e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 5.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNrrqmlPVRPRMQV 366
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKST----LLRALAdldppTSGEIYLDGKPLSAMP-----PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 367 --VFQDPnsslnprlsvlQIIEEGLRVH--QPGLSAQQR--EQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARAL 440
Cdd:COG4619 77 ayVPQEP-----------ALWGGTVRDNlpFPFQLRERKfdRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 441 ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-247 |
5.45e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.88 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvSAL-SILRLLPspPVSypqGDILFHGSSLlhade 83
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLK--PSS---GEVLLDGRDL----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGI-RGNKIAMIFQEPMVSLnPLHslekqLYEVLSL----HRGM---RKEAARGEILDCLERTGIRNAAKRlnDFpH 155
Cdd:COG1120 66 ASLSRReLARRIAYVPQEPPAPF-GLT-----VRELVALgrypHLGLfgrPSAEDREAVEEALERTGLEHLADR--PV-D 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRC 235
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250
....*....|..
gi 658548496 236 VEQNTASTLLSA 247
Cdd:COG1120 217 VAQGPPEEVLTP 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-259 |
6.03e-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: 6.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGETRtvvtDLSLQIQPGETLALVGESGSGKS--VSALSIlRLLPSP-PVSYPQGDILFHgsSLL 79
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCR----DVSFDLYPGEVLGIVGESGSGKStlLGCLAG-RLAPDHgTATYIMRSGAEL--ELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRGNKIAMIFQEPMVSLNPLHS----LEKQLYEVLSLHRGMRKEAARgeilDCLERTGIRnaAKRLNDFPH 155
Cdd:TIGR02323 74 QLSEAERRRLMRTEWGFVHQNPRDGLRMRVSaganIGERLMAIGARHYGNIRATAQ----DWLEEVEID--PTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRC 235
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....
gi 658548496 236 VEQNTASTLLSAPQHPYTQRLLDS 259
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
254-508 |
9.16e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 154.53 E-value: 9.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 254 QRLLDSEPSGDP---VPLAADSTPLLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGL 330
Cdd:COG4988 312 FALLDAPEPAAPagtAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 331 ALLRLI-ASQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPGLSaqqrEQEVM 406
Cdd:COG4988 382 LLLGFLpPYSGSILINGVDLSDLDPAS---WRRQIAWVPQNPylfAGT----------IRENLRLGRPDAS----DEELE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 407 RVMAEVGLDA----------------GTRhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKG 470
Cdd:COG4988 445 AALEAAGLDEfvaalpdgldtplgegGRG------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
|
250 260 270
....*....|....*....|....*....|....*...
gi 658548496 471 LQEKHRLayIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG4988 519 LAKGRTV--ILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
9.50e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.25 E-value: 9.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHG 75
Cdd:COG3842 1 MAMPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKT----TLLRMIagfetPD------SGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 SSLLH--ADEhtlrgiRGnkIAMIFQEP-----M-VSLN---PLHslekqlyevlslHRGMRKEAARGEILDCLERTGIR 144
Cdd:COG3842 67 RDVTGlpPEK------RN--VGMVFQDYalfphLtVAENvafGLR------------MRGVPKAEIRARVAELLELVGLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 145 NAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHN----LSiv 220
Cdd:COG3842 127 GLADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA-- 201
|
250 260 270
....*....|....*....|....*....|..
gi 658548496 221 rkLADNVAVMQNGRCVEQNTASTLLSAPQHPY 252
Cdd:COG3842 202 --LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
269-506 |
1.92e-40 |
|
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: 146.04 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFPIRKGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIF 343
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELT-------ILKGISLEVEAGESVAIVGASGSGKST----LLGLLAgldrpTSGTVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 344 FDDMPLHRWNRRQMLPVRPR-MQVVFQdpNSSLNPRLSVLQ-----IIEEGLRvhqpglSAQQREQEVMrvmAEVGLDAG 417
Cdd:COG4181 71 LAGQDLFALDEDARARLRARhVGFVFQ--SFQLLPTLTALEnvmlpLELAGRR------DARARARALL---ERVGLGHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 418 TRHrYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVI 497
Cdd:COG4181 140 LDH-YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVL 217
|
....*....
gi 658548496 498 VLRQGEVVE 506
Cdd:COG4181 218 RLRAGRLVE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-234 |
2.79e-40 |
|
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: 144.92 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHA 81
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKS----TLLRLLngllgPT------SGEVLVDGKDLTKL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRGirgnKIAMIFQEPmvslnplhslEKQLY------EVLS--LHRGMRKEAARGEILDCLERTGIRNAAKRLndf 153
Cdd:cd03225 69 SLKELRR----KVGLVFQNP----------DDQFFgptveeEVAFglENLGLPEEEIEERVEEALELVGLEGLRDRS--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:cd03225 132 PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
.
gi 658548496 234 R 234
Cdd:cd03225 211 K 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-517 |
3.80e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 148.68 E-value: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDmplH 350
Cdd:COG3839 4 LELENVSKSY-----------GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAgledpTSGEILIGG---R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRrqmLPVRPR---MqvVFQDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFS 427
Cdd:COG3839 66 DVTD---LPPKDRniaM--VFQSY--ALYPHMTVYENIAFPLKLR--KVPKAEIDRRVREAAELLGLED-LLDRKPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDlQV-VRALCHQVIVLRQGEVVE 506
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD-QVeAMTLADRIAVMNDGRIQQ 214
|
250
....*....|.
gi 658548496 507 QGECQRVFSAP 517
Cdd:COG3839 215 VGTPEELYDRP 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
276-504 |
4.14e-40 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 144.21 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03262 1 IEIKNLHKSF-----------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleepDSGTIIIDGLKLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RwNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQ 430
Cdd:cd03262 66 D-DKKNINELRQKVGMVFQQFN--LFPHLTVLENITLAPIKVK-GMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-508 |
4.44e-40 |
|
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: 145.13 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWN 353
Cdd:TIGR02315 1 MLEVENLSKVYP----------NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHQP---GLSAQQREQEVMRVMA---EVGLdAGTRHRYPAEFS 427
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQHYN--LIERLTVLENVLHGRLGYKPtwrSLLGRFSEEDKERALSaleRVGL-ADKAYQRADQLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
.
gi 658548496 508 G 508
Cdd:TIGR02315 228 G 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
277-499 |
4.81e-40 |
|
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: 144.21 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHR 351
Cdd:cd03235 1 EVEDLTVSY-----------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKST----LLKAILgllkpTSGSIRVFGKPLEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 wnrrqmlpVRPRMQVVFQDPNSSLNPRLSVLQIIEEGL---RVHQPGLSAQQREqEVMRVMAEVGLdAGTRHRYPAEFSG 428
Cdd:cd03235 66 --------ERKRIGYVPQRRSIDRDFPISVRDVVLMGLyghKGLFRRLSKADKA-KVDEALERVGL-SELADRQIGELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLQVVRALCHQVIVL 499
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTI-LVVTHDLGLVLEYFDRVLLL 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
256-508 |
4.90e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 152.61 E-value: 4.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 256 LLDSEP--SGDPVPLAADSTPLLRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL 333
Cdd:COG4987 312 LLDAPPavTEPAEPAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 334 RLI-ASQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPGLSaqqrEQEVMRVM 409
Cdd:COG4987 383 RFLdPQSGSITLGGVDLRDLDEDD---LRRRIAVVPQRPhlfDTT----------LRENLRLARPDAT----DEELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 410 AEVGLD----------------AGTRhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKG-LQ 472
Cdd:COG4987 446 ERVGLGdwlaalpdgldtwlgeGGRR------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLA 519
|
250 260 270
....*....|....*....|....*....|....*.
gi 658548496 473 EKhrlAYIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:COG4987 520 GR---TVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
276-503 |
8.55e-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: 142.14 E-value: 8.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNR 354
Cdd:cd03228 1 IEFKNVSFSYP---------GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 355 RQmlpVRPRMQVVFQDP---NSSlnprlsvlqiIEEGLrvhqpglsaqqreqevmrvmaevgldagtrhrypaeFSGGQR 431
Cdd:cd03228 72 ES---LRKNIAYVPQDPflfSGT----------IRENI------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGE 503
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
298-518 |
1.36e-39 |
|
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: 144.90 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPN 372
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTliqhlNGL----LKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 SslnprlsvlQIIEE--------GLRvhQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:TIGR04521 93 H---------QLFEEtvykdiafGPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 445 ELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
276-513 |
1.38e-39 |
|
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: 143.86 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLH 350
Cdd:cd03256 1 IEVENLSKTYP----------NGKKALKDVSLSINPGEFVALIGPSGAGKST----LLRCLnglvePTSGSVLIDGTDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEG-------LRVHQPGLSAQQReQEVMRVMAEVGLD--AGTRhr 421
Cdd:cd03256 67 KLKGKALRQLRRQIGMIFQQFN--LIERLSVLENVLSGrlgrrstWRSLFGLFPKEEK-QRALAALERVGLLdkAYQR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 422 yPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:cd03256 142 -ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
250
....*....|..
gi 658548496 502 GEVVEQGECQRV 513
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-259 |
1.45e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 144.83 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQG-----ETRTVVTDLSLQIQPGETLALVGESGSGKSVSAlSILRLLPSPPvsypQGDILFHGSSL 78
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLA-RLLVGLESPS----QGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHADEHTLRGIRGNkIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNA-AKRLndfPHQL 157
Cdd:PRK10419 77 AKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKR---PPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260
....*....|....*....|..
gi 658548496 238 QNTASTLLSApQHPYTQRLLDS 259
Cdd:PRK10419 233 TQPVGDKLTF-SSPAGRVLQNA 253
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
256-508 |
1.71e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.47 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 256 LLDSEPSGDPVPLAADSTPL---LRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaL 332
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVrgeIEFENVSFSYP----------GDRPVLKDISLTIPPGETVALVGPSGSGKST----L 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 333 LRLIA-----SQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPGLSaqqrEQE 404
Cdd:COG1132 383 VNLLLrfydpTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTflfSGT----------IRENIRYGRPDAT----DEE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 405 VMRV--MAEV---------GLDA-----GTRhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQI 464
Cdd:COG1132 446 VEEAakAAQAhefiealpdGYDTvvgerGVN------LSGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEAL 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 658548496 465 LALLKGlqekhRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG1132 520 ERLMKG-----RTT-IVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-259 |
2.23e-39 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 144.16 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQG-----ETRTVVTDLSLQIQPGETLALVGESGSGKSVSAlsilRLLpSPPVSYPQGDILFHGSSLL 79
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLA----KML-AGMIEPTSGELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHtlrgIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNaaKRLNDFPHQLSG 159
Cdd:PRK15112 79 FGDYS----YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP--DHASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQN 239
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
250 260
....*....|....*....|
gi 658548496 240 TASTLLSAPQHPYTQRLLDS 259
Cdd:PRK15112 233 STADVLASPLHELTKRLIAG 252
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-242 |
2.62e-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: 142.96 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHG 75
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLagldrPT------SGTVRLAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 SSLLHADEHTLRGIRGNKIAMIFQEPMVsLNPLHSLEkqlYEVLSLH-RGMRKEAARGEILdcLERTGIrnaAKRLNDFP 154
Cdd:COG4181 74 QDLFALDEDARARLRARHVGFVFQSFQL-LPTLTALE---NVMLPLElAGRRDARARARAL--LERVGL---GHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKlADNVAVMQNGR 234
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*...
gi 658548496 235 CVEQNTAS 242
Cdd:COG4181 224 LVEDTAAT 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
302-528 |
2.76e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.10 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPN--SS 374
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKST----LIRCInllerPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNllSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNprlsVLQIIEEGLRVhqPGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK11153 97 RT----VFDNVALPLEL--AGTPKAEIKARVTELLELVGLSD-KADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
307-528 |
3.40e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.59 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmLPV--RPrMQVVFQDPNssLNPRL 379
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKST----LLNLIAgflppDSGRILWNGQDLTA------LPPaeRP-VSMLFQENN--LFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 SVLQIIEEGLRvhqPG--LSAQQREQeVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:COG3840 87 TVAQNIGLGLR---PGlkLTAEQRAQ-VEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
277-508 |
5.30e-39 |
|
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: 140.26 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHR 351
Cdd:cd03214 1 EVENLSVGY-----------GGRTVLDDLSLSIEAGEIVGILGPNGAGKST----LLKTLAgllkpSSGEILLDGKDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQMlpvRPRMQVVFQdpnsslnprlsvlqiieeglrvhqpglsaqqreqevmrVMAEVGLdAGTRHRYPAEFSGGQR 431
Cdd:cd03214 66 LSPKEL---ARKIAYVPQ--------------------------------------ALELLGL-AHLADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
272-508 |
5.65e-39 |
|
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: 142.87 E-value: 5.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFpirkGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDD 346
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLV-------AVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLItgfyrPTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNRRQmlpvRPRMQVV--FQdpNSSLNPRLSVLQ-------------IIEEGLRVHQPGLSAQQREQEVMRVMAE 411
Cdd:COG0411 66 RDITGLPPHR----IARLGIArtFQ--NPRLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 412 VGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG0411 140 VGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMG 218
|
250
....*....|....*..
gi 658548496 492 LCHQVIVLRQGEVVEQG 508
Cdd:COG0411 219 LADRIVVLDFGRVIAEG 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
302-454 |
6.14e-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: 138.93 E-value: 6.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDPNssLN 376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKST----LLKLIAgllspTEGTILLDGQDLTDDERKS---LRKEIGYVFQDPQ--LF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 377 PRLSVLQIIEEGLRVhqPGLSAQQREQEVMRVMAEVGL--DAGTR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:pfam00005 72 PRLTVRENLRLGLLL--KGLSKREKDARAEEALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 658548496 454 S 454
Cdd:pfam00005 150 A 150
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
7.44e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.12 E-value: 7.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSL 78
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKS----TLLRCLnglvePT------SGEILVDGQDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHADEHTLRGIRGnKIAMIFQEpmvslnplHSLEKQLYeVL-----------SLHRGMRKEAARGEI---LDCLERTGIr 144
Cdd:COG3638 68 TALRGRALRRLRR-RIGMIFQQ--------FNLVPRLS-VLtnvlagrlgrtSTWRSLLGLFPPEDReraLEALERVGL- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 145 naAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLA 224
Cdd:COG3638 137 --ADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYA 214
|
250
....*....|..
gi 658548496 225 DNVAVMQNGRCV 236
Cdd:COG3638 215 DRIIGLRDGRVV 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
301-517 |
8.76e-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: 141.70 E-value: 8.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEIFFD-----DMPlhrwnrrqmlPVRPRMQVVFQd 370
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSV----LLETIAGfikpdSGKILLNgkditNLP----------PEKRDISYVPQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 pNSSLNPRLSVLQIIEEGLRVHQpgLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03299 79 -NYALFPHMTVYKNIAYGLKKRK--VDKKEIERKVLEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
294-528 |
1.50e-38 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 141.38 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 294 RIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-----ASQGEIFFDDMPLHRWNrrqmlpVRPRM-QVV 367
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAPCA------LRGRKiATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 368 FQDPNSSLNPRLSVLQIIEEGLRVhqpgLSAQQREQEVMRVMAEVGLDAGTR--HRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:PRK10418 85 MQNPRSAFNPLHTMHTHARETCLA----LGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 446 LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQL 525
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
...
gi 658548496 526 LSA 528
Cdd:PRK10418 241 VSA 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-237 |
1.57e-38 |
|
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: 139.96 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:cd03259 1 LELKGLSKTY---GSVR-ALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIaglerPD------SGEILIDGRDVTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHtlrgiRGNkIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGG 160
Cdd:cd03259 67 VPPE-----RRN-IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
276-504 |
1.86e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 138.68 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03230 1 IEVRNLSKRYG-----------KKTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIILgllkpDSGEIKVLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRqmlpVRPRMQVVFQDPnsSLNPRLSVLQIIEeglrvhqpglsaqqreqevmrvmaevgldagtrhrypaeFSGGQ 430
Cdd:cd03230 66 KEPEE----VKRRIGYLPEEP--SLYENLTVRENLK---------------------------------------LSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
304-517 |
2.42e-38 |
|
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: 143.70 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 304 NIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPV-RPRMQVVFQDPnsSLNP 377
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTT----LLRAIAglerpDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQEA--RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 378 RLSVLQIIEEGLRVHQPGLSAQQREQevmrVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDE----VVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-237 |
3.70e-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: 139.62 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVsalsILRLL-------PSPPVSypqGDILFHGSSL 78
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKST----LLRLLnrlndliPGAPDE---GEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHADEHTLRGIRgnKIAMIFQEPmvslNPLHsleKQLYEVLSL---HRGMRKEAARGEI-LDCLERTGI-RNAAKRLNdf 153
Cdd:cd03260 70 YDLDVDVLELRR--RVGMVFQKP----NPFP---GSIYDNVAYglrLHGIKLKEELDERvEEALRKAALwDEVKDRLH-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:cd03260 139 ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNG 216
|
....
gi 658548496 234 RCVE 237
Cdd:cd03260 217 RLVE 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
274-528 |
5.86e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 141.97 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPIRKGILRrIVDqnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIFFDDMplhRWN 353
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVK-AVD------RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRF---RWN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQMLPVRPR---------MQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGLS----AQQREQEVMRVMAEVGLdagTRH 420
Cdd:COG4170 72 GIDLLKLSPRerrkiigreIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrFKWRKKRAIELLHRVGI---KDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 421 R-----YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQ 495
Cdd:COG4170 149 KdimnsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADT 228
|
250 260 270
....*....|....*....|....*....|...
gi 658548496 496 VIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:COG4170 229 ITVLYCGQTVESGPTEQILKSPHHPYTKALLRS 261
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-518 |
9.94e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.48 E-value: 9.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPL 349
Cdd:COG4559 1 MLEAENLSVR-----------LGGRTLLDDVSLTLRPGELTAIIGPNGAGKST----LLKLLTgeltpSSGEVRLNGRPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNRRQMLPVRPRMQvvfQdpNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGG 429
Cdd:COG4559 66 AAWSPWELARRRAVLP---Q--HSSLAFPFTVEEVVALGRAPH--GSSAAQDRQIVREALALVGL-AHLAGRSYQTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALI-------LKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQG 216
|
250
....*....|....*.
gi 658548496 503 EVVEQGECQRVFSAPT 518
Cdd:COG4559 217 RLVAQGTPEEVLTDEL 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-235 |
1.27e-37 |
|
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: 137.99 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLlhade 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIIAglERPTS---GEVLVDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 htlRGiRGNKIAMIFQEPmvSLNPLHSLEKQLyeVLSL-HRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGER 162
Cdd:cd03293 69 ---TG-PGPDRGYVFQQD--ALLPWLTVLDNV--ALGLeLQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRC 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 |
1.44e-37 |
|
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: 137.87 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLHADEH 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPT----SGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIRGNKIAMIFQ--EPMVSLNPLHSLEKQLyevlsLHRGMRKEAARGEILDCLERTGIRnaaKRLNDFPHQLSGGER 162
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKSVKEAKERAYEMLEKVGLE---HRINHRPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLaDNVAVMQNGRCVE 237
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-509 |
2.76e-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: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA----------SQGEIFFD 345
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKST----LLRLLNrlndlipgapDEGEVLLD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNRRQMLpVRPRMQVVFQDPNsslnP-RLSVLQIIEEGLRVHQPgLSAQQREQEVMRVMAEVGL-DAGTRHRYP 423
Cdd:cd03260 66 GKDIYDLDVDVLE-LRRRVGMVFQKPN----PfPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALwDEVKDRLHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
....*.
gi 658548496 504 VVEQGE 509
Cdd:cd03260 218 LVEFGP 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-234 |
2.90e-37 |
|
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: 135.20 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsYPQGDILFHGSSLLHADEHT 85
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-----PTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRgirgNKIAMIFQEPmvslnplhslekQLYEvlslhrgmrkeaarGEILDCLertgirnaakrlndfphqLSGGERQRV 165
Cdd:cd03228 74 LR----KNIAYVPQDP------------FLFS--------------GTIRENI------------------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGR 234
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
301-527 |
3.04e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.96 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI----------ASQGEIFFD-DMPLhrwNRRQMLPVRPRMQVVFQ 369
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTT----LLRCInlleqpeagtIRVGDITIDtARSL---SQQKGLIRQLRQHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 370 DPNSSLNPRLSVLQIIEEGLRV--HQPGLSAQQREQEVMrvmAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGPVIvkGEPKEEATARARELL---AKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIfISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
276-515 |
3.32e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 138.33 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIrkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDDMplH 350
Cdd:TIGR04520 1 IEVENVSFSYPE---------SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTlakllNGL----LLPTSGKVTVDGL--D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPRMQVVFQDPNSSLnprlsVLQIIEE----GLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEF 426
Cdd:TIGR04520 66 TLDEENLWEIRKKVGMVFQNPDNQF-----VGATVEDdvafGLENL--GVPREEMRKRVDEALKLVGME-DFRDREPHLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVE 506
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVA 216
|
....*....
gi 658548496 507 QGECQRVFS 515
Cdd:TIGR04520 217 EGTPREIFS 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-508 |
8.70e-37 |
|
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: 136.03 E-value: 8.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDD---- 346
Cdd:cd03219 1 LEVRGLTKRF----GGLV-------ALDDVSFSVRPGEIHGLIGPNGAGKTT----LFNLIsgflrPTSGSVLFDGedit 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 -MPLHRWNRRQMlpVRprmqvVFQdpNSSLNPRLSVLQIIEEGLRVHQPGLSAQQR--------EQEVMRVMAEVGLdAG 417
Cdd:cd03219 66 gLPPHEIARLGI--GR-----TFQ--IPRLFPELTVLENVMVAAQARTGSGLLLARarreereaRERAEELLERVGL-AD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:cd03219 136 LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVT 214
|
250
....*....|.
gi 658548496 498 VLRQGEVVEQG 508
Cdd:cd03219 215 VLDQGRVIAEG 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-244 |
1.02e-36 |
|
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: 136.27 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLLHADEH 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-----VEPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIRgNKIAMIFQEPMVsLNPLHSLEKQLYEVLSLHRGMR------KEAARGEILDCLERTGIRN-AAKRLNdfphQL 157
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQHYNL-IERLTVLENVLHGRLGYKPTWRsllgrfSEEDKERALSALERVGLADkAYQRAD----QL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
....*..
gi 658548496 238 QNTASTL 244
Cdd:TIGR02315 227 DGAPSEL 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-252 |
1.14e-36 |
|
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: 144.59 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRNAAKRLndfPH----- 155
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFL-------FSGTIRENITLGD---PDATDEEIIEAARLAGLHDFIEAL---PMgydtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRkLADNVAV 229
Cdd:COG2274 605 vgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIV 681
|
250 260
....*....|....*....|...
gi 658548496 230 MQNGRCVEQNTASTLLSAPQHPY 252
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYA 704
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
274-528 |
1.24e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.44 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMP 348
Cdd:PRK13548 1 AMLEARNLSVR-----------LGGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelsPDSGEVRLNGRP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRWNRRQMLPVRPRM-QvvfqdpNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFS 427
Cdd:PRK13548 66 LADWSPAELARRRAVLpQ------HSSLSFPFTVEEVVAMGRAPH--GLSRAEDDALVAAALAQVDL-AHLAGRDYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALI------LKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250 260
....*....|....*....|....*..
gi 658548496 502 GEVVEQGecqrvfsAPTQRYTRQLLSA 528
Cdd:PRK13548 217 GRLVADG-------TPAEVLTPETLRR 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
304-508 |
6.31e-36 |
|
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: 133.19 E-value: 6.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 304 NIRFSLrPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPVRPR-MQVVFQdpNSSLNP 377
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKST----LLRCIAglekpDGGTIVLNGTVLFDSRKKINLPPQQRkIGLVFQ--QYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 378 RLSVLQIIEEGLRVHQPGlSAQQREQEVMRVMaevGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:cd03297 89 HLNVRENLAFGLKRKRNR-EDRISVDELLDLL---GLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658548496 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-505 |
6.66e-36 |
|
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: 131.40 E-value: 6.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03216 1 LELRGITKRFG-----------GVKALDGVSLSVRRGEVHALLGENGAGKST----LMKILSglykpDSGEILVDGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLpvRPRMQVVFQdpnsslnprlsvlqiieeglrvhqpglsaqqreqevmrvmaevgldagtrhrypaeFSGGQ 430
Cdd:cd03216 66 FASPRDAR--RAGIAMVYQ--------------------------------------------------------LSVGE 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:cd03216 88 RQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-504 |
6.80e-36 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 140.06 E-value: 6.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSYpQGDILFHGSsL 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGV----KALDNVSLKVRAGEIVSLCGENGAGKS----TLMKVLSGvyPHGTY-EGEIIFEGE-E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHAdeHTLRGIRGNKIAMIFQEPMvslnplhsLEKQLYEVLSLHRGmrKEAARGEILD----------CLERTGIR-NAA 147
Cdd:PRK13549 71 LQA--SNIRDTERAGIAIIHQELA--------LVKELSVLENIFLG--NEITPGGIMDydamylraqkLLAQLKLDiNPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 148 KRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNV 227
Cdd:PRK13549 139 TPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 228 AVMQNGRCVEQNTASTlLSAPQ-------------HPYTQRlldsePSGDPVplaadstplLRVEDLSVSFPIRKGilRR 294
Cdd:PRK13549 214 CVIRDGRHIGTRPAAG-MTEDDiitmmvgreltalYPREPH-----TIGEVI---------LEVRNLTAWDPVNPH--IK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 295 IVDqnpvlkNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI--ASQGEIFFDDMPLHRWNRRQ-------MLP------ 359
Cdd:PRK13549 277 RVD------DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpgRWEGEIFIDGKPVKIRNPQQaiaqgiaMVPedrkrd 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 360 -VRPRMQVvfqdpnsSLNPRLSVLQIIEEGLRvhqpgLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIAR 438
Cdd:PRK13549 351 gIVPVMGV-------GKNITLAALDRFTGGSR-----IDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAK 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 439 ALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
300-529 |
6.81e-36 |
|
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: 133.97 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWNRRQMlpvRPRMQVVFQdpNSSLNPR 378
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVEL---RRKIGYVIQ--QIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LSVLQIIeeGLRVHQPGLSAQQREQEVMRVMAEVGLD-AGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:cd03295 90 MTVEENI--ALVPKLLKWPKEKIRERADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 458 RTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSAD 529
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-236 |
1.15e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.08 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHT 85
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE--PTS---GSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGnKIAMIFQEP------MVSLNPLHSL--EKQLYEVLSlhrGMRKEAARGEILDCLERTGIRNAAKRLNDfphQL 157
Cdd:cd03256 73 LRQLRR-QIGMIFQQFnlierlSVLENVLSGRlgRRSTWRSLF---GLFPKEEKQRALAALERVGLLDKAYQRAD---QL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
1.33e-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: 131.02 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTL 86
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 87 RgirgNKIAMIFQepmvslnplhslekqlyevlslhrgmrkeaargeildCLERTGIRNAAKRlnDFpHQLSGGERQRVM 166
Cdd:cd03214 72 A----RKIAYVPQ-------------------------------------ALELLGLAHLADR--PF-NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
1.90e-35 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 130.21 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKT----TLIKIIlgllkPD------SGEIKVLGKDIKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRgirgnKIAMIFQEPMvslnplhslekqLYEVLSLHrgmrkeaargEILDclertgirnaakrlndfphqLSGG 160
Cdd:cd03230 67 EPEEVKR-----RIGYLPEEPS------------LYENLTVR----------ENLK--------------------LSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-237 |
1.91e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIafsTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:COG2884 2 IRFENVSK---RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLygeerPT------SGQVLVNGQDLSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRgNKIAMIFQEpmvslnplHSL--EKQLYE--VLSLH-RGMRKEAARGEILDCLERTGIRNAAKRlndFPH 155
Cdd:COG2884 69 LKRREIPYLR-RRIGVVFQD--------FRLlpDRTVYEnvALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKA---LPH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRC 235
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
..
gi 658548496 236 VE 237
Cdd:COG2884 216 VR 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-246 |
2.86e-35 |
|
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: 132.94 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSA--LSILrLLPSppvsypQGDILFHGSSLLhaDE 83
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAklLNGL-LLPT------SGKVTVDGLDTL--DE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRgNKIAMIFQepmvslNPlhslEKQLyeVLSL----------HRGMRKEAARGEILDCLERTGIRNAAKRLndf 153
Cdd:TIGR04520 70 ENLWEIR-KKVGMVFQ------NP----DNQF--VGATveddvafgleNLGVPREEMRKRVDEALKLVGMEDFRDRE--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRkLADNVAVMQNG 233
Cdd:TIGR04520 134 PHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKG 212
|
250
....*....|...
gi 658548496 234 RCVEQNTASTLLS 246
Cdd:TIGR04520 213 KIVAEGTPREIFS 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
302-514 |
2.89e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.63 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDDMPLhrWNRRQMLP-VRPRMQVVFQDPNSSL 375
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTliqhlNGL----LKPTSGKIIIDGVDI--TDKKVKLSdIRKKVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRlSVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAGT-RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK13637 97 FEE-TIEKDIAFGPI--NLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
272-513 |
3.08e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.84 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFPirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDD 346
Cdd:COG1129 1 AEPLLEMRGISKSFG-----------GVKALDGVSLELRPGEVHALLGENGAGKST----LMKILSgvyqpDSGEILLDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNRRQMLpvRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHQPGL-SAQQREQEVMRVMAEVGL--DAGTRHRyp 423
Cdd:COG1129 66 EPVRFRSPRDAQ--AAGIAIIHQELN--LVPNLSVAENIFLGREPRRGGLiDWRAMRRRARELLARLGLdiDPDTPVG-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 424 aEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:COG1129 140 -DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVLRDGR 217
|
250
....*....|
gi 658548496 504 VVEQGECQRV 513
Cdd:COG1129 218 LVGTGPVAEL 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
3.63e-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: 128.92 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 25 VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpsppvSYPQGDILFHGSSLLHADEHTLRGirgnKIAMIFQEPmvS 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-----SPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 105 LNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKR-LNDFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 658548496 184 TT 185
Cdd:pfam00005 149 TA 150
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-257 |
4.02e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.42 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 29 SLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHGSSLLHADEHtLRgirgnKIAMIFQEpmvslN 106
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIAGflPPDS---GRILWNGQDLTALPPA-ER-----PVSMLFQE-----N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PL--H-SLEKQLYevLSLHRGMR-KEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:COG3840 81 NLfpHlTVAQNIG--LGLRPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 183 PTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQRLL 257
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-258 |
5.58e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 138.36 E-value: 5.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsYPQGDILFHGSSLLHA 81
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRgirgNKIAMIFQEPmvslnplHSLEKQLYEVLSLHRGmrkEAARGEILDCLERTGIrnaAKRLNDFPH------ 155
Cdd:COG4987 403 DEDDLR----RRIAVVPQRP-------HLFDTTLRENLRLARP---DATDEELWAALERVGL---GDWLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVM 230
Cdd:COG4987 466 geggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVL 542
|
250 260
....*....|....*....|....*...
gi 658548496 231 QNGRCVEQNTASTLLSapQHPYTQRLLD 258
Cdd:COG4987 543 EDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
274-501 |
6.01e-35 |
|
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: 130.29 E-value: 6.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMP 348
Cdd:COG4133 1 MMLEAENLSCRR-----------GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILAgllppSAGEVLWNGEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRwnrrqmLPVRPRMQVVFQDPNSSLNPRLSVLqiieEGLRVHQPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSG 428
Cdd:COG4133 66 IRD------AREDYRRRLAYLGHADGLKPELTVR----ENLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLqvVRALCHQVIVLRQ 501
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQP--LELAAARVLDLGD 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
298-525 |
6.16e-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: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRL-----IASQGEI-----FFD--DMPlhrwNRRQMLPVRPRMQ 365
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSS----LLRVlnlleTPDSGQLniaghQFDfsQKP----SEKAIRLLRQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 366 VVFQDPNssLNPRLSVLQ-IIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:COG4161 86 MVFQQYN--LWPHLTVMEnLIEAPCKVL--GLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 445 ELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQrVFSAP-TQRYTR 523
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPqTEAFAH 238
|
..
gi 658548496 524 QL 525
Cdd:COG4161 239 YL 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
292-527 |
1.06e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.24 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFD----------DMPLHRWNRRQ 356
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCInflekPSEGSIVVNgqtinlvrdkDGQLKVADKNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 MLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGlRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAI 436
Cdd:PRK10619 87 LRLLRTRLTMVFQHFN--LWSHMTVLENVMEA-PIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 437 ARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|.
gi 658548496 517 PTQRYTRQLLS 527
Cdd:PRK10619 243 PQSPRLQQFLK 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
277-505 |
1.74e-34 |
|
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: 128.91 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNRR 355
Cdd:cd03226 1 RIENISFSYK----------KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 356 QMlpvrprMQVVFQDPNSSLNpRLSVlqiiEEGLRVHQPGLSA-QQREQEVMRVMAEVGLdagtRHRYPAEFSGGQRQRI 434
Cdd:cd03226 71 KS------IGYVMQDVDYQLF-TDSV----REELLLGLKELDAgNEQAETVLKDLDLYAL----KERHPLSLSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 435 AIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
2.35e-34 |
|
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: 128.80 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILR---LLPSPPvsypQGDILFHGSSLLHAD 82
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRcinLLEEPD----SGTIIIDGLKLTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHtLRGIRgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGER 162
Cdd:cd03262 69 KN-INELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-249 |
2.36e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.75 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSL---LHADEHTLRGIRgNKIAMIFQEpmV 103
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPR----SGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQ--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 SLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK11124 92 NLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 184 TTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTlLSAPQ 249
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
299-527 |
2.77e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.36 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRL-----IASQGEI-----FFDDMplHRWNRRQMLPVRPRMQVVF 368
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSS----LLRVlnlleMPRSGTLniagnHFDFS--KTPSDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 QDPNssLNPRLSVLQ-IIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11124 89 QQYN--LWPHLTVQQnLIEAPCRVL--GLSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRvFSAPTQRYTRQLLS 527
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYLS 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
277-503 |
3.08e-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: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFPirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHR 351
Cdd:cd00267 1 EIENLSFRYG-----------GRTALDNVSLTLKAGEIVALVGPNGSGKST----LLRAIAgllkpTSGEILIDGKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQmlpVRPRMQVVFQdpnsslnprlsvlqiieeglrvhqpglsaqqreqevmrvmaevgldagtrhrypaeFSGGQR 431
Cdd:cd00267 66 LPLEE---LRRRIGYVPQ--------------------------------------------------------LSGGQR 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd00267 87 QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
273-502 |
3.40e-34 |
|
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: 128.71 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPI--RKGIlrRIvdqnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFD 345
Cdd:COG4778 2 TTLLEVENLSKTFTLhlQGGK--RL----PVLDGVSFSVAAGECVALTGPSGAGKST----LLKCIygnylPDSGSILVR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 D----MPLHRWNRRQMLPVRPR--------MQVVfqdpnsslnPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVG 413
Cdd:COG4778 72 HdggwVDLAQASPREILALRRRtigyvsqfLRVI---------PRVSALDVVAEPLLER--GVDREEARARARELLARLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 414 LDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHR-LAYIFISHDLQVVRAL 492
Cdd:COG4778 141 LPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA--KARgTAIIGIFHDEEVREAV 218
|
250
....*....|
gi 658548496 493 CHQVIVLRQG 502
Cdd:COG4778 219 ADRVVDVTPF 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-255 |
3.43e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 129.36 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSL---LHADEHTLRGIRGnKIAMIFQE 100
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPD----SGQLNIAGHQFdfsQKPSEKAIRLLRQ-KVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 pmVSLNPLHSLEKQLYE----VLslhrGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPE 176
Cdd:COG4161 91 --YNLWPHLTVMENLIEapckVL----GLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 177 LLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLlsapQHPYTQR 255
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTEA 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-258 |
5.21e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.67 E-value: 5.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 19 GETrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPVsYPQGDILFHGSSLL--HADEHTLRGIRGnkiaM 96
Cdd:PRK09493 12 GPT-QVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEE-ITSGDLIVDGLKVNdpKVDERLIRQEAG----M 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 97 IFQEpmVSLNP-LHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:PRK09493 82 VFQQ--FYLFPhLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 176 ELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSapqHPYTQR 255
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK---NPPSQR 231
|
...
gi 658548496 256 LLD 258
Cdd:PRK09493 232 LQE 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-258 |
6.65e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 128.71 E-value: 6.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPVSYPQ-GDILFHGSSLLHADEHTL 86
Cdd:PRK11264 6 VKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAGTIRvGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 87 RGIRgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVM 166
Cdd:PRK11264 81 RQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
250
....*....|..
gi 658548496 247 APQHPYTQRLLD 258
Cdd:PRK11264 234 DPQQPRTRQFLE 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-252 |
8.66e-34 |
|
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: 128.92 E-value: 8.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 25 VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHTLRGIRGNKIAMIFQE--PM 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--PTS---GKVLIDGQDIAAMSRKELRELRRKKISMVFQSfaLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 VSLNPLHSLEKQLyEVLSLHRGMRKEAARgeilDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:cd03294 115 PHRTVLENVAFGL-EVQGVPRAEREERAA----EALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 183 PTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPY 252
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-248 |
9.55e-34 |
|
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: 130.99 E-value: 9.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRL---LPSPPvsypQGDILFHGSSLLHADEHTLRGIRGNKIAMIFQEPmv 103
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKT----TLLRAiagLERPD----SGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 SLNPlHslekqlYEVLS-LHRGMR---KEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:COG4148 87 RLFP-H------LSVRGnLLYGRKrapRAERRISFDEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 180 ADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAP 248
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-247 |
1.07e-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: 134.50 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFstqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsyP-QGDILFHGSSLLH 80
Cdd:COG4988 333 GPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP------PySGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRNAAKRLN---DFP--- 154
Cdd:COG4988 404 LDPASWR----RQIAWVPQNPYL-------FAGTIRENLRLGR---PDASDEELEAALEAAGLDEFVAALPdglDTPlge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 --HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELnmSLLFITHNLSIVRkLADNVAVMQN 232
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLA-QADRILVLDD 546
|
250
....*....|....*
gi 658548496 233 GRCVEQNTASTLLSA 247
Cdd:COG4988 547 GRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
274-519 |
1.51e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLhrw 352
Cdd:PRK13635 4 EIIRVEHISFRYP---------DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 353 NRRQMLPVRPRMQVVFQDPNSSLnprlsVLQIIEEGLRVhqpGLSAQQ--REQEVMRV---MAEVGLDAGTrHRYPAEFS 427
Cdd:PRK13635 72 SEETVWDVRRQVGMVFQNPDNQF-----VGATVQDDVAF---GLENIGvpREEMVERVdqaLRQVGMEDFL-NREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQ 507
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEE 221
|
250
....*....|..
gi 658548496 508 GECQRVFSAPTQ 519
Cdd:PRK13635 222 GTPEEIFKSGHM 233
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
301-506 |
1.54e-33 |
|
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: 126.70 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPVRPR-MQVVFQdpNSS 374
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKST----LLHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIYQ--FHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQiieeglRVHQPGL----SAQQREQEVMRVMAEVGLDAGTRHRyPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:TIGR02211 94 LLPDFTALE------NVAMPLLigkkSVKEAKERAYEMLEKVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALcHQVIVLRQGEVVE 506
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
297-508 |
1.91e-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: 126.22 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEIFFDDmplhrwNRRQMLPVRPR-MQVVFQd 370
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGG------RDVTDLPPKDRdIAMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 pNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:cd03301 80 -NYALYPHMTVYDNIAFGLKLR--KVPKDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-257 |
2.53e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.88 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSL-- 78
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNGRDLft 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 -LHADEhtlrgiRgnKIAMIFQEPM------VSLNPLHSLEkqlyevlslHRGMRKEAARGEILDCLERTGIRNAAKRln 151
Cdd:COG1118 69 nLPPRE------R--RVGFVFQHYAlfphmtVAENIAFGLR---------VRPPSKAEIRARVEELLELVQLEGLADR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 dFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQ 231
Cdd:COG1118 130 -YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
250 260
....*....|....*....|....*.
gi 658548496 232 NGRCVEQNTASTLLSAPQHPYTQRLL 257
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-234 |
2.70e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVsalsILRLLPS--PPVSypqGDILFHGSSLLHADE 83
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKST----LLRALADldPPTS---GEIYLDGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGirgnKIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAARGE-ILDCLERTGIRNAAkrLNDFPHQLSGGER 162
Cdd:COG4619 70 PEWRR----QVAYVPQEPAL-------WGGTVRDNLPFPFQLRERKFDRErALELLERLGLPPDI--LDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-504 |
2.91e-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: 132.64 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 23 TVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSYpQGDILFHGSSLlhadehTLRGIRGNK---IAMI 97
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKS----TLMKILSGvyPHGTW-DGEIYWSGSPL------KASNIRDTEragIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 98 FQEPMVSLNpLHSLEKQLYEVLSLHRGMRKEAA----RGEILDCLERTGIRNAAKRLNDfphqLSGGERQRVMIAMALLT 173
Cdd:TIGR02633 84 HQELTLVPE-LSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGD----YGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 174 RPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTlLSAPQ---- 249
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMST-MSEDDiitm 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 250 --HPYTQRLLDSEPS--GDPVplaadstplLRVEDLSVSFPIRKGILRriVDqnpvlkNIRFSLRPGESLGLVGESGSGK 325
Cdd:TIGR02633 237 mvGREITSLYPHEPHeiGDVI---------LEARNLTCWDVINPHRKR--VD------DVSFSLRRGEILGVAGLVGAGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 326 STTGLALLRLIASQ--GEIFFDDMPLHRWNRRQ-------MLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVhqpgl 396
Cdd:TIGR02633 300 TELVQALFGAYPGKfeGNVFINGKPVDIRNPAQairagiaMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRI----- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 397 SAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHr 476
Cdd:TIGR02633 375 DAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG- 453
|
490 500
....*....|....*....|....*...
gi 658548496 477 LAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:TIGR02633 454 VAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
3.68e-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: 124.22 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLlhADEHT 85
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDL--TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGNKIAMIFQEPmvslnplhslekQLYEVLSlhrgmrkeaargeILDclertgirNAAkrlndfpHQLSGGERQRV 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDF------------ALFPHLT-------------VLE--------NIA-------LGLSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
5.66e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.30 E-value: 5.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILR-------LLPSPPVSypqGDILFH 74
Cdd:COG1117 8 LEPKIEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKS----TLLRclnrmndLIPGARVE---GEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 75 GSSLLHA--DEHTLRgiRgnKIAMIFQEPmvslNPL-HSLekqlYE-V---LSLHrGMRKEAARGEIL-DCLERTGIRNA 146
Cdd:COG1117 77 GEDIYDPdvDVVELR--R--RVGMVFQKP----NPFpKSI----YDnVaygLRLH-GIKSKSELDEIVeESLRKAALWDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 147 AK-RLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVRKLAD 225
Cdd:COG1117 144 VKdRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSD 221
|
250 260
....*....|....*....|....*....
gi 658548496 226 NVAVMQNGRCVEQNTASTLLSAPQHPYTQ 254
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-230 |
5.98e-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: 5.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsyP-QGDILFHGSSLlhadeht 85
Cdd:cd03235 1 EVEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK------PtSGSIRVFGKPL------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 lrGIRGNKIAMIFQEPMVSLN-PLHSLE---KQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAAKRLNDfphQLSGGE 161
Cdd:cd03235 64 --EKERKRIGYVPQRRSIDRDfPISVRDvvlMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIG---ELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVM 230
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
292-518 |
6.42e-33 |
|
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: 125.53 E-value: 6.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmLPVRPRmQV 366
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTT----LLRLIAglerpDSGTILFGGEDATD------VPVQER-NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 367 --VFQdpNSSLNPRLSVLQIIEEGLRVH--QPGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQRQRIAIARALIL 442
Cdd:cd03296 77 gfVFQ--HYALFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 443 KPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-260 |
7.95e-33 |
|
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: 125.49 E-value: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLL-PSppvsypQGDILFHGSSLLHADEH 84
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT------SGEIFIDGEDIREQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRgirgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIrNAAKRLNDFPHQLSGGERQR 164
Cdd:cd03295 72 ELR----RKIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTL 244
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 658548496 245 LSAPQHPYTQRLLDSE 260
Cdd:cd03295 224 LRSPANDFVAEFVGAD 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
298-520 |
8.04e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 125.59 E-value: 8.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLhRWNRRQMLPVRPRMQVVFQDPN 372
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCInkleeITSGDLIVDGLKV-NDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 ssLNPRLSVLQIIEEGlRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHrYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK09493 88 --LFPHLTALENVMFG-PLRVRGASKEEAEKQARELLAKVGLAERAHH-YPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 453 TSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSA-PTQR 520
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNpPSQR 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-240 |
9.32e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 9.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLlh 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL--PEA---GTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 aDEHTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLndf 153
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPdnqfvgaTVQDDVAFGLENI---------GVPREEMVERVDQALRQVGMEDFLNRE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKlADNVAVMQNG 233
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
....*..
gi 658548496 234 RCVEQNT 240
Cdd:PRK13635 217 EILEEGT 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-517 |
9.44e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 126.35 E-value: 9.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLhRWN 353
Cdd:PRK13639 1 ILETRDLKYSYP----------DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPI-KYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQMLPVRPRMQVVFQDPNSSL-NPRlsVLQIIEEGlrvhqP---GLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGG 429
Cdd:PRK13639 70 KKSLLEVRKTVGIVFQNPDDQLfAPT--VEEDVAFG-----PlnlGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
....*...
gi 658548496 510 CQRVFSAP 517
Cdd:PRK13639 221 PKEVFSDI 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-234 |
1.03e-32 |
|
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: 122.35 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTL 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 87 RgirgNKIAMIFQepmvslnplhslekqlyevlslhrgmrkeaargeildclertgirnaakrlndfphqLSGGERQRVM 166
Cdd:cd00267 72 R----RRIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
301-528 |
1.44e-32 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 124.53 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmLPVRPR-MQVVFQdpNSS 374
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKST----LLRIIAgleqpDSGRIRLNGQDATR------VHARDRkIGFVFQ--HYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQIIEEGLRVHQPglSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKH--PKAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGE 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-249 |
1.67e-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: 124.37 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFStqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGssllhADEHT 85
Cdd:cd03299 1 LKVENLSKDWK-----EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDS---GKILLNG-----KDITN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGNkIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAakrLNDFPHQLSGGERQRV 165
Cdd:cd03299 66 LPPEKRD-ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGIDHL---LNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLL 245
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
....
gi 658548496 246 SAPQ 249
Cdd:cd03299 219 KKPK 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-238 |
2.01e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.06 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 19 GETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHGSSLLHADEHTLRgirgNKIAM 96
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRfyDPTS---GRILIDGVDIRDLTLESLR----RQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 97 IFQEPMVslnplhsLEKQLYEVLSLhrGmRKEAARGEILDCLERTgirNAAKRLNDFPHQ-----------LSGGERQRV 165
Cdd:COG1132 419 VPQDTFL-------FSGTIRENIRY--G-RPDATDEEVEEAAKAA---QAHEFIEALPDGydtvvgergvnLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQ 238
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
298-508 |
6.56e-32 |
|
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: 122.72 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDP---NS 373
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKS---LRSMIGVVLQDTflfSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 374 SlnprlsvlqiIEEGLRVHQPGlsaqQREQEVMRVMAEVGLDAGTRHR------YPAE----FSGGQRQRIAIARALILK 443
Cdd:cd03254 92 T----------IMENIRLGRPN----ATDEEVIEAAKEAGAHDFIMKLpngydtVLGEnggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 444 PELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03254 158 PKILILDEATSNIDteteKLIQEALEKLMKG-----RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
276-491 |
9.24e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.43 E-value: 9.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVsfpirkgilrrIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA--------SQGEIFFDDM 347
Cdd:COG4136 2 LSLENLTI-----------TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKST----LLAAIAgtlspafsASGEVLLNGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRwnrrqmLPVRPR-MQVVFQDPnsSLNPRLSVLQIIEEGLRvhqPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEF 426
Cdd:COG4136 67 RLTA------LPAEQRrIGILFQDD--LLFPHLSVGENLAFALP---PTIGRAQRRARVEQALEEAGL-AGFADRDPATL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
1.23e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 127.98 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLH 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV----HALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPT----KGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADeHTLRGIRGnkIAMIFQEPMVsLNPLhSLEKQLY-------EVLSL----HRGMRKEAArgEILDcleRTGIRnaaKR 149
Cdd:PRK09700 72 LD-HKLAAQLG--IGIIYQELSV-IDEL-TVLENLYigrhltkKVCGVniidWREMRVRAA--MMLL---RVGLK---VD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 150 LNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAV 229
Cdd:PRK09700 139 LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 230 MQNGRCVeqntASTLLSAPQHPYTQRLLDSEPSGDPVPLAADSTpllRVEDLSVSFPIRKgILRRivDQNPVlKNIRFSL 309
Cdd:PRK09700 218 MKDGSSV----CSGMVSDVSNDDIVRLMVGRELQNRFNAMKENV---SNLAHETVFEVRN-VTSR--DRKKV-RDISFSV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 310 RPGESLGLVGESGSGKSTTGLALLRL--IASqGEIFFDDMPLHrwNRRQMLPVRPRMQVVFQD-------PNSSLNPRLS 380
Cdd:PRK09700 287 CRGEILGFAGLVGSGRTELMNCLFGVdkRAG-GEIRLNGKDIS--PRSPLDAVKKGMAYITESrrdngffPNFSIAQNMA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 381 VLQIIEEGLRVHQPGLSAQQREQEVMRVMAE-VGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:PRK09700 364 ISRSLKDGGYKGAMGLFHEVDEQRTAENQRElLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 658548496 460 VQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK09700 444 AKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
300-504 |
1.23e-31 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 121.36 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDpnSS 374
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKST----LLKLIYkeelpTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQIIEEGLRVHQ-PGLSAQQReqeVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:cd03292 89 LLPDRNVYENVAFALEVTGvPPREIRKR---VPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658548496 454 SSLDRTVQAQILALLKGLQEkhRLAYIFIS-HDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINK--AGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-246 |
1.53e-31 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 121.89 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLL 79
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKT----TLLRMLagllkPD------SGSILIDGEDVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRgirgnKIAMIFQEPMVSLNplHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIRNAAKRLNdfpHQLSG 159
Cdd:COG4555 67 KEPREARR-----QIGVLPDERGLYDR--LTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRV---GELST 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQN 239
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
....*..
gi 658548496 240 TASTLLS 246
Cdd:COG4555 215 SLDELRE 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
275-515 |
1.58e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.03 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHrWN 353
Cdd:PRK13636 5 ILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPID-YS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQMLPVRPRMQVVFQDPNSSLNPRlSVLQIIEEGlrVHQPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQR 433
Cdd:PRK13636 74 RKGLMKLRESVGMVFQDPDNQLFSA-SVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
..
gi 658548496 514 FS 515
Cdd:PRK13636 230 FA 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
278-518 |
1.65e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.99 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 278 VEDLSVSFPIRKgilrrivdqNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLaLLRLIASQGEIFFDDMPLhrw 352
Cdd:PRK13640 8 FKHVSFTYPDSK---------KPALNDISFSIPRGSWTALIGHNGSGKSTiskliNGL-LLPDDNPNSKITVDGITL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 353 NRRQMLPVRPRMQVVFQDPNSSLnprlsVLQIIEE----GLRvhQPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSG 428
Cdd:PRK13640 75 TAKTVWDIREKVGIVFQNPDNQF-----VGATVGDdvafGLE--NRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
250
....*....|
gi 658548496 509 ECQRVFSAPT 518
Cdd:PRK13640 226 SPVEIFSKVE 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-227 |
2.32e-31 |
|
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: 120.41 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSppvsYPQGDILFHGSSLLHADEHTLR 87
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEK----FDSGQVYLNGQETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 88 GIRGNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAaRGEILDCLERTGIRNaakRLNDFPHQLSGGERQRVMI 167
Cdd:TIGR03608 72 KFRREKLGYLFQN--FALIENETVEENLDLGLKYKKLSKKEK-REKKKEALEKVGLNL---KLKQKIYELSGGEQQRVAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 168 AMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKlADNV 227
Cdd:TIGR03608 146 ARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRV 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-234 |
2.35e-31 |
|
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: 120.48 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQ---PGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHGSSLLHADEHTLRGIRGNKIAMIFQEpmV 103
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKS-TLLRCIAGLEKPDG----GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 SLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaakrLNDFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHL------LNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658548496 184 TTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
269-522 |
3.54e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIF 343
Cdd:PRK09452 8 PSSLSPLVELRGISKSF-----------DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 344 FDDMPLHRwnrrqmLPVRPR-MQVVFQdpNSSLNPRLSVLQIIEEGLRVHQpgLSAQQREQEVMRVMAEVGLDAGTRHRy 422
Cdd:PRK09452 73 LDGQDITH------VPAENRhVNTVFQ--SYALFPHMTVFENVAFGLRMQK--TPAAEITPRVMEALRMVQLEEFAQRK- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
250 260
....*....|....*....|
gi 658548496 503 EVVEQGECQRVFSAPTQRYT 522
Cdd:PRK09452 222 RIEQDGTPREIYEEPKNLFV 241
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-507 |
4.69e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.12 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPIRKGilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMP 348
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTT----LLNLIAgflapSSGEITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRwnrrqmlPVRPRmQVVFQDpnSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSG 428
Cdd:COG4525 71 VTG-------PGADR-GVVFQK--DALLPWLNVLDNVAFGLRLR--GVPKAERRARAEELLALVGL-ADFARRRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL--RQGEVVE 506
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
.
gi 658548496 507 Q 507
Cdd:COG4525 218 R 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
275-521 |
5.30e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 121.25 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPLHRWN 353
Cdd:PRK13644 1 MIRLENVSYSYP----------DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 354 RRQmlPVRPRMQVVFQDPNSSLnprlsVLQIIEEGLRVHQPGLSAQQRE--QEVMRVMAEVGLDAgTRHRYPAEFSGGQR 431
Cdd:PRK13644 71 KLQ--GIRKLVGIVFQNPETQF-----VGRTVEEDLAFGPENLCLPPIEirKRVDRALAEIGLEK-YRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQ 511
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
250
....*....|
gi 658548496 512 RVFSAPTQRY 521
Cdd:PRK13644 221 NVLSDVSLQT 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-246 |
1.06e-30 |
|
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: 119.57 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRL-LPSppvsypQGDILFHGSSLLHADEHTLRgirgNKIAMIFQEPM 102
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPT------SGEILLDGVDIRDLNLRWLR----SQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 VSLNPLhsLEKQLYEVLSLHRGMRKEAARgeildclertgIRNAAKRLNDFPH-----------QLSGGERQRVMIAMAL 171
Cdd:cd03249 88 LFDGTI--AENIRYGKPDATDEEVEEAAK-----------KANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 172 LTRPELLIADEPTTALDVTVQAQILTLLRELRdeLNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTLLS 246
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
273-509 |
1.51e-30 |
|
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: 119.42 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI------ASQGEIFFDD 346
Cdd:COG1119 1 DPLLELRNVTVRR-----------GGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLItgdlppTYGNDVRLFG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNrrqMLPVRPRMQVVFQDPNSSLNPRLSVLQIIEEGL-----RVHQPglSAQQREQeVMRVMAEVGLdAGTRHR 421
Cdd:COG1119 66 ERRGGED---VWELRKRIGLVSPALQLRFPRDETVLDVVLSGFfdsigLYREP--TDEQRER-ARELLELLGL-AHLADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 422 YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKD 218
|
....*...
gi 658548496 502 GEVVEQGE 509
Cdd:COG1119 219 GRVVAAGP 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
305-517 |
2.38e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 121.37 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 305 IRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPV-RPRMQVVFQDpnSSLNPR 378
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTT----LIRLIAgltrpDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LSVLQIIEEGLRVHQPGLSaQQREQEVMRVMaevGLDAGTRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDR 458
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSER-RISFERVIELL---GIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 459 TVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-252 |
2.75e-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: 118.21 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 23 TVVTDLSLQIQPGETLALVGESGSGKSvsalSILRL---LPSPPvsypQGDILFHGssllhaDEHTLRGIRGNKIAMIFQ 99
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKT----TLLRLiagLERPD----SGTILFGG------EDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 100 ------EPMVSLNPLHSLEKQlyevlslHRGMRKEAA--RGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMAL 171
Cdd:cd03296 82 hyalfrHMTVFDNVAFGLRVK-------PRSERPPEAeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 172 LTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRcVEQ-NTASTLLSAPQH 250
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQvGTPDEVYDHPAS 230
|
..
gi 658548496 251 PY 252
Cdd:cd03296 231 PF 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-521 |
2.80e-30 |
|
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: 120.68 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 317 LVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLhrwnrRQMLPVRPRMQVVFQdpNSSLNPRLSVLQIIEEGLRv 391
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAgfeqpDSGSIMLDGEDV-----TNVPPHLRHINMVFQ--SYALFPHMTVEENVAFGLK- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 392 hQPGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGL 471
Cdd:TIGR01187 69 -MRKVPRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658548496 472 QEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-528 |
3.82e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 120.29 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPIRKGILRrIVDQnpvlknIRFSLRPGESLGLVGESGSGKSTTGLAL-------LRLIASQgeIFFDD 346
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVK-AVDR------VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnWRVTADR--MRFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNRRQMLP-VRPRMQVVFQDPNSSLNPRLSV-LQIIEEGLRVHQPGLSAQQ---REQEVMRVMAEVGLDA--GTR 419
Cdd:PRK15093 73 IDLLRLSPRERRKlVGHNVSMIFQEPQSCLDPSERVgRQLMQNIPGWTYKGRWWQRfgwRKRRAIELLHRVGIKDhkDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260
....*....|....*....|....*....
gi 658548496 500 RQGEVVEQGECQRVFSAPTQRYTRQLLSA 528
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRA 261
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
256-508 |
3.98e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 124.83 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 256 LLDSEPSGDPVPLAADSTPLLRVE--DLSVSFPIRKgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL 333
Cdd:TIGR00958 457 YLDRKPNIPLTGTLAPLNLEGLIEfqDVSFSYPNRP--------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 334 RL-IASQGEIFFDDMPL----HRWNRRQMlpvrprmQVVFQDPnssLNPRLSVLQIIEEGLRvhqpglsaQQREQEVMRV 408
Cdd:TIGR00958 529 NLyQPTGGQVLLDGVPLvqydHHYLHRQV-------ALVGQEP---VLFSGSVRENIAYGLT--------DTPDEEIMAA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 409 MAEVGLD---AGTRHRYPAE-------FSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILALLKGLQEKHRLA 478
Cdd:TIGR00958 591 AKAANAHdfiMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRT 666
|
250 260 270
....*....|....*....|....*....|
gi 658548496 479 YIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR00958 667 VLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
8-276 |
4.21e-30 |
|
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: 120.87 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS-PPVSYPQGDILFHGSSLLHADEHTl 86
Cdd:TIGR03258 8 IDHLRVAYGA----NTVLDDLSLEIEAGELLALIGKSGCGKT----TLLRAIAGfVKAAGLTGRIAIADRDLTHAPPHK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 87 rgiRGnkIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAAKRLndfPHQLSGGERQRVM 166
Cdd:TIGR03258 79 ---RG--LALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAE-RVADALKLVGLGDAAAHL---PAQLSGGMQQRIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDEL-NMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLL 245
Cdd:TIGR03258 148 IARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALY 227
|
250 260 270
....*....|....*....|....*....|.
gi 658548496 246 SAPQHPYTQRLLDSEPSGDPVPLAADSTPLL 276
Cdd:TIGR03258 228 DAPADGFAAEFLGAANILPAIALGITEAPGL 258
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
297-508 |
6.62e-30 |
|
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: 116.82 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDD-----MPLHRWnrrqmlpvRPRMQVVFQD 370
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGvdiskIGLHDL--------RSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 PN-------SSLNP--RLSVLQIIEEGLRVHQPGLSAQQREQEVMRVmAEVGLDagtrhrypaeFSGGQRQRIAIARALI 441
Cdd:cd03244 87 PVlfsgtirSNLDPfgEYSDEELWQALERVGLKEFVESLPGGLDTVV-EEGGEN----------LSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 442 LKPELIILDEPTSSLDRTVQAQILALLkglqeKHRLA---YIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTI-----REAFKdctVLTIAHRLDTI-IDSDRILVLDKGRVVEFD 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-238 |
7.37e-30 |
|
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: 116.23 E-value: 7.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHT 85
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL--PDS---GEVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 L------RGIRGNkiaMIFQEPMVSLNPLhslekqlyevlslhRGMRKEAARGEILDCLERTGIRN-AAKRLNdfphQLS 158
Cdd:cd03269 72 IgylpeeRGLYPK---MKVIDQLVYLAQL--------------KGLKKEEARRRIDEWLERLELSEyANKRVE----ELS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-236 |
8.88e-30 |
|
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: 116.77 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqGETrTVVTDLSLQIQPGETLALVGESGSGKS--VSALS-ILRllPSppvsypQGDILFHGSSLLHAD 82
Cdd:cd03219 1 LEVRGLTKRF---GGL-VALDDVSFSVRPGEIHGLIGPNGAGKTtlFNLISgFLR--PT------SGSVLFDGEDITGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EH--TLRGI-RGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKE-AARGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:cd03219 69 PHeiARLGIgRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREErEARERAEELLERVGLADLADRP---AGELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
302-515 |
1.12e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtgLALLRL---IASQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDPNSSLnpr 378
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKST--IAKLMIgieKVKSGEIFYNNQAITDDNFEK---LRKHIGIVFQNPDNQF--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 lsVLQIIEE----GLRVHQpgLSAQQREQEVMRVMAEVGLDAGTRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK13648 97 --VGSIVKYdvafGLENHA--VPYDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDL-QVVRAlcHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAMEA--DHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
297-515 |
1.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.14 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEIFFDDMPL---HRWNRRQmlpvrpRMQVVF 368
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIdglleAESGQIIIDGDLLteeNVWDIRH------KIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 QDPNSSLnprlsVLQIIEE----GLRvhQPGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:PRK13650 88 QNPDNQF-----VGATVEDdvafGLE--NKGIPHEEMKERVNEALELVGMQD-FKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 445 ELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
276-504 |
2.02e-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: 113.85 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:cd03246 1 LEVENVSFRYP---------GAEPPVLRNVSFSIEPGESLAIIGPSGSGKST----LARLILgllrpTSGRVRLDGADIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQmlpvrprmqvvfqdpnsslnprlsvlqiieegLRVHqpglsaqqreqeVMRVMAEVGLDAGTrhryPAE--FSG 428
Cdd:cd03246 68 QWDPNE--------------------------------LGDH------------VGYLPQDDELFSGS----IAEniLSG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVrALCHQVIVLRQGEV 504
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
297-512 |
2.85e-29 |
|
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: 114.91 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTgLALL--RLIASQGEIFFDDMPLhrwnRRQMLPVRPRMQVVFQDpnSS 374
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtgELRPTSGTAYINGYSI----RTDRKAARQSLGYCPQF--DA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:cd03263 86 LFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 455 SLDRTVQAQILALLKGLQEKHrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQR 512
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-527 |
3.30e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.90 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-------LIASQ-- 339
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPGArv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 340 -GEIFFDDMPLHRwnrRQMLPVRPRMQV--VFQDPNsslnP-RLSVLQIIEEGLRVHQPgLSAQQREQEVMRVMAEVGL- 414
Cdd:COG1117 70 eGEILLDGEDIYD---PDVDVVELRRRVgmVFQKPN----PfPKSIYDNVAYGLRLHGI-KSKSELDEIVEESLRKAALw 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 415 ----DagtR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFISHDLQVV 489
Cdd:COG1117 142 devkD---RlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQA 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 658548496 490 RALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:COG1117 217 ARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
5.26e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.26 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQGETRTVvtdlSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSLL- 79
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSV----SLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 -HADEHTLRgirgNKIAMIFQEPmvslNPLhslEKQLYEvlSLHRGMRKEAARG-EILDCLERTGIRNAA------KRLN 151
Cdd:PRK14239 77 pRTDTVDLR----KEIGMVFQQP----NPF---PMSIYE--NVVYGLRLKGIKDkQVLDEAVEKSLKGASiwdevkDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMslLFITHNLSIVRKLADNVAVMQ 231
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|...
gi 658548496 232 NGRCVEQNTASTLLSAPQHPYTQ 254
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKETE 244
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
239-508 |
5.70e-29 |
|
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: 121.22 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 239 NTASTLLSA-PQHPYTQRLLDSEP-----SGDPVPLAAdstpllRVEDLSVSFPIRKgilrrivDQNPVLKNIRFSLRPG 312
Cdd:TIGR03797 413 NTLISILAViPLWERAKPILEALPevdeaKTDPGKLSG------AIEVDRVTFRYRP-------DGPLILDDVSLQIEPG 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 313 ESLGLVGESGSGKSTtglaLLRLIAS-----QGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQdpNSSLNPRlSVLQIIEE 387
Cdd:TIGR03797 480 EFVAIVGPSGSGKST----LLRLLLGfetpeSGSVFYDGQDLAGLDVQA---VRRQLGVVLQ--NGRLMSG-SIFENIAG 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 388 GLRVHQpglsaqqreQEVMRVMAEVGLDAGTR------HRYPAE----FSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:TIGR03797 550 GAPLTL---------DEAWEAARMAGLAEDIRampmgmHTVISEgggtLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 658548496 458 RTVQAQILALLKGLQekhrLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03797 621 NRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
284-521 |
6.57e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 6.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 284 SFPIRKGILRRIVDqNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFD--DMPLHRWNRRQ 356
Cdd:PRK11432 5 NFVVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDgeDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 MLpvrprmqVVFQdpNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAI 436
Cdd:PRK11432 80 IC-------MVFQ--SYALFPHMSLGENVGYGLKML--GVPKEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 437 ARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
....*
gi 658548496 517 PTQRY 521
Cdd:PRK11432 228 PASRF 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
266-520 |
8.45e-29 |
|
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: 120.24 E-value: 8.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 266 VPLAADSTPL------LRVEDLSVSFPIRkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI--- 336
Cdd:COG4618 315 VPAEPERMPLprpkgrLSVENLTVVPPGS---------KRPILRGVSFSLEPGEVLGVIGPSGSGKST----LARLLvgv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 337 --ASQGEIFFDDMPLHRWNRRQM------LPvrprmQVV-------------FQDPNSSlnprlsvlQIIEeglrvhqpg 395
Cdd:COG4618 382 wpPTAGSVRLDGADLSQWDREELgrhigyLP-----QDVelfdgtiaeniarFGDADPE--------KVVA--------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 396 lSAQqreqevmrvMA---------------EVGlDAGTRhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTV 460
Cdd:COG4618 440 -AAK---------LAgvhemilrlpdgydtRIG-EGGAR------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 461 QAQILALLKGLQEKHRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFSAPTQR 520
Cdd:COG4618 503 EAALAAAIRALKARGATV-VVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-255 |
1.04e-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: 116.75 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHGSSLLHADEHTLRGIRGNKIAMIFQEpmVSLN 106
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKT-TLIRLIAGLTRPDE----GEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLEKQLYEVLSLHRGMRKEAARGEILDCLertGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 187 LDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQR 255
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
277-508 |
1.05e-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: 113.79 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFPIRKGIlrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNRR 355
Cdd:cd03249 2 EFKNVSFRYPSRPDV--------PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILLDGVDIRDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 356 QmlpVRPRMQVVFQDPNsslnprL---SVLQIIEEGLRvhqpglSAQQREQEVMRVMAEV---------GLD--AGTRHr 421
Cdd:cd03249 74 W---LRSQIGLVSQEPV------LfdgTIAENIRYGKP------DATDEEVEEAAKKANIhdfimslpdGYDtlVGERG- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 422 ypAEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAyIFISHDLQVVRAlCHQVI 497
Cdd:cd03249 138 --SQLSGGQKQRIAIARALLRNPKILLLDEATSALDaeseKLVQEALDRAMKG-----RTT-IVIAHRLSTIRN-ADLIA 208
|
250
....*....|.
gi 658548496 498 VLRQGEVVEQG 508
Cdd:cd03249 209 VLQNGQVVEQG 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
298-508 |
1.14e-28 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 113.08 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMplhrwNRRQMLPVRPRMQVVFQDPnsSLN 376
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGK-----SYQKNIEALRRIGALIEAP--GFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 377 PRLSVlqiiEEGLRVHQPGLsaQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:cd03268 85 PNLTA----RENLRLLARLL--GIRKKRIDEVLDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658548496 457 DRTVQAQILALLKGLQEKHRLayIFI-SHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03268 158 DPDGIKELRELILSLRDQGIT--VLIsSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
298-496 |
1.23e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.76 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPVRPRmQVVFQDPN 372
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKST----LLHLLGgldtpTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 SSLNPRLSVLQIIEEGLRV-HQPGLSAQQREQEVMrvmAEVGLDAGTRHRyPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK11629 96 HHLLPDFTALENVAMPLLIgKKKPAEINSRALEML---AAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 658548496 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-264 |
1.30e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.81 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSLL-HAD 82
Cdd:PRK14271 20 PAMAAVNLTLGFAG----KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRgirgNKIAMIFQEPmvslNPL-HSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAK-RLNDFPHQLSGG 160
Cdd:PRK14271 96 VLEFR----RRVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELnmSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
250 260
....*....|....*....|....
gi 658548496 241 ASTLLSAPQHPYTQRLLdSEPSGD 264
Cdd:PRK14271 246 TEQLFSSPKHAETARYV-AGLSGD 268
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-238 |
1.57e-28 |
|
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: 113.10 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLH 80
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIagfetPT------SGEILLDGKDITN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTlrgirgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGG 160
Cdd:cd03300 67 LPPHK------RPVNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRcVEQ 238
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK-IQQ 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
271-514 |
2.08e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 271 DSTPLLRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFD 345
Cdd:PRK13632 3 NKSVMIKVENVSFSYP---------NSENNALKNVSFEINEGEYVAILGHNGSGKSTiskilTGL----LKPQSGEIKID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNRRQmlpVRPRMQVVFQDPNSslnprlsvlQIIeeGLRVHQP---GLSAQQREQEVMR-----VMAEVGLDaG 417
Cdd:PRK13632 70 GITISKENLKE---IRKKIGIIFQNPDN---------QFI--GATVEDDiafGLENKKVPPKKMKdiiddLAKKVGME-D 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 418 TRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVI 497
Cdd:PRK13632 135 YLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVI 213
|
250
....*....|....*..
gi 658548496 498 VLRQGEVVEQGECQRVF 514
Cdd:PRK13632 214 VFSEGKLIAQGKPKEIL 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-246 |
2.87e-28 |
|
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: 112.71 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 9 DNLSIAFSTqgeTRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHADE 83
Cdd:cd03253 4 ENVTFAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLfrfydVS------SGSILIDGQDIREVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRgirgNKIAMIFQEpMVSLNplhslEKQLYEVlslhRGMRKEAARGEIldclertgiRNAAK------RLNDFPHQ- 156
Cdd:cd03253 71 DSLR----RAIGVVPQD-TVLFN-----DTIGYNI----RYGRPDATDEEV---------IEAAKaaqihdKIMRFPDGy 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 ----------LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADN 226
Cdd:cd03253 128 dtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADK 204
|
250 260
....*....|....*....|
gi 658548496 227 VAVMQNGRCVEQNTASTLLS 246
Cdd:cd03253 205 IIVLKDGRIVERGTHEELLA 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
302-520 |
2.92e-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: 112.56 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmlPVRPRMqVVFQdpNSSLN 376
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST----LLNLISglaqpTSGGVILEGKQITE-------PGPDRM-VVFQ--NYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 377 PRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 457 DRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV-FSAPTQR 520
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
275-497 |
3.15e-28 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 112.10 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPI-RKGILRRivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFF---- 344
Cdd:TIGR02324 1 LLEVEDLSKTFTLhQQGGVRL-----PVLKNVSLTVNAGECVALSGPSGAGKST----LLKSLyanylPDSGRILVrheg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 345 DDMPLHRWNRRQMLPVRpRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAGTRHRYPA 424
Cdd:TIGR02324 72 AWVDLAQASPREVLEVR-RKTIGYVSQFLRVIPRVSALEVVAEPLLER--GVPREAARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHR-LAYIFISHDLQVVRALCHQVI 497
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIA--EAKARgAALIGIFHDEEVRELVADRVM 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-504 |
3.21e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 117.84 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLH--- 80
Cdd:PRK15439 10 PLLCARSISKQYSGV----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-----SGTLEIGGNPCARltp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLrgirgnKIAMIFQEPMVSLNpLHSLEKQLYevlslhrGMRKEAARGEILDCLertgIRNAAKRLNdfPHQLSG- 159
Cdd:PRK15439 81 AKAHQL------GIYLVPQEPLLFPN-LSVKENILF-------GLPKRQASMQKMKQL----LAALGCQLD--LDSSAGs 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 ---GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:PRK15439 141 levADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 237 -----EQNTASTLLSA-------PQHPYTQRLLDSEPSGDPVPLAAdsTPLLRVEDLSvsfpirkgilrrivdqNPVLKN 304
Cdd:PRK15439 220 lsgktADLSTDDIIQAitpaareKSLSASQKLWLELPGNRRQQAAG--APVLTVEDLT----------------GEGFRN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 305 IRFSLRPGESLGLVGESGSGKSTTGLAL--LRLIASqGEIFFDDMPLHRWNRRQ-------MLPVRPRMQVVFQDPNSSL 375
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLygLRPARG-GRIMLNGKEINALSTAQrlarglvYLPEDRQSSGLYLDAPLAW 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPrlsvlqiieEGLRVHQPGLSAQ-QREQEVM-RVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:PRK15439 361 NV---------CALTHNRRGFWIKpARENAVLeRYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 658548496 454 SSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
297-508 |
3.46e-28 |
|
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: 112.32 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLHRWNR---RQMLPVRPRMQVVF 368
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLfrfydVSSGSILIDGQDIREVTLdslRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 QDpnsslnprlsvlqIIEEGLRVHQPGLSAQQREQ---------EVMR-------VMAEVGLdagtrhrypaEFSGGQRQ 432
Cdd:cd03253 88 ND-------------TIGYNIRYGRPDATDEEVIEaakaaqihdKIMRfpdgydtIVGERGL----------KLSGGEKQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 433 RIAIARALILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAyIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDthteREIQAALRDVSKG-----RTT-IVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-516 |
3.54e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPIRKGILRRI-----------VDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA---- 337
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKST----LLKLIAgile 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 338 -SQGEiffddmplhrwnrrqmlpVRPRMQVVFQ-DPNSSLNPRLSVLQIIEEGLRVHqpGLSaqqrEQEVMRVMAEVgld 415
Cdd:COG1134 78 pTSGR------------------VEVNGRVSALlELGAGFHPELTGRENIYLNGRLL--GLS----RKEIDEKFDEI--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 416 agtrhrypAEFSG--------------GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIF 481
Cdd:COG1134 131 --------VEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIF 201
|
250 260 270
....*....|....*....|....*....|....*
gi 658548496 482 ISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:COG1134 202 VSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
297-529 |
3.66e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 114.03 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEIFFDDMPLhrwnrRQMLPVRPRMQV--VFQ 369
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT----LRMInrliePTSGRILIDGEDI-----RDLDPVELRRRIgyVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 370 dpNSSLNPRLSVLQIIEeglRVhqPGL---SAQQREQEVMRVMAEVGLDAGT-RHRYPAEFSGGQRQRIAIARALILKPE 445
Cdd:COG1125 84 --QIGLFPHMTVAENIA---TV--PRLlgwDKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 446 LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQL 525
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236
|
....
gi 658548496 526 LSAD 529
Cdd:COG1125 237 VGAD 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
302-526 |
3.92e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.29 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNRRQMLPVR-PRMQVVFQdpNSSLNPRL 379
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQ--SFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 SVLQIIEEGLRVhqPGLSAQQREQEVMRVMAEVGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:PRK10070 122 TVLDNTAFGMEL--AGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 460 VQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLL 526
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
301-527 |
3.92e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 115.18 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMlpvrpRMQVVFQdpNSSL 375
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAglehqTSGHIRFHGTDVSRLHARDR-----KVGFVFQ--HYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRLSVLQIIEEGLRVhqpgLSAQQR------EQEVMRVMAEVGLDagtrH---RYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PRK10851 86 FRHMTVFDNIAFGLTV----LPRRERpnaaaiKAKVTQLLEMVQLA----HladRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 447 IILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQLL 526
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
.
gi 658548496 527 S 527
Cdd:PRK10851 238 G 238
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-311 |
4.05e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.67 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpsppvsYP-QGDILFHGSSLlhaDEH 84
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL------APdSGEVLWDGEPL---DPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGI------RGnkiamifqepmvsLNPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:COG4152 69 DRRRIgylpeeRG-------------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGL---GDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VTVQAqILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 238 QNTASTLLSApqhpYTQRLLDSEPSGDPVPLAADSTPL-LRVEDLSVSFPIRKG-----ILRRIVDQNPVlknIRFSLRP 311
Cdd:COG4152 210 SGSVDEIRRQ----FGRNTLRLEADGDAGWLRALPGVTvVEEDGDGAELKLEDGadaqeLLRALLARGPV---REFEEVR 282
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-508 |
4.26e-28 |
|
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: 111.69 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIA-----SQGEIFFDDMPL 349
Cdd:cd03266 1 MITADALTKRFRDVKKTVQ-------AVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDGFDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRwnrrQMLPVRPRMQVVFQdpNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGG 429
Cdd:cd03266 70 VK----EPAEARRRLGFVSD--STGLYDRLTARENLEYFAGLY--GLKGDELTARLEELADRLGMEE-LLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
6.69e-28 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 111.37 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTqPLLSIDNLSIAFS--TQGETR-TVVTDLSLQIQPGETLALVGESGSGKSvsalSILRL-----LPSppvsypQGDIL 72
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCiygnyLPD------SGSIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 73 FHGSS----LLHADEHTLRGIRGNKIAMIFQ----EPMVS-----LNPLhslekqlyevlsLHRGMRKEAARGEILDCLE 139
Cdd:COG4778 70 VRHDGgwvdLAQASPREILALRRRTIGYVSQflrvIPRVSaldvvAEPL------------LERGVDREEARARARELLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 140 RTGIRnaaKRLND-FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLS 218
Cdd:COG4778 138 RLNLP---ERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEE 213
|
250
....*....|....*.
gi 658548496 219 IVRKLADNVAVMQNGR 234
Cdd:COG4778 214 VREAVADRVVDVTPFS 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
298-515 |
7.91e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTTGL---ALLrlIASQGEIFFDDMPL----HRWNrrqmlpVRPRMQVVFQD 370
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALL--IPSEGKVYVDGLDTsdeeNLWD------IRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 PNSSLnprlsVLQIIEEGLRVHQPGLSAQQRE--QEVMRVMAEVGLDAGTRHRyPAEFSGGQRQRIAIARALILKPELII 448
Cdd:PRK13633 94 PDNQI-----VATIVEEDVAFGPENLGIPPEEirERVDESLKKVGMYEYRRHA-PHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 449 LDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDL-QVVRAlcHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIFK 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-245 |
1.24e-27 |
|
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: 110.78 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 13 IAFStQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFHGSSLLHADEHTLRgirg 91
Cdd:cd03254 8 VNFS-YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------PQkGQILIDGIDIRDISRKSLR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 92 NKIAMIFQEPMVslnplhsLEKQLYEVLSLHrgmRKEAARGEILDCLERTGIRNAAKRL--------NDFPHQLSGGERQ 163
Cdd:cd03254 77 SMIGVVLQDTFL-------FSGTIMENIRLG---RPNATDEEVIEAAKEAGAHDFIMKLpngydtvlGENGGNLSQGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTAST 243
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
..
gi 658548496 244 LL 245
Cdd:cd03254 224 LL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
302-519 |
1.74e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.80 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDDMPLHRWNRRQML-PVRPRMQVVFQDPNSSL 375
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTliqniNAL----LKPTTGTVTVDDITITHKTKDKYIrPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRlSVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13646 99 FED-TVEREIIFGPK--NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 456 LDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQ 519
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
304-508 |
2.08e-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: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 304 NIRFSLR--PGESLGLVGESGSGKSTtglaLLRLIASQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPNssLNPRLSV 381
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKST----LLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN--LFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 382 LQIIEEGLrvhQPGL--SAQQReQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:cd03298 88 EQNVGLGL---SPGLklTAEDR-QAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658548496 460 VQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-216 |
2.82e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.48 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 18 QGETR-TVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLHADEHTLRGIRGNKIAM 96
Cdd:PRK10584 18 QGEHElSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQMDEEARAKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 97 IFQEPMV--SLNPLHSLEkqlyeVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLTR 174
Cdd:PRK10584 93 VFQSFMLipTLNALENVE-----LPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658548496 175 PELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHN 216
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-256 |
3.27e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 115.31 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGS 76
Cdd:PRK11160 335 DQVSLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLtrawdPQ------QGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 77 SLLHADEHTLRgirgNKIAMIFQEPmvslnplHSLEKQLYEVLSLhrgmRKEAARGEIL-DCLERTGIRN---AAKRLN- 151
Cdd:PRK11160 403 PIADYSEAALR----QAISVVSQRV-------HLFSATLRDNLLL----AAPNASDEALiEVLQQVGLEKlleDDKGLNa 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 ---DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKLaDNVA 228
Cdd:PRK11160 468 wlgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRIC 544
|
250 260
....*....|....*....|....*...
gi 658548496 229 VMQNGRCVEQNTASTLLSapQHPYTQRL 256
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLA--QQGRYYQL 570
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
27-260 |
4.28e-27 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 112.09 E-value: 4.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSVsalsILRLLPS--PPVSypqGDILFHGSSLlhadehTLRGIRGNKIAMIFQEPMvs 104
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTV----LLELIAGiwPPDS---GKIYLDGKDI------TNLPPEKRGIAYVYQNYM-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 105 LNPLHSLEKQLYEVLSLHRGMRKEAAR--GEILDCLertGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:NF040840 83 LFPHKTVFENIAFGLKLRKVPKEEIERkvKEIMELL---GISHLLHRK---PRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 183 PTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQRLLDSE 260
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
5.40e-27 |
|
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: 107.95 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFstqGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLLHA 81
Cdd:COG4133 1 MMLEAENLSCRR---GE-RLLFSGLSFTLAAGEALALTGPNGSGKT----TLLRILAglLPPSA---GEVLWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRgirgnKIAMIFQEPMV--SLNPLhslekqlyEVLSLHRGMRK-EAARGEILDCLERTGIrnaAKRLNDFPHQLS 158
Cdd:COG4133 70 REDYRR-----RLAYLGHADGLkpELTVR--------ENLRFWAALYGlRADREAIDEALEAVGL---AGLADLPVRQLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMsLLFITH 215
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTH 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
6.98e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 6.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVsaLS-ILRLLPSPPvsypQGDILFHGSSLlha 81
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKST--ISkILTGLLKPQ----SGEIKIDGITI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQLYEvlslhrgmRKEAARgEILDCLERTGIRNAAKRLndfP 154
Cdd:PRK13632 74 SKENLKEIR-KKIGIIFQNPdnqfigaTVEDDIAFGLENKKVP--------PKKMKD-IIDDLAKKVGMEDYLDKE---P 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVrKLADNVAVMQNGR 234
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGK 219
|
....
gi 658548496 235 CVEQ 238
Cdd:PRK13632 220 LIAQ 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
297-516 |
7.67e-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: 108.73 E-value: 7.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEIFFD--DMPL--HRWNRRQMlpvrprmQVVFQDp 371
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDghDLALadPAWLRRQV-------GVVLQE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSLNprlsvlQIIEEGLRVHQPGLSAQQREQ--------EVMRVMAEvGLDAGTRHRyPAEFSGGQRQRIAIARALILK 443
Cdd:cd03252 85 NVLFN------RSIRDNIALADPGMSMERVIEaaklagahDFISELPE-GYDTIVGEQ-GAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 444 PELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAyIFISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:cd03252 157 PRILIFDEATSALDyeseHAIMRNMHDICAG-----RTV-IIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-257 |
8.64e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 8.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLlhADEHT-LRGIRgNKIAMIFQEPmvsl 105
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK--PTS---GKIIIDGVDI--TDKKVkLSDIR-KKVGLVFQYP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 106 nplhslEKQLYEvlslhRGMRKEAARGEILDCLERTGIRNAAKR--------LNDF----PHQLSGGERQRVMIAMALLT 173
Cdd:PRK13637 93 ------EYQLFE-----ETIEKDIAFGPINLGLSEEEIENRVKRamnivgldYEDYkdksPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 174 RPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT-------ASTL-- 244
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTprevfkeVETLes 241
|
250
....*....|....*
gi 658548496 245 --LSAPQHPYTQRLL 257
Cdd:PRK13637 242 igLAVPQVTYLVRKL 256
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-508 |
8.73e-27 |
|
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: 107.84 E-value: 8.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGE--IFFDDMplhrwnRRQMLPVRPRMQVVF 368
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRatVAGHDV------VREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 QDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:cd03265 80 QDL--SVDDELTGWENLYIHARLY--GVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 449 LDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-240 |
9.06e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 108.36 E-value: 9.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFStQGETRT-VVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLL 79
Cdd:PRK11629 1 MNKILLQCDNLCKRYQ-EGSVQTdVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPT----SGDVIFNGQPMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRGNKIAMIFQ--EPMVSLNPLHSLEKQLyevlsLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQL 157
Cdd:PRK11629 75 KLSSAAKAELRNQKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAvMQNGRCVE 237
Cdd:PRK11629 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
|
...
gi 658548496 238 QNT 240
Cdd:PRK11629 226 ELS 228
|
|
| 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 658548496 6 LSIDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHT 85
Cdd:cd03224 1 LEVENLNAGY---GKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRS---GSIRFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 L--RGIrgnkiAMIFQEPMV--SLNPLHSLEkqlyevLSLHRGMRKEAARG--EILDCLERTgirnaAKRLNDFPHQLSG 159
Cdd:cd03224 72 RarAGI-----GYVPEGRRIfpELTVEENLL------LGAYARRRAKRKARleRVYELFPRL-----KERRKQLAGTLSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQN 239
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
....*..
gi 658548496 240 TASTLLS 246
Cdd:cd03224 215 TAAELLA 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
297-508 |
1.30e-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: 107.68 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEIFFDDMPLhrwnrRQMLPV--RPRMQVVFQDPns 373
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDI-----RQLDPAdlRRNIGYVPQDV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 374 slnpRL---SVLQIIEEGLRVHQpglsaqqrEQEVMRVMAEVGLDAGTRhRYPAEF-----------SGGQRQRIAIARA 439
Cdd:cd03245 88 ----TLfygTLRDNITLGAPLAD--------DERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 440 LILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
27-234 |
1.38e-26 |
|
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: 107.33 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHADEHTLRGIRgNKIAMIFQEP 101
Cdd:TIGR02673 20 DVSLHIRKGEFLFLTGPSGAGKT----TLLKLLygaltPS------RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 102 MVSLNplhsleKQLYE--VLSLH-RGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:TIGR02673 89 RLLPD------RTVYEnvALPLEvRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 179 IADEPTTALDVTVQAQILTLLRELRDeLNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
297-516 |
1.51e-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: 113.81 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLhrwnrRQMLP--VRPRMQVVFQ 369
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKST----LLKLLLglyqpTEGSVLLDGVDI-----RQIDPadLRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 370 DPnsslnpRL---SVLQIIEEGlrvhqpglSAQQREQEVMRVMAEVGLDAGTRhRYPAEF-----------SGGQRQRIA 435
Cdd:TIGR03375 547 DP------RLfygTLRDNIALG--------APYADDEEILRAAELAGVTEFVR-RHPDGLdmqigergrslSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 436 IARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688
|
.
gi 658548496 516 A 516
Cdd:TIGR03375 689 A 689
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-257 |
1.78e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.01 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSLLHADEHTLRGIRgnKIAMIFQEPmv 103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQYP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 slNPLHSLekQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAA------KRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK14267 95 --NPFPHL--TIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 178 LIADEPTTALDVTVQAQILTLLRELRDELnmSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQRLL 257
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
275-504 |
1.85e-26 |
|
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: 107.17 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRKgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPL---- 349
Cdd:cd03248 11 IVKFQNVTFAYPTRP--------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPIsqye 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNRRQMlpvrprmQVVFQDPnsSLNPRlSVLQIIEEGLRVHQPG--LSAQQREQE---VMRVMAEVGLDAGTRHrypA 424
Cdd:cd03248 83 HKYLHSKV-------SLVGQEP--VLFAR-SLQDNIAYGLQSCSFEcvKEAAQKAHAhsfISELASGYDTEVGEKG---S 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlaYIFISHDLQVV-RAlcHQVIVLRQGE 503
Cdd:cd03248 150 QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT--VLVIAHRLSTVeRA--DQILVLDGGR 225
|
.
gi 658548496 504 V 504
Cdd:cd03248 226 I 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
305-510 |
2.17e-26 |
|
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: 106.87 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 305 IRFSL--RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMplhrwNRRQMLPVRPRMQVVFQDPNssLNP 377
Cdd:TIGR01277 15 MEFDLnvADGEIVAIMGPSGAGKST----LLNLIAgfiepASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENN--LFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 378 RLSVLQIIEEGLRvhqPGLSAQQREQEVMRVMA-EVGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:TIGR01277 84 HLTVRQNIGLGLH---PGLKLNAEQQEKVVDAAqQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658548496 457 DRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGEC 510
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-486 |
2.23e-26 |
|
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: 112.45 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 254 QRLLDSEPSGDPVPLAADST--------PLLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGK 325
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPAagavglgkPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 326 STTGLALLRLIA-SQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDPN---SSlnprlsvlqiIEEGLRVHQPGLSaqqr 401
Cdd:TIGR02868 375 STLLATLAGLLDpLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAHlfdTT----------VRENLRLARPDAT---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 402 EQEVMRVMAEVGLD---------AGTR-HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILA-LLKG 470
Cdd:TIGR02868 438 DEELWAALERVGLAdwlralpdgLDTVlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEdLLAA 517
|
250
....*....|....*.
gi 658548496 471 LQEKhrlAYIFISHDL 486
Cdd:TIGR02868 518 LSGR---TVVLITHHL 530
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-238 |
3.02e-26 |
|
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: 106.42 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPVsyPQGdilfhGSSLLHADEHTLRGIRGNKIAMIFQEPmvSLN 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS----TLLNLIAGFET--PQS-----GRVLINGVDVTAAPPADRPVSMLFQEN--NLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLEKQLyeVLSLHRGMR-KEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:cd03298 83 AHLTVEQNV--GLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658548496 186 ALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
297-508 |
3.92e-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: 112.53 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPLHR----WNRRQMlpvrprmQVVFQDp 371
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQhGQVLVDGVDLAIadpaWLRRQM-------GVVLQE- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 nsslnprlSVL--QIIEEGLRVHQPGLSaqqrEQEVMRVMAEVGLDA---GTRHRYPAE-------FSGGQRQRIAIARA 439
Cdd:TIGR01846 540 --------NVLfsRSIRDNIALCNPGAP----FEHVIHAAKLAGAHDfisELPQGYNTEvgekganLSGGQRQRIAIARA 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 440 LILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-510 |
4.07e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFPirkGILrrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDD 346
Cdd:COG3845 2 MPPALELRGITKRFG---GVV--------ANDDVSLTVRPGEIHALLGENGAGKST----LMKILyglyqPDSGEILIDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNrrqmlpvrPR--------MqvVFQDPnsSLNPRLSVLQIIEEGL-RVHQPGLSAQQREQEVMRVMAEVGL--D 415
Cdd:COG3845 67 KPVRIRS--------PRdaialgigM--VHQHF--MLVPNLTVAENIVLGLePTKGGRLDRKAARARIRELSERYGLdvD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 416 AgtrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLdrTVQ--AQILALLKGLQEKHRlAYIFISHDLQVVRALC 493
Cdd:COG3845 135 P---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAEGK-SIIFITHKLREVMAIA 208
|
250
....*....|....*..
gi 658548496 494 HQVIVLRQGEVVeqGEC 510
Cdd:COG3845 209 DRVTVLRRGKVV--GTV 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-238 |
4.09e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.40 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPvSYPQGDILFHGS--SLLHAdeht 85
Cdd:PRK10851 5 IANIKKSF---GRTQ-VLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIAGLE-HQTSGHIRFHGTdvSRLHA---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 lrgiRGNKIAMIFQ------EPMVSLNPLHSLekqlyEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSG 159
Cdd:PRK10851 72 ----RDRKVGFVFQhyalfrHMTVFDNIAFGL-----TVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGrCVEQ 238
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-236 |
4.81e-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: 104.05 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 23 TVVTDLSLQIQPGETLALVGESGSGKS--VSALSILRllpsPPVSypqGDILFHGssllhadehtlrgirgnkiamifqE 100
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKStlMKILSGLY----KPDS---GEILVDG------------------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PMVSLNPLHSLekqlyevlslhrgmrkeaargeildcleRTGIRnaakrlndFPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03216 63 EVSFASPRDAR----------------------------RAGIA--------MVYQLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 181 DEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
254-499 |
5.59e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 111.22 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 254 QRLLDSE--PSGDPVPLAADSTPLLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLA 331
Cdd:TIGR02857 298 FAVLDAAprPLAGKAPVTAAPASSLEFSGVSVAYP----------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 332 LLRLI-ASQGEIFFDDMPLHRWN----RRQM--LPVRPRMqvvfqdpnsslnprlsVLQIIEEGLRVHQPGLSAQQREQE 404
Cdd:TIGR02857 368 LLGFVdPTEGSIAVNGVPLADADadswRDQIawVPQHPFL----------------FAGTIAENIRLARPDASDAEIREA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 405 VMRVMA---EVGLDAGTRHRY---PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLa 478
Cdd:TIGR02857 432 LERAGLdefVAALPQGLDTPIgegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV- 510
|
250 260
....*....|....*....|.
gi 658548496 479 yIFISHDLqVVRALCHQVIVL 499
Cdd:TIGR02857 511 -LLVTHRL-ALAALADRIVVL 529
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-254 |
6.14e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 109.74 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 25 VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTLRGIRGNKIAMIFQEpmVS 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-----RGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 105 LNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAkrlNDFPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYA---HSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 185 TALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQ 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-508 |
6.80e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.46 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFPIRkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIF 343
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYPDQ---------PQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLtrawdPQQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 344 FDDMPLHRWNRRQMlpvRPRMQVVFQDP---NSSL--NPRLSVLQIIEEGLR--VHQPGLSAQQREQEvmrvmaevGLDA 416
Cdd:PRK11160 399 LNGQPIADYSEAAL---RQAISVVSQRVhlfSATLrdNLLLAAPNASDEALIevLQQVGLEKLLEDDK--------GLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 417 ----GTRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALL-KGLQEKhrlAYIFISHDLqvvRA 491
Cdd:PRK11160 468 wlgeGGR-----QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLaEHAQNK---TVLMITHRL---TG 536
|
250
....*....|....*....
gi 658548496 492 LCH--QVIVLRQGEVVEQG 508
Cdd:PRK11160 537 LEQfdRICVMDNGQIIEQG 555
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
276-508 |
6.83e-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: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKgilrrivdqnpVLKNIRFSLRPGeSLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLh 350
Cdd:cd03264 1 LQLENLTKRYGKKR-----------ALDGVSLTLGPG-MYGLLGPNGAGKTT----LMRILAtltppSSGTIRIDGQDV- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 rwnRRQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQ 430
Cdd:cd03264 64 ---LKQPQKLRRRIGYLPQEFG--VYPNFTVREFLDYIAWLK--GIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-245 |
7.27e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.59 E-value: 7.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 13 IAFSTQGeTRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHG---SSLlhadehTLRGI 89
Cdd:PRK13657 340 VSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPQ----SGRILIDGtdiRTV------TRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 90 RGNkIAMIFQEPMVslnplhsLEKQLYEVLSLHRG------MRKEAARGEILDCLERTGIR---NAAKRLNdfphQLSGG 160
Cdd:PRK13657 408 RRN-IAVVFQDAGL-------FNRSIEDNIRVGRPdatdeeMRAAAERAQAHDFIERKPDGydtVVGERGR----QLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNT 240
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
....*
gi 658548496 241 ASTLL 245
Cdd:PRK13657 553 FDELV 557
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-521 |
7.35e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA------SQGEIFFDDMPL 349
Cdd:PRK14247 4 IEIRDLKVSF-----------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRWNrrqMLPVRPRMQVVFQDPNSSlnPRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPA---EF 426
Cdd:PRK14247 73 FKMD---VIELRRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
250
....*....|....*....
gi 658548496 507 QGECQRVFSAP----TQRY 521
Cdd:PRK14247 226 WGPTREVFTNPrhelTEKY 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-255 |
7.35e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.67 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYP-QGDILFHGSSLLHADEHTLRgirgNKIAMIFQE 100
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PmvslNPLH--SLEKQLYEVLSLHRGMRKEAARGEILDCLERTGI-RNAAKRLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK14246 99 P----NPFPhlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 178 LIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQR 255
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-248 |
8.44e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 8.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSiaFSTQGetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLL 79
Cdd:COG4559 1 MLEAENLS--VRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRgnkiAMIFQEpmVSLN-PLHSLEkqlyeVLSLHR---GMRKEAARGEILDCLERTGIRNAAKRlnDFPh 155
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFTVEE-----VVALGRaphGSSAAQDRQIVREALALVGLAHLAGR--SYQ- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALL-------TRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVA 228
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRIL 211
|
250 260
....*....|....*....|
gi 658548496 229 VMQNGRCVEQNTASTLLSAP 248
Cdd:COG4559 212 LLHQGRLVAQGTPEEVLTDE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-244 |
9.79e-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: 105.14 E-value: 9.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 23 TVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLHADehtlRGIRgNKIAMIFQEPm 102
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKT-TTIKMLTTLLKPT----SGRATVAGHDVVREP----REVR-RRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 vslnplhSLEKQL--YEVLSLH---RGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03265 83 -------SVDDELtgWENLYIHarlYGVPGAERRERIDELLDFVGLLEAADRL---VKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 178 LIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTL 244
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-247 |
1.02e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.01 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDILFHGSSLLHADE 83
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRAL-SGELSPDSGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRgnkiAMIFQEPMVSLnPLhSLEkqlyEVLSL----HRGMRKEAARgEILDCLERTGIRNAAKRlnDFPhQLSG 159
Cdd:PRK13548 72 AELARRR----AVLPQHSSLSF-PF-TVE----EVVAMgrapHGLSRAEDDA-LVAAALAQVDLAHLAGR--DYP-QLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 160 GERQRVMIAMAL--LTRPE----LLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:PRK13548 138 GEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
250
....*....|....
gi 658548496 234 RCVEQNTASTLLSA 247
Cdd:PRK13548 218 RLVADGTPAEVLTP 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-248 |
1.08e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHTLRgirgNKIAMIFQEPmv 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ--PTG---GQVLLDGVPLVQYDHHYLH----RQVALVGQEP-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 slnplhslekQLYEvlslhRGMRKEAARGeiLDCLERTGIRNAAKRLN------DFPH-----------QLSGGERQRVM 166
Cdd:TIGR00958 565 ----------VLFS-----GSVRENIAYG--LTDTPDEEIMAAAKAANahdfimEFPNgydtevgekgsQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 167 IAMALLTRPELLIADEPTTALDVTVQAqiltLLRELRDELNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTLLS 246
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 658548496 247 AP 248
Cdd:TIGR00958 703 DQ 704
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-255 |
1.44e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSLLHADEHT 85
Cdd:PRK14247 4 IEIRDLKVSF---GQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRgirgNKIAMIFQEPmvslNPLHSLE--KQLYEVLSLHRGMR-KEAARGEILDCLERTGIRNAAK-RLNDFPHQLSGGE 161
Cdd:PRK14247 80 LR----RRVQMVFQIP----NPIPNLSifENVALGLKLNRLVKsKKELQERVRWALEKAQLWDEVKdRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTA 241
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
250
....*....|....
gi 658548496 242 STLLSAPQHPYTQR 255
Cdd:PRK14247 230 REVFTNPRHELTEK 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-238 |
1.64e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.47 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqGETrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSL-- 78
Cdd:COG3839 4 LELENVSKSY---GGV-EALKDIDLDIEDGEFLVLLGPSGCGKS----TLLRMIagledPT------SGEILIGGRDVtd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHADEhtlrgiRGnkIAMIFQEPMvslnplhslekqLYEVLSLH---------RGMRKEAARGEILDCLERTGIRNAAKR 149
Cdd:COG3839 70 LPPKD------RN--IAMVFQSYA------------LYPHMTVYeniafplklRKVPKAEIDRRVREAAELLGLEDLLDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 150 LndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAV 229
Cdd:COG3839 130 K---PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAV 206
|
....*....
gi 658548496 230 MQNGRcVEQ 238
Cdd:COG3839 207 MNDGR-IQQ 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-508 |
1.73e-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: 104.62 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMlpvRPRMQVVFQDP 371
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPrfydvDSGRILIDGHDVRDYTLASL---RRQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 ---NSSlnprlsvlqiIEEGLRVHQPGLSAQQRE--------QEVMRVMAEvGLDA--GTRHrypAEFSGGQRQRIAIAR 438
Cdd:cd03251 86 flfNDT----------VAENIAYGRPGATREEVEeaaraanaHEFIMELPE-GYDTviGERG---VKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 439 ALILKPELIILDEPTSSLD----RTVQAQILALLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03251 152 ALLKDPPILILDEATSALDteseRLVQAALERLMKN-----RTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
257-502 |
1.94e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 257 LDSEPSGDPVPLAADStPLLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI 336
Cdd:COG4178 345 ADALPEAASRIETSED-GALALEDLTLRTP----------DGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRAI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 337 A-----SQGEIFFDDmplhrwNRRQM-LPVRPRMqvvfqdPNSSLnpRLSVLQiieeglrvhqPGLSAQQREQEVMRVMA 410
Cdd:COG4178 410 AglwpyGSGRIARPA------GARVLfLPQRPYL------PLGTL--REALLY----------PATAEAFSDAELREALE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 411 EVGLDA-----GTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHD 485
Cdd:COG4178 466 AVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHR 543
|
250
....*....|....*..
gi 658548496 486 lQVVRALCHQVIVLRQG 502
Cdd:COG4178 544 -STLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
300-515 |
2.17e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.47 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPLHrWNRRQMLPVRPRMQVVFQDPNSSLnpr 378
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQI--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 lsVLQIIEEGLRVHQPGLSAQqrEQEVMRVMAE--VGLDA-GTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13638 91 --FYTDIDSDIAFSLRNLGVP--EAEITRRVDEalTLVDAqHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 456 LDRTVQAQILALLKGLQEKHRLAYIfISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-238 |
2.40e-25 |
|
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: 103.45 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 21 TRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLHADEHTlrgirgNKIAMIFQE 100
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKT-TTMKIILGLIKPD----SGEITFDGKSYQKNIEAL------RRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PmvSLNPLHSLEKQLYeVLSLHRGMRKEaargEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03268 81 P--GFYPNLTARENLR-LLARLLGIRKK----RIDEVLDVVGLKDSAKKK---VKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 181 DEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
274-520 |
4.59e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.23 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMP 348
Cdd:PRK09536 2 PMIDVSDLSVEF-----------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLRAIngtltPTAGTVLVAGDD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRWNRRQmlpVRPRMQVVFQDpnSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQE--VMRVMAEVGLDAGTrHRYPAEF 426
Cdd:PRK09536 67 VEALSARA---ASRRVASVPQD--TSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRaaVERAMERTGVAQFA-DRPVTSL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFIsHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRA 219
|
250
....*....|....
gi 658548496 507 QGECQRVFSAPTQR 520
Cdd:PRK09536 220 AGPPADVLTADTLR 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
278-517 |
4.70e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 109.03 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 278 VEDLSVSFPIRKGILRRIVDQ-------NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFD 345
Cdd:PRK10789 300 VKDGSEPVPEGRGELDVNIRQftypqtdHPALENVNFTLKPGQMLGICGPTGSGKST----LLSLIqrhfdVSEGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWnrrQMLPVRPRMQVVFQDP---------NSSLNPRLSVLQIIEEGLR---VHQPGLSAQQREQevmrvmAEVG 413
Cdd:PRK10789 376 DIPLTKL---QLDSWRSRLAVVSQTPflfsdtvanNIALGRPDATQQEIEHVARlasVHDDILRLPQGYD------TEVG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 414 lDAGTRhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQvvrAL- 492
Cdd:PRK10789 447 -ERGVM------LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLS---ALt 514
|
250 260
....*....|....*....|....*.
gi 658548496 493 -CHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:PRK10789 515 eASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
301-507 |
4.88e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 103.32 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPVRPR-MQVVFQdpNSS 374
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKST----LLAILAglddgSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQ--SFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQIIEegLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHrYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK10584 99 LIPTLNALENVE--LPALLRGESSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658548496 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQ 507
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-230 |
4.99e-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: 108.53 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFstqGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALS-ILRLLPSPpvsypQGDILFHGSSLLHAD 82
Cdd:TIGR02857 320 SSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS-TLLNlLLGFVDPT-----EGSIAVNGVPLADAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGirgnKIAMIFQEPmvslnplHSLEKQLYEVLSLHRgmrKEAARGEILDCLERTGI--------RNAAKRLNDFP 154
Cdd:TIGR02857 391 ADSWRD----QIAWVPQHP-------FLFAGTIAENIRLAR---PDASDAEIREALERAGLdefvaalpQGLDTPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRkLADNVAVM 230
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
275-506 |
5.38e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.01 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFPIRkgilrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPL 349
Cdd:PRK11248 1 MLQISHLYADYGGK-----------PALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAgfvpyQHGSITLDGKPV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRwnrrqmlPVRPRmQVVFQdpNSSLNPRLSVLQIIEEGLRVhqPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGG 429
Cdd:PRK11248 66 EG-------PGAER-GVVFQ--NEGLLPWRNVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLR--QGEVVE 506
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
273-526 |
5.42e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.46 E-value: 5.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDM 347
Cdd:PRK11607 17 TPLLEIRNLTKSF-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAgfeqpTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLhrwnrRQMLPVRPRMQVVFQdpNSSLNPRLSVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAGTRhRYPAEFS 427
Cdd:PRK11607 82 DL-----SHVPPYQRPINMMFQ--SYALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQEFAK-RKPHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQ 507
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250
....*....|....*....
gi 658548496 508 GECQRVFSAPTQRYTRQLL 526
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFI 250
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-247 |
6.05e-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: 103.08 E-value: 6.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 12 SIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHGSSLlhaDEHTLRGIRg 91
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRF-YDVDSGRILIDGHDV---RDYTLASLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 92 NKIAMIFQEPMVSLNPLHslEKQLYEvlslhrgmRKEAARGEILDCLErtgIRNAAKRLNDFPH-----------QLSGG 160
Cdd:cd03251 76 RQIGLVSQDVFLFNDTVA--ENIAYG--------RPGATREEVEEAAR---AANAHEFIMELPEgydtvigergvKLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNT 240
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
....*..
gi 658548496 241 ASTLLSA 247
Cdd:cd03251 220 HEELLAQ 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-515 |
7.31e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.74 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 306 RFSL--RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMplhrwNRRQMLPVRPRMQVVFQDPNssLNPR 378
Cdd:PRK10771 17 RFDLtvERGERVAILGPSGAGKST----LLNLIAgfltpASGSLTLNGQ-----DHTTTPPSRRPVSMLFQENN--LFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LSVLQIIeeGLRVHqPGL--SAQQREQevMRVMAE-VGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK10771 86 LTVAQNI--GLGLN-PGLklNAAQREK--LHAIARqMGIED-LLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 456 LDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
302-518 |
7.37e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-----LIASQGEIFF-DDMPLHRWNRRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKST----LLQhlnglLQPTSGTVTIgERVITAGKKNKKLKPLRKKVGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRlSVLQIIEEGlrvhqP---GLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK13634 99 FEE-TVEKDICFG-----PmnfGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 453 TSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
302-505 |
1.10e-24 |
|
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: 107.22 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEIFFDDMPLHRWNRRQMlpvrPRMQVVFQDPNSS 374
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKST----LMKILSGvyphgtwDGEIYWSGSPLKASNIRDT----ERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQ-------IIEEGLRVHQPGLSaqQREQEVMRvmaEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:TIGR02633 89 LVPELSVAEniflgneITLPGGRMAYNAMY--LRAKNLLR---ELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-508 |
1.54e-24 |
|
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: 101.84 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKGILRRIVDQN-----------PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQ 339
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAgiyppDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 340 GEIffddmplhrWNRRQmlpVRPRMqvvfqDPNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVM--AEVG--LD 415
Cdd:cd03220 77 GTV---------TVRGR---VSSLL-----GLGGGFNPELTGRENIYLNGRLL--GLSRKEIDEKIDEIIefSELGdfID 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 416 AGTRHrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQ 495
Cdd:cd03220 138 LPVKT-----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDR 211
|
250
....*....|...
gi 658548496 496 VIVLRQGEVVEQG 508
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
276-508 |
1.99e-24 |
|
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: 101.36 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNR 354
Cdd:cd03224 1 LEVENLNAGY-----------GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 355 RQmlpvRPRMQVVFQDPNSSLNPRLSVlqiiEEGLRVhqpGLSAQQREqEVMRVMAEVgLD-----AGTRHRYPAEFSGG 429
Cdd:cd03224 70 HE----RARAGIGYVPEGRRIFPELTV----EENLLL---GAYARRRA-KRKARLERV-YElfprlKERRKQLAGTLSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
296-524 |
2.19e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 296 VDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWN---RRQMLPVRPRMQVVFQDP 371
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKdifQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSlnPRLSVLQIIEEGLRVHqpGLSAQQREQEVMR-VMAEVGL--DAGTRHRYPA-EFSGGQRQRIAIARALILKPELI 447
Cdd:PRK14246 100 NPF--PHLSIYDNIAYPLKSH--GIKEKREIKKIVEeCLRKVGLwkEVYDRLNSPAsQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRYTRQ 524
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-247 |
2.24e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 106.72 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 13 IAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHGSSLLHadeHTLRGIRgN 92
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRF-YEPDSGQILLDGHDLAD---YTLASLR-R 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 93 KIAMIFQEPMVSLNPLHSlekqlyevlSLHRGMRKEAARGEILDCLERTGIRNAAKRLNDFPHQ--------LSGGERQR 164
Cdd:TIGR02203 407 QVALVSQDVVLFNDTIAN---------NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTL 244
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
...
gi 658548496 245 LSA 247
Cdd:TIGR02203 555 LAR 557
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
298-504 |
2.24e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.06 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmlpVRPRMQVVFQDpn 372
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLAgletpSAGELLAGTAPLAE--------AREDTRLMFQD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 SSLNPRLSVlqIIEEGLrvhqpGLSAQQREQeVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK11247 90 ARLLPWKKV--IDNVGL-----GLKGQWRDA-ALQALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658548496 453 TSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-240 |
2.65e-24 |
|
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: 101.03 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFStqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSppvsyPQGDILFHGSSLLHADEHT 85
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRgirgNKIAMIFQEPMV-------SLNPLHslekqlyevlslhrgmrkEAARGEILDCLERTGIRNAAKRLN---DFPH 155
Cdd:cd03244 76 LR----SRISIIPQDPVLfsgtirsNLDPFG------------------EYSDEELWQALERVGLKEFVESLPgglDTVV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVM 230
Cdd:cd03244 134 eeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVL 210
|
250
....*....|
gi 658548496 231 QNGRCVEQNT 240
Cdd:cd03244 211 DKGRVVEFDS 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
302-515 |
3.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTTGlallRLIASQGEIFFDDMPL--HRWNRRQMLPVRPRMQVVFQDPNSSLnprl 379
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTA----RLIDGLFEEFEGKVKIdgELLTAENVWNLRRKIGMVFQNPDNQF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 sVLQIIEEGLRVhqpGLSAQ--QREQEVMRV----MAEVGLDAGTRHryPAEFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:PRK13642 95 -VGATVEDDVAF---GMENQgiPREEMIKRVdealLAVNMLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 454 SSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-246 |
3.49e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHTLRgIRGNkIAMIFQEPMVSLN 106
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILK--PSS---GRILFDGKPIDYSRKGLMK-LRES-VGMVFQDPDNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLEKQLYEVLSLhrGMRKEAARGEILDCLERTGIrnaaKRLNDFP-HQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK13636 97 SASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 186 ALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-247 |
4.41e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 101.02 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 13 IAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTLRgirgN 92
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-----NGRVLVDGHDLALADPAWLR----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 93 KIAMIFQEPMVslnplhslekqlyevlsLHRGMRKEAARGEILDCLERtgIRNAAKRL--NDFPHQ-------------- 156
Cdd:cd03252 77 QVGVVLQENVL-----------------FNRSIRDNIALADPGMSMER--VIEAAKLAgaHDFISElpegydtivgeqga 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRC 235
Cdd:cd03252 138 gLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
250
....*....|..
gi 658548496 236 VEQNTASTLLSA 247
Cdd:cd03252 215 VEQGSHDELLAE 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-236 |
5.58e-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: 100.13 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDILFHGSSLLHADEH 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKT----TTLRML-AGLLEPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIrgnkiamifqepmvslnPLHSLEKQLYEVLS----------LHrGMRKEAARGEILDCLERTGIRN-AAKRLNDF 153
Cdd:cd03266 76 ARRRL-----------------GFVSDSTGLYDRLTarenleyfagLY-GLKGDELTARLEELADRLGMEElLDRRVGGF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 phqlSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:cd03266 138 ----STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRG 212
|
...
gi 658548496 234 RCV 236
Cdd:cd03266 213 RVV 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
256-508 |
7.65e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.43 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 256 LLDSEPSGDPVPLAADSTPL---LRVEDLSVSFPIRKgilrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTTgLAL 332
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRVkgaVEFDDVSFSYDNSR----------QGVEDVSFEAKPGQTVAIVGPTGAGKSTL-INL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 333 LRLI--ASQGEIFFDDMPLHRWNRRQMlpvRPRMQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPGLSaqqrEQEVMR 407
Cdd:PRK13657 381 LQRVfdPQSGRILIDGTDIRTVTRASL---RRNIAVVFQDAglfNRS----------IEDNIRVGRPDAT----DEEMRA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 408 VMA-----------EVGLD--AGTRHRypaEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLKG 470
Cdd:PRK13657 444 AAEraqahdfierkPDGYDtvVGERGR---QLSGGERQRLAIARALLKDPPILILDEATSALDveteAKVKAALDELMKG 520
|
250 260 270
....*....|....*....|....*....|....*...
gi 658548496 471 lqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PRK13657 521 -----RTTFI-IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
276-508 |
8.26e-24 |
|
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: 99.02 E-value: 8.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDD-----MPL 349
Cdd:cd03369 7 IEVENLSVRYA---------PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGidistIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRwnrrqmlpVRPRMQVVFQDP-------NSSLNP--RLSVLQIIeEGLRVHQPGLSaqqreqevmrvmaevgldagtrh 420
Cdd:cd03369 78 ED--------LRSSLTIIPQDPtlfsgtiRSNLDPfdEYSDEEIY-GALRVSEGGLN----------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 421 rypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVVrALCHQVIVLR 500
Cdd:cd03369 126 -----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTI-IDYDKILVMD 197
|
....*...
gi 658548496 501 QGEVVEQG 508
Cdd:cd03369 198 AGEVKEYD 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-249 |
8.47e-24 |
|
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: 100.06 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADE 83
Cdd:COG0410 2 PMLEVENLHAGY---GGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PRS---GSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTL--RGI------RGnkiamIFQEpmvslnplhslekqlyevLS----LHRGMRKEAARGEILDCLERTgirnaakrLN 151
Cdd:COG0410 73 HRIarLGIgyvpegRR-----IFPS------------------LTveenLLLGAYARRDRAEVRADLERV--------YE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 DFP------HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVR 221
Cdd:COG0410 122 LFPrlkerrRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFAL 200
|
250 260
....*....|....*....|....*...
gi 658548496 222 KLADNVAVMQNGRCVEQNTASTLLSAPQ 249
Cdd:COG0410 201 EIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
276-508 |
9.80e-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: 98.15 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivDQN-PVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEIFFDDMPLHrw 352
Cdd:cd03247 1 LSINNVSFSYP----------EQEqQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTgdLKPQQGEITLDGVPVS-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 353 nrrqmlpvrprmqvvfqDPNSSLNPRLSVLQiieeglrvhqpglsaqqreQEVMRVMAEVGLDAGTRhrypaeFSGGQRQ 432
Cdd:cd03247 68 -----------------DLEKALSSLISVLN-------------------QRPYLFDTTLRNNLGRR------FSGGERQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 433 RIAIARALILKPELIILDEPTSSLDRTVQAQILALL-KGLQEKhrlAYIFISHDLQVVRALcHQVIVLRQGEVVEQG 508
Cdd:cd03247 106 RLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-257 |
1.05e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.43 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGS----------SLLHADEHTLRGIRgNK 93
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEKPS----EGSIVVNGQtinlvrdkdgQLKVADKNQLRLLR-TR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 94 IAMIFQEPMV--SLNPLHSLEKQLYEVLslhrGMRKEAARGEILDCLERTGIRNAAKrlNDFPHQLSGGERQRVMIAMAL 171
Cdd:PRK10619 94 LTMVFQHFNLwsHMTVLENVMEAPIQVL----GLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 172 LTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHP 251
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
....*.
gi 658548496 252 YTQRLL 257
Cdd:PRK10619 247 RLQQFL 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
9-240 |
1.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.55 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 9 DNLSIAF--STQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLL-PSPPVSYPQGdilfhgssLLHADEHT 85
Cdd:PRK13633 8 KNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDG--------LDTSDEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRgNKIAMIFQEPM-----------VSLNPlhslekqlyEVLslhrGMRKEAARGEILDCLERTGIRNAAKRLndfP 154
Cdd:PRK13633 80 LWDIR-NKAGMVFQNPDnqivativeedVAFGP---------ENL----GIPPEEIRERVDESLKKVGMYEYRRHA---P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKlADNVAVMQNGR 234
Cdd:PRK13633 143 HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGK 221
|
....*.
gi 658548496 235 CVEQNT 240
Cdd:PRK13633 222 VVMEGT 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-234 |
1.16e-23 |
|
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: 99.47 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 10 NLSIAFSTQGETRtVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFHGSSLLHADEHTLRg 88
Cdd:cd03248 16 NVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ------PQgGQVLLDGKPISQYEHKYLH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 89 irgNKIAMIFQEPMVSLNPLHslEKQLYEVLSLHRGMRKEAARGEildclertgirNAAKRLNDFPH-----------QL 157
Cdd:cd03248 88 ---SKVSLVGQEPVLFARSLQ--DNIAYGLQSCSFECVKEAAQKA-----------HAHSFISELASgydtevgekgsQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRElrDELNMSLLFITHNLSIVRKlADNVAVMQNGR 234
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
276-508 |
1.27e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.76 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEIFFD-----DM 347
Cdd:COG0396 1 LEIKNLHVS-----------VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKYEVTSGSILLDgedilEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRwnrrqmlpvRPRMQV--VFQDPnsslnPR---LSVLQIIEEGL-RVHQPGLSAQQREQEVMRVMAEVGLDAGTRHR 421
Cdd:COG0396 70 SPDE---------RARAGIflAFQYP-----VEipgVSVSNFLRTALnARRGEELSAREFLKLLKEKMKELGLDEDFLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 422 YPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQA-QILA-LLKGLQEKHRlAYIFISHD---LQVVRAlcHQ 495
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLD--IDAlRIVAeGVNKLRSPDR-GILIITHYqriLDYIKP--DF 210
|
250
....*....|...
gi 658548496 496 VIVLRQGEVVEQG 508
Cdd:COG0396 211 VHVLVDGRIVKSG 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-238 |
1.66e-23 |
|
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: 98.48 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVsalsILRLLPS--PPVSypqGDILFHGSSLlhade 83
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTT----TLRMIAGleEPTS---GRIYIGGRDV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 hTLRGIRGNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAakrLNDFPHQLSGGERQ 163
Cdd:cd03301 65 -TDLPPKDRDIAMVFQN--YALYPHMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHL---LDRKPKQLSGGQRQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRcVEQ 238
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-246 |
1.70e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 29 SLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSypqgdilfhGSSLLHADEHTLRGIRGNKIAMIFQEPmvSLN 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGflTPAS---------GSLTLNGQDHTTTPPSRRPVSMLFQEN--NLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLEKQLyeVLSLHRGMRKEAA-RGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK10771 84 SHLTVAQNI--GLGLNPGLKLNAAqREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 186 ALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-246 |
1.95e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVvTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLlhaDEH 84
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGQIIIDGDLL---TEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQL 157
Cdd:PRK13650 75 NVWDIR-HKIGMVFQNPdnqfvgaTVEDDVAFGLENK---------GIPHEEMKERVNEALELVGMQDFKERE---PARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVrKLADNVAVMQNGRCVE 237
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
....*....
gi 658548496 238 QNTASTLLS 246
Cdd:PRK13650 221 TSTPRELFS 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
272-527 |
2.11e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFPIRKGilrrivdqnpvLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL------IASQGEIFFD 345
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKA-----------LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRwNRRQMLPVRPRMQVVFQDPNSSlnPrLSVLQIIEEGLRVhqpglsAQQREQEVMRVMAEVGLDAGT------- 418
Cdd:PRK14239 71 GHNIYS-PRTDTVDLRKEIGMVFQQPNPF--P-MSIYENVVYGLRL------KGIKDKQVLDEAVEKSLKGASiwdevkd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 419 -RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDLQVVRALCHQVI 497
Cdd:PRK14239 141 rLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTG 218
|
250 260 270
....*....|....*....|....*....|
gi 658548496 498 VLRQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-246 |
2.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.24 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 25 VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSllhADEHtLRGIRgNKIAMIFQEPmvs 104
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT---KDKY-IRPVR-KRIGMVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 105 lnplhslEKQLYEVlSLHR---------GMRKEAARGEILDCLERTGI-RNAakrLNDFPHQLSGGERQRVMIAMALLTR 174
Cdd:PRK13646 95 -------ESQLFED-TVEReiifgpknfKMNLDEVKNYAHRLLMDLGFsRDV---MSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 175 PELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-504 |
2.51e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.16 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFSTqgetrtvVTDLS---LQIQPGETLALVGESGSGKSvsalSILRLLPSppvSYP--QGDILFHGs 76
Cdd:PRK10762 1 MQALLQLKGIDKAFPG-------VKALSgaaLNVYPGRVMALVGENGAGKS----TMMKVLTG---IYTrdAGSILYLG- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 77 sllhaDEHTLRGIRGNK---IAMIFQEpmVSLNPLHSLEKQLY---EVLS-----LHRGMRKEAARgeildCLERTGIRN 145
Cdd:PRK10762 66 -----KEVTFNGPKSSQeagIGIIHQE--LNLIPQLTIAENIFlgrEFVNrfgriDWKKMYAEADK-----LLARLNLRF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 146 AAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLAD 225
Cdd:PRK10762 134 SSDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 226 NVAVMQNG-----RCVEQNTASTLLS-------APQHPYtqrlLDSEPSGdpvplaadstPLLRVEDLSvsfpirkgilr 293
Cdd:PRK10762 210 DVTVFRDGqfiaeREVADLTEDSLIEmmvgrklEDQYPR----LDKAPGE----------VRLKVDNLS----------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 294 rivdqNPVLKNIRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEIFFDDMPLHRWNRRQMLPV-------- 360
Cdd:PRK10762 265 -----GPGVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLygalpRTSGYVTLDGHEVVTRSPQDGLANgivyised 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 361 RPR------MQVvfqDPNSSLNprlSVLQIIEEGLRVhqpglsaqQREQEVMRVMAEVGL---DAGTRHRYPAEFSGGQR 431
Cdd:PRK10762 336 RKRdglvlgMSV---KENMSLT---ALRYFSRAGGSL--------KHADEQQAVSDFIRLfniKTPSMEQAIGLLSGGNQ 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-266 |
4.98e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHT 85
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQS---GTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LrgirGNKIAMIFQEPM----VSLNPLHSLEKQLYevLSLHrGMRKEAARGEILDCLERTGIRN-AAKRLNDfphqLSGG 160
Cdd:PRK11231 74 L----ARRLALLPQHHLtpegITVRELVAYGRSPW--LSLW-GRLSAEDNARVNQAMEQTRINHlADRRLTD----LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
250 260 270
....*....|....*....|....*....|..
gi 658548496 241 astllsaPQHPYTQRLL------DSEPSGDPV 266
Cdd:PRK11231 222 -------PEEVMTPGLLrtvfdvEAEIHPEPV 246
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-508 |
5.00e-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: 97.75 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHR 351
Cdd:COG0410 1 MPMLEVENLHAGY-----------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLpPRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQmlpvRPRM---QV-----VFqdpnsslnPRLSVlqiiEEGLRVhqpGLSAQQREQEVMRVMAEV----------- 412
Cdd:COG0410 70 LPPHR----IARLgigYVpegrrIF--------PSLTV----EENLLL---GAYARRDRAEVRADLERVyelfprlkerr 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 413 GLDAGTrhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRAL 492
Cdd:COG0410 131 RQRAGT-------LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEI 202
|
250
....*....|....*.
gi 658548496 493 CHQVIVLRQGEVVEQG 508
Cdd:COG0410 203 ADRAYVLERGRIVLEG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
5.18e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpsppvSYPQGDILFHGSSLlh 80
Cdd:PRK13648 3 DKNSIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE-----KVKSGEIFYNNQAI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 aDEHTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDclertgirnaakRLNDF 153
Cdd:PRK13648 74 -TDDNFEKLR-KHIGIVFQNPdnqfvgsIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE------------RADYE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKlADNVAVMQNG 233
Cdd:PRK13648 140 PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
250
....*....|...
gi 658548496 234 RCVEQNTASTLLS 246
Cdd:PRK13648 219 TVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
302-517 |
6.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDDMPLH-RWNRRQMLPVRPRMQVVFQDPNSSL 375
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPSSGTITIAGYHITpETGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRlSVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSS 455
Cdd:PRK13641 99 FEN-TVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 456 LDRTVQAQILALLKGLQ-EKHRLayIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQkAGHTV--ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
292-508 |
6.81e-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: 96.58 E-value: 6.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS-QGEIFFDDMPLHRWNRRQM--LPvrprmqvvf 368
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGKPLDIAARNRIgyLP--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 qdPNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:cd03269 77 --EERGLYPKMKVIDQLVYLAQLK--GLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 449 LDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
301-508 |
7.85e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.64 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLI-----ASQGEIFFDDMPLHRWNRRQM--LP-VRprmqvvfqdpn 372
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTT----IRIIlgilaPDSGEVLWDGEPLDPEDRRRIgyLPeER----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 sSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:COG4152 81 -GLYPKMKVGEQLVYLARLK--GLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 453 TSSLDrTVQAQILA-LLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4152 157 FSGLD-PVNVELLKdVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-257 |
8.16e-23 |
|
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: 99.11 E-value: 8.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 40 LVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHADEHtLRGIrgnkiAMIFQEpmVSLNPLHSLEKQ 114
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLagfeqPD------SGSIMLDGEDVTNVPPH-LRHI-----NMVFQS--YALFPHMTVEEN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 115 LYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQ 194
Cdd:TIGR01187 63 VAFGLKM-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 195 ILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQHPYTQRLL 257
Cdd:TIGR01187 139 MQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-238 |
9.11e-23 |
|
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: 95.46 E-value: 9.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILR-LLPSppvsypQGDILFHGSSLlhadeH 84
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQ------QGEITLDGVPV-----S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIRGNKIAMIFQEPMvslnplhslekqlyevlslhrgmrkeaargeildcLERTGIRNAAKRlndfphQLSGGERQR 164
Cdd:cd03247 68 DLEKALSSLISVLNQRPY-----------------------------------LFDTTLRNNLGR------RFSGGERQR 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRE-LRDElnmSLLFITHNLSIVRKlADNVAVMQNGRCVEQ 238
Cdd:cd03247 107 LALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLKDK---TLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
300-508 |
1.02e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 102.33 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGlallRLIA-----SQGEIFFDDMPlhrwnRRQMLPVRPRMQVVFQDPNSS 374
Cdd:TIGR03796 493 PLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIP-----REEIPREVLANSVAMVDQDIF 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 L-------NPRLSVLQIIEEGLRvhqpgLSAQQRE-QEVMRVM-----AEVGLDAgtrhrypAEFSGGQRQRIAIARALI 441
Cdd:TIGR03796 564 LfegtvrdNLTLWDPTIPDADLV-----RACKDAAiHDVITSRpggydAELAEGG-------ANLSGGQRQRLEIARALV 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 442 LKPELIILDEPTSSLDRTVQAQILALLKglqeKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
276-516 |
1.04e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPLHRWNR 354
Cdd:PRK11231 3 LRTENLTVGY-----------GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 355 RQmlpvrprmqvvfqdpnssLNPRLSVL-QI--IEEGLRVHQ-------PGLS-----AQQREQEVMRVMAEVGLDAGTR 419
Cdd:PRK11231 72 RQ------------------LARRLALLpQHhlTPEGITVRElvaygrsPWLSlwgrlSAEDNARVNQAMEQTRINHLAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 420 HRYpAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK11231 134 RRL-TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVL 211
|
250
....*....|....*..
gi 658548496 500 RQGEVVEQGECQRVFSA 516
Cdd:PRK11231 212 ANGHVMAQGTPEEVMTP 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
276-508 |
1.31e-22 |
|
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: 96.63 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIR----------KGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEI- 342
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-LKILSglLQPTSGEVr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 343 FFDDMPlhrWNRRQMLpvRPRMQVVFQDpNSSLNPRLSVLqiieEGLRVHQP--GLSAQQREQEVMRV--MAEVG--LDA 416
Cdd:cd03267 80 VAGLVP---WKRRKKF--LRRIGVVFGQ-KTQLWWDLPVI----DSFYLLAAiyDLPPARFKKRLDELseLLDLEelLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 417 GTRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:cd03267 150 PVR-----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRV 224
|
250
....*....|..
gi 658548496 497 IVLRQGEVVEQG 508
Cdd:cd03267 225 LVIDKGRLLYDG 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-234 |
1.43e-22 |
|
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: 96.03 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgeTRTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL--RLLPSppvsypQGDILFHGSSLlhade 83
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLtgELRPT------SGTAYINGYSI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRGNKIAMIFQEPMV--SLNPLHSLEkqLYevlSLHRGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGE 161
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDALfdELTVREHLR--FY---ARLKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
299-507 |
1.53e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.15 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDmplhrwnRR--QMLPVRPRMQVVFQdp 371
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAgleriTSGEIWIGG-------RVvnELEPADRDIAMVFQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRV--MAEVG--LDagtrhRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIR--GMPKAEIEERVAEAarILELEplLD-----RKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDlQV-VRALCHQVIVLRQGeVVEQ 507
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-QVeAMTLADRVVVMNGG-VAEQ 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
297-521 |
1.80e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDmplhrwnrRQMLPVRPRMQ---VVF 368
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAglediTSGDLFIGE--------KRMNDVPPAERgvgMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 QdpNSSLNPRLSVLQIIEEGLRVhqPGLSAQQREQEVMRVmAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELII 448
Cdd:PRK11000 82 Q--SYALYPHLSVAENMSFGLKL--AGAKKEEINQRVNQV-AEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 449 LDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRY 521
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
276-508 |
2.05e-22 |
|
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: 94.93 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKGILRRivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-------GEIFFDDMP 348
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGK-----QLLKNVSGKAKPGELTAIMGPSGAGKST----LLNALAGRrtglgvsGEVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRWNrrqmlpVRPRMQVVFQDpnSSLNPRLSVlqiiEEGLRVhqpglSAQQReqevmrvmaevGLdagtrhrypaefSG 428
Cdd:cd03213 75 LDKRS------FRKIIGYVPQD--DILHPTLTV----RETLMF-----AAKLR-----------GL------------SG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDL-QVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTI-ICSIHQPsSEIFELFDKLLLLSQGRVIYF 193
|
.
gi 658548496 508 G 508
Cdd:cd03213 194 G 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-247 |
2.40e-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: 96.31 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSYPQGDILfhGSSLLH 80
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGdlPPTYGNDVRLF--GERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLR---GIRGNKIAMIFQEPMVSLNPLHSlekQLYEVLSLHRGMrKEAARGEILDCLERTGIRNAAKRLndFpHQL 157
Cdd:COG1119 71 EDVWELRkriGLVSPALQLRFPRDETVLDVVLS---GFFDSIGLYREP-TDEQRERARELLELLGLAHLADRP--F-GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
250
....*....|
gi 658548496 238 QNTASTLLSA 247
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-237 |
2.60e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVsypQGDILFHGSSL 78
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAgfEQPT---AGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHADEHTlrgirgNKIAMIFQEpmVSLNPLHSLEKQLYEVLSLHRGMRKEAArGEILDCLERTGIRNAAKRLndfPHQLS 158
Cdd:PRK11607 84 SHVPPYQ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQEFAKRK---PHQLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
233-516 |
3.02e-22 |
|
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: 100.16 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 233 GRCVEQNTASTLLSAPQHPYTQrlldsepsgdPVPLAADstplLRVEDLSVSFPIRKgilrrivdQNPVLKNIRFSLRPG 312
Cdd:TIGR02204 309 ERLIELLQAEPDIKAPAHPKTL----------PVPLRGE----IEFEQVNFAYPARP--------DQPALDGLNLTVRPG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 313 ESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLhrwnrRQMLP--VRPRMQVVFQDPNSSLNprlSVLqiieEGL 389
Cdd:TIGR02204 367 ETVALVGPSGAGKSTLFQLLLRFYdPQSGRILLDGVDL-----RQLDPaeLRARMALVPQDPVLFAA---SVM----ENI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 390 RVHQPGLSAQQREQEVMRVMAE---VGLDAGTrHRYPAE----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQA 462
Cdd:TIGR02204 435 RYGRPDATDEEVEAAARAAHAHefiSALPEGY-DTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQ 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658548496 463 QILALLKGLQeKHRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:TIGR02204 514 LVQQALETLM-KGRTTLI-IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
4.16e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILR-------LLPSPPVsypQGDILFH 74
Cdd:PRK14243 7 TETVLRTENLNVYYGSF----LAVKNVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRV---EGKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 75 GSSLL--HADEHTLRgirgNKIAMIFQEPmvslNPLhslEKQLYEVLSLhrGMRKEAARGEILDCLERTgIRNAA----- 147
Cdd:PRK14243 76 GKNLYapDVDPVEVR----RRIGMVFQKP----NPF---PKSIYDNIAY--GARINGYKGDMDELVERS-LRQAAlwdev 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 148 -KRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVRKLADN 226
Cdd:PRK14243 142 kDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDM 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 658548496 227 VAVM---------QNGRCVEQNTASTLLSAPQHPYTQ 254
Cdd:PRK14243 220 TAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATR 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
276-508 |
4.20e-22 |
|
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: 94.92 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKgilrrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDD-----MPL 349
Cdd:cd03218 1 LRAENLSKRYGKRK-----------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGqditkLPM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 350 HRwnrrqmlpvRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGG 429
Cdd:cd03218 70 HK---------RARLGIGYLPQEASIFRKLTVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 430 QRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFIS-HDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL--KDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-247 |
5.57e-22 |
|
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: 99.51 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 15 FSTQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHADEHTLRGI 89
Cdd:COG5265 365 FGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVT------SGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 90 rgnkIAMIFQEPmvslnplhslekqlyeVL-------SLHRGmRKEAARGEIldclertgiRNAAK--RLNDF----PHQ 156
Cdd:COG5265 434 ----IGIVPQDT----------------VLfndtiayNIAYG-RPDASEEEV---------EAAARaaQIHDFieslPDG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 -----------LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLS-IVRklA 224
Cdd:COG5265 484 ydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStIVD--A 559
|
250 260
....*....|....*....|...
gi 658548496 225 DNVAVMQNGRCVEQNTASTLLSA 247
Cdd:COG5265 560 DEILVLEAGRIVERGTHAELLAQ 582
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
255-508 |
6.20e-22 |
|
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: 99.51 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 255 RLLDSEP----SGDPVPLAADStPLLRVEDlsVSF---PIRkgilrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKST 327
Cdd:COG5265 334 DLLDQPPevadAPDAPPLVVGG-GEVRFEN--VSFgydPER-----------PILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 328 TGLALLRLI-ASQGEIFFDDMPLhrwnrRQMLP--VRPRMQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPGLSaqqr 401
Cdd:COG5265 400 LARLLFRFYdVTSGRILIDGQDI-----RDVTQasLRAAIGIVPQDTvlfNDT----------IAYNIAYGRPDAS---- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 402 EQEVMRV--MA------------------EVGLdagtrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTV 460
Cdd:COG5265 461 EEEVEAAarAAqihdfieslpdgydtrvgERGL----------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDsRTE 530
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 658548496 461 QAqILALLKGLQEKHrlAYIFISHDLQ-VVRAlcHQVIVLRQGEVVEQG 508
Cdd:COG5265 531 RA-IQAALREVARGR--TTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-227 |
8.01e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.80 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILrllpsppvsypqgdilfhgsSLLHADE 83
Cdd:PRK09544 3 SLVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL--------------------GLVAPDE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRGNKIAMIFQEpmVSLNPlhSLEKQLYEVLSLHRGMRKeaarGEILDCLERTgirnAAKRLNDFPHQ-LSGGER 162
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPGTKK----EDILPALKRV----QAGHLIDAPMQkLSGGET 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNV 227
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
276-484 |
9.56e-22 |
|
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: 92.22 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIffdDMPLH 350
Cdd:cd03223 1 IELENLSLATP----------DGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALAglwpwGSGRI---GMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 rwNRRQMLPVRPRMqvvfqdPNSSLnprlsvlqiieeglrvhqpglsaqqREQEVmrvmaevgldagtrhrYP--AEFSG 428
Cdd:cd03223 64 --EDLLFLPQRPYL------PLGTL-------------------------REQLI----------------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglqeKHRLAYIFISH 484
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-527 |
1.20e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 285 FPIRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA------SQGEIFFDDMPLHRwnrRQML 358
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYS---PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 359 PVRPRMQV--VFQDPNSSlnPRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHR---YPAEFSGGQRQR 433
Cdd:PRK14267 80 PIEVRREVgmVFQYPNPF--PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 434 IAIARALILKPELIILDEPTSSLDRTVQAQILALLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
250
....*....|....
gi 658548496 514 FSAPTQRYTRQLLS 527
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-248 |
1.25e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 23 TVVTDLSLQIQPGETLALVGESGSGKSvsalSILRL---LPSPPvsypQGDILFHGSSLLHadehtlRGIRGNKIAMIFQ 99
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLvagLEKPT----EGQIFIDGEDVTH------RSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 100 E----PMVSL--NPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLT 173
Cdd:PRK11432 86 SyalfPHMSLgeNVGYGLKML---------GVPKEERKQRVKEALELVDLAGFEDRYVD---QISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 174 RPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAP 248
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-215 |
1.32e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.93 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIafsTQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPVSYpQGDILFHGSSLLHADEHt 85
Cdd:COG4136 2 LSLENLTI---TLGG-RPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIAGTLSPAFSA-SGEVLLNGRRLTALPAE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIrgnkiAMIFQEPMvsLNPLHSLEKQLyeVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRV 165
Cdd:COG4136 75 QRRI-----GILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITH 215
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
259-508 |
1.33e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.38 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 259 SEPSGDPVPLAADSTPLLRVEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIAS 338
Cdd:PRK11174 333 AHPQQGEKELASNDPVTIEAEDLEILSP----------DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 339 QGEIFFDDMPLHRWNRRQMlpvrpRMQV--VFQdpnsslNPRLsVLQIIEEGLRVHQPGLSAQQREQEVMRVMA------ 410
Cdd:PRK11174 403 QGSLKINGIELRELDPESW-----RKHLswVGQ------NPQL-PHGTLRDNVLLGNPDASDEQLQQALENAWVseflpl 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 411 -EVGLDAGTRHRyPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVV 489
Cdd:PRK11174 471 lPQGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDL 547
|
250
....*....|....*....
gi 658548496 490 RAlCHQVIVLRQGEVVEQG 508
Cdd:PRK11174 548 AQ-WDQIWVMQDGQIVQQG 565
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-512 |
1.40e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 97.94 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSYpQGDILFHGssllhaDEHTLRGIRGNK---IAMIFQEp 101
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKS----TLMKVLSGvyPHGSY-EGEILFDG------EVCRFKDIRDSEalgIVIIHQE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 102 mVSLNPLHSLEKQLYevlslhrgMRKEAARGEILDcLERTGIRNAA--KR--LNDFPHQLSG----GERQRVMIAMALLT 173
Cdd:NF040905 87 -LALIPYLSIAENIF--------LGNERAKRGVID-WNETNRRAREllAKvgLDESPDTLVTdigvGKQQLVEIAKALSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 174 RPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQntastlLSAPQHPYT 253
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET------LDCRADEVT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 254 Q--------------RLLDSEPS-GDPVplaadstplLRVEDLSVSFPIRKGilRRIVDqnpvlkNIRFSLRPGESLGLV 318
Cdd:NF040905 230 EdriirgmvgrdledRYPERTPKiGEVV---------FEVKNWTVYHPLHPE--RKVVD------DVSLNVRRGEIVGIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 319 GESGSGKstTGLALL-------RLIAsqGEIFFDDMPLHRWNRRQMLPV--------RPRMQVVFQDP---NSSLN--PR 378
Cdd:NF040905 293 GLMGAGR--TELAMSvfgrsygRNIS--GTVFKDGKEVDVSTVSDAIDAglayvtedRKGYGLNLIDDikrNITLAnlGK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LSVLQIIEEglrvhqpglsaqQREQEV-------MR-----VMAEVGldagtrhrypaEFSGGQRQRIAIARALILKPEL 446
Cdd:NF040905 369 VSRRGVIDE------------NEEIKVaeeyrkkMNiktpsVFQKVG-----------NLSGGNQQKVVLSKWLFTDPDV 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 447 IILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVeqGECQR 512
Cdd:NF040905 426 LILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRIT--GELPR 488
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
1.65e-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: 91.72 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAfstqgetrTVVTDLSLQIQPGETLALVGESGSGKS--VSALSILRllpsPPVSypqGDILFHGSSLLHA 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTelAEALFGLR----PPAS---GEITLDGKPVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DehtLRGIRGNKIAMIFQEPmvslnplhslekqlyevlsLHRGMrkeaargeildCLERTGIRNAAkrlndFPHQLSGGE 161
Cdd:cd03215 68 S---PRDAIRAGIAYVPEDR-------------------KREGL-----------VLDLSVAENIA-----LSSLLSGGN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
238-508 |
1.71e-21 |
|
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: 97.86 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 238 QNTASTLLSAPQHPYTqrLLDSEPSGDPVPLAAD-STPLLRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLG 316
Cdd:TIGR02203 294 NAPMQRGLAAAESLFT--LLDSPPEKDTGTRAIErARGDVEFRNVTFRYP---------GRDRPALDSISLVIEPGETVA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 317 LVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWN----RRQMLPVRprMQVVFQDPNSSLNPRLSVLQII--EEGL 389
Cdd:TIGR02203 363 LVGRSGSGKSTLVNLIPRFYePDSGQILLDGHDLADYTlaslRRQVALVS--QDVVLFNDTIANNIAYGRTEQAdrAEIE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 390 RVHQPGLSAQQREQEVMRVMAEVGLDAGtrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQIL 465
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGV-------LLSGGQRQRLAIARALLKDAPILILDEATSALDneseRLVQAALE 513
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 658548496 466 ALLKGlqekhRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR02203 514 RLMQG-----RTTLV-IAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
300-526 |
2.42e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 93.68 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEIFFDDMPLHRWNRRQMLPVRPRMQVVFQdpNSS 374
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQiapdhGEILFDGENIPAMSRSRLYTVRKRMSMLFQ--SGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHT-QLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 455 SLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQRyTRQLL 526
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-249 |
2.64e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 28 LSLQIQPGETLALVGESGSGKSVSAL---SILRllPSppvsypQGDILFHGSSLLHaDEHTLRGIRgNKIAMIFQEPMVS 104
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLhfnGILK--PT------SGEVLIKGEPIKY-DKKSLLEVR-KTVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 105 LNPLHSLEKQLYEVLSLhrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK13639 91 LFAPTVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 185 TALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQ 249
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-525 |
2.65e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.01 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 317 LVGESGSGKSTTGLALLRL------IASQGEIFFDDMPLhrWNRRQMLPVRPRMQVVFQDPNSSlnpRLSVLQIIEEGLR 390
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF---PMSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 391 VHQPGLSAQQREQEVMRvMAEVGLDAGTRHRY---PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILAL 467
Cdd:PRK14271 127 AHKLVPRKEFRGVAQAR-LTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 468 LKGLQEkhRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP----TQRYTRQL 525
Cdd:PRK14271 206 IRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYVAGL 265
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
301-509 |
2.66e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.38 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEI---FFDDMPLHRWNR------------------ 354
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlNAL----LLPDTGTIewiFKDEKNKKKTKEkekvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 355 RQMLPVRPRMQVVFQDPNSSLnprlsVLQIIEEGLrVHQP---GLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQR 431
Cdd:PRK13651 98 KKIKEIRRRVGVVFQFAEYQL-----FEQTIEKDI-IFGPvsmGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-236 |
3.05e-21 |
|
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: 91.46 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 21 TRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILR-LLPSPPVSypqGDILFHGSSLlhaDEHTLRGIrgnkIAMIFQ 99
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKS-TLLNALAgRRTGLGVS---GEVLINGRPL---DKRSFRKI----IGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 100 EPMvslnplhslekqLYEVLSLHRGMRKEAA-RGeildclertgirnaakrlndfphqLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03213 90 DDI------------LHPTLTVRETLMFAAKlRG------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 179 IADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSI-VRKLADNVAVMQNGRCV 236
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSeIFELFDKLLLLSQGRVI 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-215 |
3.28e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILR----LLPsppvsYPQGDILFHgssllha 81
Cdd:COG4178 363 LALEDLTLRTPDG---RPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWP-----YGSGRIARP------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 dehtlrgiRGNKIAMIFQEPMVslnPLHSLEKQLyevlsLHRGMRKEAARGEILDCLERTGIRNAAKRLN---DFPHQLS 158
Cdd:COG4178 424 --------AGARVLFLPQRPYL---PLGTLREAL-----LYPATAEAFSDAELREALEAVGLGHLAERLDeeaDWDQVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRElrdEL-NMSLLFITH 215
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELpGTTVISVGH 542
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
276-503 |
3.44e-21 |
|
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: 89.82 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQGEIffddmplhrwnrr 355
Cdd:cd03221 1 IELENLSKTY-----------GGKLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIAGELEP------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 356 qmlpvrprmqvvfqdpnsslnprlsvlqiiEEGlrvhqpglsaqqreqevmrvmaEVGLDAGTRHRYPAEFSGGQRQRIA 435
Cdd:cd03221 53 ------------------------------DEG----------------------IVTWGSTVKIGYFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 436 IARALILKPELIILDEPTSSLDrtVQAqILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLD--LES-IEALEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
278-508 |
3.75e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 278 VEDLSVSFPirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEIFFDDMPLHRWNRRQ 356
Cdd:PRK13647 7 VEDLHFRYK----------DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 mlpVRPRMQVVFQDPNSSLNPrLSVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAI 436
Cdd:PRK13647 77 ---VRSKVGLVFQDPDDQVFS-STVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMWD-FRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 437 ARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-234 |
3.78e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 91.85 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 29 SLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSllhadeHTLRGIRGNKIAMIFQEPmvslNPL 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPA----SGSIKVNDQS------HTGLAPYQRPVSMLFQEN----NLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 109 HSLEKQLYEVLSLHRGMRKEAARGE-ILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLKLNAEQQEkVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658548496 188 DVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-249 |
3.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.33 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKS-VSALSILRLLPSppvSYPQGDILFHGSSLl 79
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKStISKLINGLLLPD---DNPNSKITVDGITL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 haDEHTLRGIRgNKIAMIFQEP-------MVSLNPLHSLEkqlyevlslHRGMRKEAARGEILDCLERTGIRNAAKRLnd 152
Cdd:PRK13640 75 --TAKTVWDIR-EKVGIVFQNPdnqfvgaTVGDDVAFGLE---------NRAVPRPEMIKIVRDVLADVGMLDYIDSE-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 153 fPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVrKLADNVAVMQN 232
Cdd:PRK13640 141 -PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDD 218
|
250
....*....|....*..
gi 658548496 233 GRCVEQNTASTLLSAPQ 249
Cdd:PRK13640 219 GKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
302-514 |
4.89e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 4.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWNR-RQMLPVRPRMQVVFQDPNSSLNPRl 379
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKqKEIKPVRKKVGVVFQFPESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 SVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRT 459
Cdd:PRK13643 101 TVLKDVAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 460 VQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
5.53e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.62 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSL 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIagflaPS------SGEITLDGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LH--ADehtlRGIrgnkiamIFQEP--MVSLNPLHSLEkqlyevLSLH-RGMRKEAARGEILDCLERTGIRNAAKRlndF 153
Cdd:COG4525 72 TGpgAD----RGV-------VFQKDalLPWLNVLDNVA------FGLRlRGVPKAERRARAEELLALVGLADFARR---R 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITH 215
Cdd:COG4525 132 IWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
265-518 |
6.49e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 265 PVPLAADStpLLRVEDLSVSFPirkgilRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQ 339
Cdd:PRK13631 13 PNPLSDDI--ILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTlvthfNGL----IKSKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 340 GEIFFDDMPL--HRWNRRQMLP-----------VRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQEVM 406
Cdd:PRK13631 81 GTIQVGDIYIgdKKNNHELITNpyskkiknfkeLRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 407 RVMaevGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIfISHDL 486
Cdd:PRK13631 161 NKM---GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTM 236
|
250 260 270
....*....|....*....|....*....|..
gi 658548496 487 QVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK13631 237 EHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
254-516 |
6.77e-21 |
|
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: 95.88 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 254 QRLLDSEPSGDPVPLAADSTPLLRVEDLSVSFPIRKgilrrivdqNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLL 333
Cdd:TIGR01842 295 NELLANYPSRDPAMPLPEPEGHLSVENVTIVPPGGK---------KPTLRGISFSLQAGEALAIIGPSGSGKST----LA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 334 RLIA-----SQGEIFFDDMPLHRWNRRQM------LPvrprmQVV-------------FQDpnsSLNPRlsvlQIIEEGL 389
Cdd:TIGR01842 362 RLIVgiwppTSGSVRLDGADLKQWDRETFgkhigyLP-----QDVelfpgtvaeniarFGE---NADPE----KIIEAAK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 390 --RVHQPGLSAQQREQevmrvmAEVGlDAGtrhrypAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILAL 467
Cdd:TIGR01842 430 laGVHELILRLPDGYD------TVIG-PGG------ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 658548496 468 LKGLQEKHRLAyIFISHDLQVVrALCHQVIVLRQGEVVEQGECQRVFSA 516
Cdd:TIGR01842 497 IKALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-505 |
6.80e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.46 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPIRKgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLH 350
Cdd:COG1101 2 LELKNLSKTFNPGT------VNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAgslppDSGSILIDGKDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWN--RRQMLPVRprmqvVFQDPNSSLNPRLSvlqiIEE------------GLRvhqPGLSAQQREqEVMRVMAEVGLDA 416
Cdd:COG1101 72 KLPeyKRAKYIGR-----VFQDPMMGTAPSMT----IEEnlalayrrgkrrGLR---RGLTKKRRE-LFRELLATLGLGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 417 GTRHRYPAEF-SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQ 495
Cdd:COG1101 139 ENRLDTKVGLlSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNR 218
|
250
....*....|
gi 658548496 496 VIVLRQGEVV 505
Cdd:COG1101 219 LIMMHEGRII 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
7.16e-21 |
|
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: 90.66 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlPSPPVSypQGDILFHGSSLLHA--DE 83
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVT--EGEILFKGEDITDLppEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIrgnkiAMIFQEPMvslnplhslekqlyevlslhrgmrkeaargEIldclerTGIRNAaKRLNDFPHQLSGGERQ 163
Cdd:cd03217 74 RARLGI-----FLAFQYPP------------------------------EI------PGVKNA-DFLRYVNEGFSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKL-ADNVAVMQNGRCVE 237
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
7.39e-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: 91.37 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypqgdilfHGSSLLHADEHTLRGirgNKIAMIFQEpmVSLN 106
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQPT----------SGGVILEGKQITEPG---PDRMVVFQN--YSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLEKQLY-EVLSLHRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:TIGR01184 67 PWLTVRENIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658548496 186 ALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-236 |
1.16e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTqPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLH 80
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPT----SGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGNKIAMIFQEpmVSLNPlHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGG 160
Cdd:PRK10535 75 LDADALAQLRREHFGFIFQR--YHLLS-HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKlADNVAVMQNGRCV 236
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-524 |
1.19e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.64 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEI-------FFDD 346
Cdd:PRK14258 6 PAIKVNNLSFYY-----------DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrvegrveFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRwnRRQMLPVRPRMQVVFQDPNssLNPrLSVLQIIEEGLRV--HQPGLSAQQREQEVMRVmAEVGLDAGTR-HRYP 423
Cdd:PRK14258 75 NIYER--RVNLNRLRRQVSMVHPKPN--LFP-MSVYDNVAYGVKIvgWRPKLEIDDIVESALKD-ADLWDEIKHKiHKSA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL---- 499
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgne 228
|
250 260
....*....|....*....|....*.
gi 658548496 500 -RQGEVVEQGECQRVFSAPTQRYTRQ 524
Cdd:PRK14258 229 nRIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-234 |
1.33e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLsIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSppVSYPQGDILFHGSSLLHADE 83
Cdd:PRK11247 12 PLL-LNAVSKRYGE----RTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAG--LETPSAGELLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRgirgnkiaMIFQEpmVSLNPLhsleKQLYEVLSLH-RGMRKEAArgeiLDCLERTGIrnaAKRLNDFPHQLSGGER 162
Cdd:PRK11247 81 EDTR--------LMFQD--ARLLPW----KKVIDNVGLGlKGQWRDAA----LQALAAVGL---ADRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
300-514 |
1.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEIFFDDMPLHRWNR-RQMLPVRPRMQVVFQDPNSSLN 376
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTI-MQLLNglHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 377 PRlSVLQIIEEGLRvhQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13649 100 EE-TVLKDVAFGPQ--NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 457 DRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
302-505 |
1.79e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.93 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDP----N 372
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICgierpSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHhllmD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 SSLNPRLSVLQIIEeglrvhqpGLSAQQREQEVMRVMAEVGLDAGTRHrYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK10908 94 RTVYDNVAIPLIIA--------GASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 453 TSSLDRTVQAQILALlkgLQEKHRLA--YIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK10908 165 TGNLDDALSEGILRL---FEEFNRVGvtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-233 |
3.58e-20 |
|
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: 88.85 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSIAFstqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADehtl 86
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-----SGSILLNGKPIKAKE---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 87 rgiRGNKIAMIFQEPmvslnplhslEKQLYE--VLS-LHRGMRKEAARGEILDCLERTGIRNAAKRLNdfPHQLSGGERQ 163
Cdd:cd03226 69 ---RRKSIGYVMQDV----------DYQLFTdsVREeLLLGLKELDAGNEQAETVLKDLDLYALKERH--PLSLSGGQKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLfITHNLSIVRKLADNVAVMQNG 233
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANG 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
300-509 |
3.87e-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: 94.04 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNR---RQMLPVRPRMQVVFQDpnssl 375
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDIDRhtlRQFINYLPQEPYIFSG----- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 nprlsvlQIIEEGLRVHQPGLSaqqrEQEVMRV--MAEVGLD-----AGTRHRYPAE---FSGGQRQRIAIARALILKPE 445
Cdd:TIGR01193 563 -------SILENLLLGAKENVS----QDEIWAAceIAEIKDDienmpLGYQTELSEEgssISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 446 LIILDEPTSSLDRTVQAQILALLKGLQEKhrlAYIFISHDLQVVRaLCHQVIVLRQGEVVEQGE 509
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGS 691
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-275 |
3.92e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFstqGETrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHGSSLLHADE 83
Cdd:PRK09536 2 PMIDVSDLSVEF---GDT-TVLDGVDLSVREGSLVGLVGPNGAGKT----TLLRAINGT-LTPTAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLrgirGNKIAMIFQEPMVSLNplHSLEKQLYEVLSLHRG---MRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGG 160
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLSFE--FDVRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQFADRPVT---SLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFItHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGP 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 658548496 241 ASTLLSAPqhpyTQR-LLDSEP--SGDPVPLAADSTPL 275
Cdd:PRK09536 223 PADVLTAD----TLRaAFDARTavGTDPATGAPTVTPL 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
301-517 |
4.04e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.25 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-----LIASQGEIFFDDMPLHRWNRRQmlpVRPRMQVVFQDPNSSL 375
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKST----LFRhfngiLKPTSGSVLIRGEPITKENIRE---VRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 -NPrlSVLQIIEEGlrvhqP---GLSAQQREQEVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK13652 92 fSP--TVEQDIAFG-----PinlGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAP 517
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
275-511 |
4.61e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEIFFDDMP------ 348
Cdd:PRK09984 4 IIRVEKLAKTF-----------NQHQALHAVDLNIHHGEMVALLGPSGSGKST----LLRHLS--GLITGDKSAgshiel 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 ----LHRWNR--RQMLPVRPRMQVVFQDPNssLNPRLSVLQIIEEGLRVHQP------GLSAQQREQEVMRVMAEVGLdA 416
Cdd:PRK09984 67 lgrtVQREGRlaRDIRKSRANTGYIFQQFN--LVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGM-V 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 417 GTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQV 496
Cdd:PRK09984 144 HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERI 223
|
250
....*....|....*
gi 658548496 497 IVLRQGEVVEQGECQ 511
Cdd:PRK09984 224 VALRQGHVFYDGSSQ 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-512 |
6.14e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.67 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSppVSYPQGdilfhGSSLLHA 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGV----KALDDISFDCRAGQVHALMGENGAGKS----TLLKILSG--NYQPDA-----GSILIDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRGIR---GNKIAMIFQEpmvslnpLHSL-EKQLYEVLSL----HRG--MRKEAARGEILDCLERTGIR-NAAKRL 150
Cdd:PRK11288 66 QEMRFASTTaalAAGVAIIYQE-------LHLVpEMTVAENLYLgqlpHKGgiVNRRLLNYEAREQLEHLGVDiDPDTPL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 151 NDfphqLSGGERQRVMIAMALLtRPELLIA-DEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAV 229
Cdd:PRK11288 139 KY----LSIGQRQMVEIAKALA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 230 MQNGRCVE------QNTASTLLSAP-----QHPYTQRlldSEPSGDpvplaadstPLLRVEDLsvsfpirkgilrrivdQ 298
Cdd:PRK11288 213 FKDGRYVAtfddmaQVDRDQLVQAMvgreiGDIYGYR---PRPLGE---------VRLRLDGL----------------K 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 299 NPVLKN-IRFSLRPGESLGLVGESGSGKSttglALLRLI-----ASQGEIFFDDMPLHRWNRRQ------ML-------- 358
Cdd:PRK11288 265 GPGLREpISFSVRAGEIVGLFGLVGAGRS----ELMKLLygatrRTAGQVYLDGKPIDIRSPRDairagiMLcpedrkae 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 359 ---PVRPrmqvVFQDPNSS-----------LNPR----LSVLQIieEGLRVHQPGlsaqqREQEVMRVmaevgldagtrh 420
Cdd:PRK11288 341 giiPVHS----VADNINISarrhhlragclINNRweaeNADRFI--RSLNIKTPS-----REQLIMNL------------ 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 421 rypaefSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLR 500
Cdd:PRK11288 398 ------SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMR 470
|
570
....*....|..
gi 658548496 501 QGEVVeqGECQR 512
Cdd:PRK11288 471 EGRIA--GELAR 480
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
278-508 |
7.99e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 278 VEDLSVSFPIR----------KGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTT-----GLallrLIASQGEI 342
Cdd:COG4586 4 VENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltGI----LVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 343 FFDDM-PlhrWNRRQMLpVRpRMQVVF-QdpNSSLNPRLSVLqiieEGLRVHQP--GLSAQQREQEvMRVMAEVgLDAG- 417
Cdd:COG4586 80 RVLGYvP---FKRRKEF-AR-RIGVVFgQ--RSQLWWDLPAI----DSFRLLKAiyRIPDAEYKKR-LDELVEL-LDLGe 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 418 -----TRhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRAL 492
Cdd:COG4586 147 lldtpVR-----QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250
....*....|....*.
gi 658548496 493 CHQVIVLRQGEVVEQG 508
Cdd:COG4586 222 CDRVIVIDHGRIIYDG 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-234 |
8.09e-20 |
|
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: 86.89 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSiaFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHT 85
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PTS---GRVRLDGADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIrgnkIAMIFQEpmvslnplhsleKQLYEvlslhrgmrkeaarGEILDCLertgirnaakrlndfphqLSGGERQRV 165
Cdd:cd03246 74 LGDH----VGYLPQD------------DELFS--------------GSIAENI------------------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRkLADNVAVMQNGR 234
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLA-SADRILVLEDGR 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
274-508 |
8.25e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSFPIRkgilrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTT-----GLallrLIASQGEIFFDD-- 346
Cdd:COG1137 2 MTLEAENLVKSYGKR-----------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymivGL----VKPDSGRIFLDGed 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 ---MPLHRwnRRQM----LPvrprmqvvfQDPnsSLNPRLSVLQIIEEGLRVHqpGLSAQQREQEVMRVMAEVGLdAGTR 419
Cdd:COG1137 67 ithLPMHK--RARLgigyLP---------QEA--SIFRKLTVEDNILAVLELR--KLSKKEREERLEELLEEFGI-THLR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLqeKHRLAYIFIS-HDlqvVR---ALCHQ 495
Cdd:COG1137 131 KSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL--KERGIGVLITdHN---VRetlGICDR 205
|
250
....*....|...
gi 658548496 496 VIVLRQGEVVEQG 508
Cdd:COG1137 206 AYIISEGKVLAEG 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-249 |
8.31e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.69 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFhGSSLLHA--DEHTLRGIRgNKIAMIFQ 99
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKS-TLLQHLNGLLQPT----SGTVTI-GERVITAgkKNKKLKPLR-KKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 100 EPmvslnplhslEKQLYE--VLS------LHRGMRKEAARGEILDCLERTGIrnAAKRLNDFPHQLSGGERQRVMIAMAL 171
Cdd:PRK13634 93 FP----------EHQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 172 LTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQ 249
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-249 |
8.75e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.74 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 28 LSLQIQPGETLALVGESGSGKSvSALSILR-LLPSppvsypQGDILFHGSSLLHADEHTLRGIRgnkiAMIFQEPMvsln 106
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMAgLLPG------QGEILLNGRPLSDWSAAELARHR----AYLSQQQS---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLekQLYEVLSLHR--GMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALLT-------RPEL 177
Cdd:COG4138 80 PPFAM--PVFQYLALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 178 LIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQ 249
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-234 |
1.06e-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: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSVSALSILRL-LPSppvsypQGDILFHGSSLLHADEHTLRGIRgNKIAMIFQEP--MV 103
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPT------SGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFrlLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 SLNPLHSLEKQLYEVLSLHRGMRKEAArgeilDCLERTGIRNaakRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVP-----AALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658548496 184 TTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-217 |
1.07e-19 |
|
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: 92.04 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTLRGIrgnkIAMIFQEPmv 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPVSSLDQDEVRRR----VSVCAQDA-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 slnplHSLEKQLYEVLSLHRGmrkEAARGEILDCLERTGIRNAAKRLNDFPH--------QLSGGERQRVMIAMALLTRP 175
Cdd:TIGR02868 419 -----HLFDTTVRENLRLARP---DATDEELWAALERVGLADWLRALPDGLDtvlgeggaRLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658548496 176 ELLIADEPTTALDVTVQAQILTLLRELRDELnmSLLFITHNL 217
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-234 |
1.07e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.70 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQ---PGETL-ALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHGSSLLHADEHTLRGIRGNKIAMIFQEpm 102
Cdd:PRK11144 12 DLCLTVNltlPAQGItAIFGRSGAGKT-SLINAISGLTRPQ----KGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 VSLNPLHSLEKqlyevlSLHRGMRKEAaRGEILDCLERTGIRNAAKRlndFPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:PRK11144 85 ARLFPHYKVRG------NLRYGMAKSM-VAQFDKIVALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658548496 183 PTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-249 |
1.26e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.12 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 15 FSTQGetrtvVTDLSLQIQPGETLALVGESGSGKSV-----SALsilrLLPSppvsypQGDILFHGSSL-LHADEHTLRG 88
Cdd:PRK13641 18 MEKKG-----LDNISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPS------SGTITIAGYHItPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 89 IRgNKIAMIFQEPmvslnplhslEKQLYE--VLS------LHRGMRKEAARGEILDCLERTGIRNAAkrLNDFPHQLSGG 160
Cdd:PRK13641 83 LR-KKVSLVFQFP----------EAQLFEntVLKdvefgpKNFGFSEDEAKEKALKWLKKVGLSEDL--ISKSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHAS 228
|
....*....
gi 658548496 241 ASTLLSAPQ 249
Cdd:PRK13641 229 PKEIFSDKE 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-238 |
1.27e-19 |
|
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: 87.25 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGeTLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHGSSLLhADE 83
Cdd:cd03264 1 LQLENLTKRYGK----KRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILATltPPSS---GTIRIDGQDVL-KQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIrgnkIAMIFQEPMVSlnPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQ 163
Cdd:cd03264 68 QKLRRR----IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKK---IGSLSGGMRR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:cd03264 138 RVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
267-518 |
2.32e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.92 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 267 PLAADSTplLRVEDLSVSFPIRKgilrrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGE 341
Cdd:PRK10575 5 TNHSDTT--FALRNVSFRVPGRT-----------LLHPLSLTFPAGKVTGLIGHNGSGKST----LLKMLgrhqpPSEGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 342 IFFDDMPLHRWNRR----------QMLPVRPRMqvvfqdpnsslnprlSVLQIIEEGlRVHQPG----LSAQQREQeVMR 407
Cdd:PRK10575 68 ILLDAQPLESWSSKafarkvaylpQQLPAAEGM---------------TVRELVAIG-RYPWHGalgrFGAADREK-VEE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 408 VMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQ 487
Cdd:PRK10575 131 AISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDIN 209
|
250 260 270
....*....|....*....|....*....|.
gi 658548496 488 VVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK10575 210 MAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
10-269 |
2.41e-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: 91.49 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 10 NLSIAFSTQGetrtvVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHGSSLLHADEHTLRgi 89
Cdd:TIGR01192 341 TFEFANSSQG-----VFDVSFEAKAGQTVAIVGPTGAGKT-TLINLLQRVYDPTV----GQILIDGIDINTVTRESLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 90 rgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRN-AAKRLNDFP-------HQLSGGE 161
Cdd:TIGR01192 409 --KSIATVFQDAGL-------FNRSIRENIRLGR---EGATDEEVYEAAKAAAAHDfILKRSNGYDtlvgergNRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTA 241
Cdd:TIGR01192 477 RQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSF 553
|
250 260 270
....*....|....*....|....*....|..
gi 658548496 242 STLLSAPQHPY----TQRLLDSEPSGDPVPLA 269
Cdd:TIGR01192 554 QELIQKDGRFYkllrRSGLLTNQPATKPLRKA 585
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
276-508 |
2.75e-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: 86.81 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDD---- 346
Cdd:TIGR03410 1 LEVSNLNVYY-----------GQSHILRGVSLEVPKGEVTCVLGRNGVGKTT----LLKTLmgllpVKSGSIRLDGedit 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 -MPLHRWNRRQMLPVrPRMQVVFqdpnsslnPRLSVlqiiEEGLRVhqpGLSAQQREQE-----------VMRVMaevgl 414
Cdd:TIGR03410 66 kLPPHERARAGIAYV-PQGREIF--------PRLTV----EENLLT---GLAALPRRSRkipdeiyelfpVLKEM----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 415 dagtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCH 494
Cdd:TIGR03410 125 ----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELAD 200
|
250
....*....|....
gi 658548496 495 QVIVLRQGEVVEQG 508
Cdd:TIGR03410 201 RYYVMERGRVVASG 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-254 |
2.75e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 13 IAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppvsYP--QGDILFHGSSLlhaDEHTLRGIR 90
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF-------YDidEGEILLDGHDL---RDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 91 gNKIAMIFQEpmVSL------NPLHSLEKQLYEvlslhRGMRKEAARG----EILDCLER---TGI-RNAAkrlndfphQ 156
Cdd:PRK11176 417 -NQVALVSQN--VHLfndtiaNNIAYARTEQYS-----REQIEEAARMayamDFINKMDNgldTVIgENGV--------L 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKlADNVAVMQNGRCV 236
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
250
....*....|....*...
gi 658548496 237 EQNTASTLLsAPQHPYTQ 254
Cdd:PRK11176 558 ERGTHAELL-AQNGVYAQ 574
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-234 |
4.21e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.06 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAF--STQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL--RLLPSppvsypQGDILFHGSSLLHA 81
Cdd:COG1101 2 LELKNLSKTFnpGTVNE-KRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIagSLPPD------SGSILIDGKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHtlrgIRGNKIAMIFQEPMVSLNPLHSLEKQLyeVLSLHRGMR-------KEAARGEILDCLERTGIrNAAKRLNDFP 154
Cdd:COG1101 74 PEY----KRAKYIGRVFQDPMMGTAPSMTIEENL--ALAYRRGKRrglrrglTKKRRELFRELLATLGL-GLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
298-508 |
4.29e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 298 QNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNRRQMlpvrpRMQVVFQDPNSSL- 375
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYdIDEGEILLDGHDLRDYTLASL-----RNQVALVSQNVHLf 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 ------------NPRLSVLQIIEEGLRVHQPGLsAQQREQEVMRVMAEVGldagtrhrypAEFSGGQRQRIAIARALILK 443
Cdd:PRK11176 430 ndtianniayarTEQYSREQIEEAARMAYAMDF-INKMDNGLDTVIGENG----------VLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 444 PELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIfISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQ-KNRTSLV-IAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-234 |
6.57e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.70 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHADEHTLRGIRgNKIAM 96
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLIcgierPS------AGKIWFSGHDITRLKNREVPFLR-RQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 97 IFQEpmvslnplHSL--EKQLYEVLSLH---RGMRKEAARGEILDCLERTGIRNAAKrlnDFPHQLSGGERQRVMIAMAL 171
Cdd:PRK10908 84 IFQD--------HHLlmDRTVYDNVAIPliiAGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 172 LTRPELLIADEPTTALDVTVQAQILTLLRELrDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-238 |
6.83e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.47 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHG 75
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIagfetPD------SGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 SSLLHAD-EHtlrgirgNKIAMIFQEpmVSLNPLHSLekqlYEVLSLHRGMRKEAARgEIldcleRTGIRNAAK--RLND 152
Cdd:PRK09452 76 QDITHVPaEN-------RHVNTVFQS--YALFPHMTV----FENVAFGLRMQKTPAA-EI-----TPRVMEALRmvQLEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 153 F----PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVA 228
Cdd:PRK09452 137 FaqrkPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIV 216
|
250
....*....|
gi 658548496 229 VMQNGRcVEQ 238
Cdd:PRK09452 217 VMRDGR-IEQ 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-254 |
6.89e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSLLHADE 83
Cdd:PRK14258 6 PAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRgnKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhrGMRKEAargEILDCLErTGIRNA------AKRLNDFPHQL 157
Cdd:PRK14258 82 NLNRLRR--QVSMVHPKP--NLFPMSVYDNVAYGVKIV--GWRPKL---EIDDIVE-SALKDAdlwdeiKHKIHKSALDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQN----- 232
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenri 231
|
250 260
....*....|....*....|..
gi 658548496 233 GRCVEQNTASTLLSAPQHPYTQ 254
Cdd:PRK14258 232 GQLVEFGLTKKIFNSPHDSRTR 253
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
274-504 |
7.10e-19 |
|
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: 84.41 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVSfpirkgilrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTTGLAL--LRLIASqGEIFFDDMPLHR 351
Cdd:cd03215 3 PVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALfgLRPPAS-GEITLDGKPVTR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQMlpVRPRMQVVFQDPNSS-LNPRLSVLQIIeeGLRVHqpglsaqqreqevmrvmaevgldagtrhrypaeFSGGQ 430
Cdd:cd03215 67 RSPRDA--IRAGIAYVPEDRKREgLVLDLSVAENI--ALSSL---------------------------------LSGGN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-236 |
8.42e-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: 85.33 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 13 IAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHG--SSLLHADEht 85
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS----TLLKLLaglykPT------SGSVLLDGtdIRQLDPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 lrgIRGNkIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRNAAKRLndfPH---------- 155
Cdd:cd03245 76 ---LRRN-IGYVPQDVTL-------FYGTLRDNITLGAPLADDE---RILRAAELAGVTDFVNKH---PNgldlqigerg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 -QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVrKLADNVAVMQNGR 234
Cdd:cd03245 139 rGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLL-DLVDRIIVMDSGR 215
|
..
gi 658548496 235 CV 236
Cdd:cd03245 216 IV 217
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-508 |
9.09e-19 |
|
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: 85.29 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 307 FSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPlHRWNRRQMLPVRPRMQVVFQDPnsslnprLSVLQII 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKVAGAS-PGKGWRHIGYVPQRHEFAWDFP-------ISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 386 EEGlRVHQPGLSAQQREQE---VMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQA 462
Cdd:TIGR03771 73 MSG-RTGHIGWLRRPCVADfaaVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658548496 463 QILALLKGL-QEKHrlAYIFISHDLQVVRALCHQViVLRQGEVVEQG 508
Cdd:TIGR03771 151 LLTELFIELaGAGT--AILMTTHDLAQAMATCDRV-VLLNGRVIADG 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-457 |
9.57e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 88.92 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 20 ETRTVVTDlSLQIQPGETLALVGESGSGKSVSALSIlrllpsppvsypqgdilfHGSSLLhadehtLRGIRGNKiamiFQ 99
Cdd:PRK10938 15 DTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARAL------------------AGELPL------LSGERQSQ----FS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 100 EP-MVSLNPLHSLEKQLYE-----VLSLHRGMRKEAARGEILD-------CLERTGIRNAAKRLNDFPHQLSGGERQRVM 166
Cdd:PRK10938 66 HItRLSFEQLQKLVSDEWQrnntdMLSPGEDDTGRTTAEIIQDevkdparCEQLAQQFGITALLDRRFKYLSTGETRKTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 167 IAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 247 ---APQHPYTQRLLDS------EPSGDPvPLAADsTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGL 317
Cdd:PRK10938 225 qalVAQLAHSEQLEGVqlpepdEPSARH-ALPAN-EPRIVLNNGVVSY-----------NDRPILHNLSWQVNPGEHWQI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 318 VGESGSGKSTtglaLLRLIAS---QGeiFFDDMPLhrWNRRQ-----MLPVRPRMQVVfqdpNSSL--NPRLS--VLQII 385
Cdd:PRK10938 292 VGPNGAGKST----LLSLITGdhpQG--YSNDLTL--FGRRRgsgetIWDIKKHIGYV----SSSLhlDYRVStsVRNVI 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 386 EEG----LRVHQPGLSAQQreQEVMRVMAEVGLDAGTRHRYPAEFSGGQrQRIA-IARALILKPELIILDEPTSSLD 457
Cdd:PRK10938 360 LSGffdsIGIYQAVSDRQQ--KLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-247 |
1.10e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 2 TQPLLS----IDNLSIAFSTQgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsYPQGDILFHG-- 75
Cdd:PRK10790 333 DRPLQSgridIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGrp 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 -SSLLHAdehTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAargeILDCLERTGIRNAAKRLNDFP 154
Cdd:PRK10790 405 lSSLSHS---VLR----QGVAMVQQDPVV-------LADTFLANVTLGRDISEEQ----VWQALETVQLAELARSLPDGL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 H--------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLS-IVRklAD 225
Cdd:PRK10790 467 YtplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStIVE--AD 542
|
250 260
....*....|....*....|..
gi 658548496 226 NVAVMQNGRCVEQNTASTLLSA 247
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAA 564
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-249 |
1.22e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQGETRTVvTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEH 84
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRgirgNKIAMIFQEP-------MVSLNPLHSLEKQlyevlslhrGMRKEAARGEILDCLERTGIRNAAKRLndfPHQL 157
Cdd:PRK13642 78 NLR----RKIGMVFQNPdnqfvgaTVEDDVAFGMENQ---------GIPREEMIKRVDEALLAVNMLDFKTRE---PARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKlADNVAVMQNGRCVE 237
Cdd:PRK13642 142 SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
250
....*....|..
gi 658548496 238 QNTASTLLSAPQ 249
Cdd:PRK13642 221 EAAPSELFATSE 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
297-508 |
1.46e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.13 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMlpVRpRMQVVFQDP 371
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKST----LLSMISrllppDSGEVLVDGLDVATTPSREL--AK-RLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NssLNPRLSVLQIIEEGLRVHQPG-LSAQQREQeVMRVMAEVGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILD 450
Cdd:COG4604 85 H--INSRLTVRELVAFGRFPYSKGrLTAEDREI-IDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 451 EPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
302-508 |
1.49e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS--------QGEIFFDDMPLhrwNRRQMlpvRPRMQVVFQDpns 373
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTT----LMNALAFrspkgvkgSGSVLLNGMPI---DAKEM---RAISAYVQQD--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 374 SLN-PRLSVLQ--IIEEGLRVHQPgLSAQQREQEVMRVMAEVGLD--AGTRHRYPAE---FSGGQRQRIAIARALILKPE 445
Cdd:TIGR00955 108 DLFiPTLTVREhlMFQAHLRMPRR-VTKKEKRERVDEVLQALGLRkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 446 LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-237 |
1.51e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSIL-RllPSPPVSypQGDILFHGSSLLH--AD 82
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgH--PKYEVT--SGSILLDGEDILElsPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGIrgnkiAMIFQEPM----VSL-NPLH-SLEKQLYEVLSLhrgmrkEAARGEILDCLERTGIRNA-AKR-LNDfp 154
Cdd:COG0396 73 ERARAGI-----FLAFQYPVeipgVSVsNFLRtALNARRGEELSA------REFLKLLKEKMKELGLDEDfLDRyVNE-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 hQLSGGERQRVMIA-MALLtRPELLIADEPTTALDVTVqAQILT-LLRELRDElNMSLLFITHNLSIVRKL-ADNVAVMQ 231
Cdd:COG0396 140 -GFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIDA-LRIVAeGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLV 215
|
....*.
gi 658548496 232 NGRCVE 237
Cdd:COG0396 216 DGRIVK 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
277-492 |
1.78e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFpirkGILRRIVdQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIasqgeiffddmplhrWNRRQ 356
Cdd:COG2401 26 RVAIVLEAF----GVELRVV-ERYVLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL---------------AGALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 MLPVrprmQVVFQDPNSSLNPRLSVLQIIeegLRVHQPGlsaqqreqEVMRVMAEVGL-DAGTRHRYPAEFSGGQRQRIA 435
Cdd:COG2401 82 GTPV----AGCVDVPDNQFGREASLIDAI---GRKGDFK--------DAVELLNAVGLsDAVLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 436 IARALILKPELIILDEPTSSLDRTVqAQILAllKGLQE---KHRLAYIFISHDLQVVRAL 492
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQT-AKRVA--RNLQKlarRAGITLVVATHHYDVIDDL 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-236 |
1.96e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 14 AFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKS--VSALSILR---LLPSPPV----------------SYPQGDIL 72
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTtlMNALAFRSpkgVKGSGSVllngmpidakemraisAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 73 FHGSslLHADEHtlrgirgnkiaMIFQEpmvslnplhslekqlyeVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLND 152
Cdd:TIGR00955 110 FIPT--LTVREH-----------LMFQA-----------------HLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 153 FPHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAV 229
Cdd:TIGR00955 160 VPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
....*..
gi 658548496 230 MQNGRCV 236
Cdd:TIGR00955 240 MAEGRVA 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
301-516 |
2.48e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQ-GEIFFDDMPLHRWNRRQmlpVRPRMQVVFQdpNSSLNPRL 379
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAhGHVWLDGEHIQHYASKE---VARRIGLLAQ--NATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 SVLQIIEEGLRVHQPGLSAQQREQE--VMRVMAEVGLDAGTRHRYPAeFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK10253 97 TVQELVARGRYPHQPLFTRWRKEDEeaVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 458 RTVQAQILALLKGLQEKHRLAYIFISHDL-QVVRALCHqVIVLRQGEVVEQGECQRVFSA 516
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASH-LIALREGKIVAQGAPKEIVTA 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
273-505 |
2.55e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPIRKGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL---------IASQGEIF 343
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVE-------VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLdkptsgtyrVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 344 FDDMPLHRWNRRQMlpvrprmQVVFQdpNSSLNPRLSVLQIIEegLRVHQPGLSAQQREQEVMRVMAEVGLdaGTRHRY- 422
Cdd:PRK10535 75 LDADALAQLRREHF-------GFIFQ--RYHLLSHLTAAQNVE--VPAVYAGLERKQRLLRAQELLQRLGL--EDRVEYq 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 423 PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEK-HRLayIFISHDLQVVrALCHQVIVLRQ 501
Cdd:PRK10535 142 PSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTV--IIVTHDPQVA-AQAERVIEIRD 218
|
....
gi 658548496 502 GEVV 505
Cdd:PRK10535 219 GEIV 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
269-527 |
2.97e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.83 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLR-------LIAS--- 338
Cdd:PRK14243 4 LNGTETVLRTENLNVYY-----------GSFLAVKNVWLDIPKNQITAFIGPSGCGKST----ILRcfnrlndLIPGfrv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 339 QGEIFFDDMPLHRwNRRQMLPVRPRMQVVFQDPNS---------SLNPRLSVLQ-----IIEEGLRvhQPGLSaqqreQE 404
Cdd:PRK14243 69 EGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPfpksiydniAYGARINGYKgdmdeLVERSLR--QAALW-----DE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 405 VMRVMAEVGLdagtrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISH 484
Cdd:PRK14243 141 VKDKLKQSGL----------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTH 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 658548496 485 DLQVVRALCHQVIVL---------RQGEVVEQGECQRVFSAPTQRYTRQLLS 527
Cdd:PRK14243 209 NMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-248 |
3.17e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 38 LALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHTLRGIRGnkiaMIFQEPMVSLnpLHSLEKQLYE 117
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILK--PTS---GSVLIRGEPITKENIREVRKFVG----LVFQNPDDQI--FSPTVEQDIA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 118 VLSLHRGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILT 197
Cdd:PRK13652 102 FGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 658548496 198 LLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAP 248
Cdd:PRK13652 179 FLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
276-508 |
3.18e-18 |
|
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: 84.23 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEIFFDDMPLHrw 352
Cdd:TIGR01978 1 LKIKDLHVS-----------VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGQDLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 353 nrrQMLP---VRPRMQVVFQDPNSSlnPRLSVLQIIEEGLRVH-----QPGLSAQQREQEVMRVMAEVGLDAGTRHRYPA 424
Cdd:TIGR01978 68 ---ELEPderARAGLFLAFQYPEEI--PGVSNLEFLRSALNARrsargEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 E-FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI-VLRQG 502
Cdd:TIGR01978 143 EgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKPDYVhVLLDG 221
|
....*.
gi 658548496 503 EVVEQG 508
Cdd:TIGR01978 222 RIVKSG 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-527 |
3.30e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.49 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 223 LADNVAVMQNGRCVEQ----NTASTLLSAP------------QHPYTQRLLDS-EPSGDPVPLAADSTPLLRVEDLSVSF 285
Cdd:PLN03232 1150 LTATFAVLRNGNAENQagfaSTMGLLLSYTlnittllsgvlrQASKAENSLNSvERVGNYIDLPSEATAIIENNRPVSGW 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 286 PIRKGI------LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRW---NRR 355
Cdd:PLN03232 1230 PSRGSIkfedvhLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRIMIDDCDVAKFgltDLR 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 356 QMLPVRPRMQVVFQ-------DPNSSLNPRlSVLQIIEeglRVHQpglsaqqreQEVMRvMAEVGLDAGTRHRyPAEFSG 428
Cdd:PLN03232 1310 RVLSIIPQSPVLFSgtvrfniDPFSEHNDA-DLWEALE---RAHI---------KDVID-RNPFGLDAEVSEG-GENFSV 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYD 1451
|
330
....*....|....*....
gi 658548496 509 ECQRVFSAPTQRYTRQLLS 527
Cdd:PLN03232 1452 SPQELLSRDTSAFFRMVHS 1470
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
274-468 |
4.07e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 274 PLLRVEDLSVsfpIRKGILrrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMP 348
Cdd:PRK13539 1 MMLEGEDLAC---VRGGRV--------LFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLIAgllppAAGTIKLDGGD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHrwnrrqmLPvRPRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpglsaqQREQEVMRVMAEVGLdAGTRHRYPAEFSG 428
Cdd:PRK13539 66 ID-------DP-DVAEACHYLGHRNAMKPALTVAENLEFWAAFLG------GEELDIAAALEAVGL-APLAHLPFGYLSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALL 468
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-236 |
4.66e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 15 FSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILR--LLPSppvsypQGDILFHGSSLlHADEHTLRgirgN 92
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgiLVPT------SGEVRVLGYVP-FKRRKEFA----R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 93 KIAMIF---QEPMVSLNPLHSLE--KQLYEV-LSLHRGMRKEAArgEILDclertgirnaakrLNDFPH----QLSGGER 162
Cdd:COG4586 96 RIGVVFgqrSQLWWDLPAIDSFRllKAIYRIpDAEYKKRLDELV--ELLD-------------LGELLDtpvrQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-237 |
4.99e-18 |
|
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: 82.46 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLLHADEHT 85
Cdd:cd03369 7 IEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRF-----LEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRgirgNKIAMIFQEPMV-------SLNPL-HSLEKQLYEVLSLHRGmrkeaarGEildclertgirnaakrlndfphQL 157
Cdd:cd03369 80 LR----SSLTIIPQDPTLfsgtirsNLDPFdEYSDEEIYGALRVSEG-------GL----------------------NL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKLaDNVAVMQNGRCVE 237
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
271-485 |
5.39e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.84 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 271 DSTPLLRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEIFFD 345
Cdd:PRK10247 3 ENSPLLQLQNVGYL-----------AGDAKILNNISFSLRAGEFKLITGPSGCGKST----LLKIVASlisptSGTLLFE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNrrqmlPVRPRMQV--VFQDP---NSSLNPRLsvlqIIEEGLRVHQPglsaqqREQEVMRVMAEVGLDAGTRH 420
Cdd:PRK10247 68 GEDISTLK-----PEIYRQQVsyCAQTPtlfGDTVYDNL----IFPWQIRNQQP------DPAIFLDDLERFALPDTILT 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHD 485
Cdd:PRK10247 133 KNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
131-486 |
6.23e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.79 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 131 RGEILDCLERTGIRNAAKRlnDFpHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSL 210
Cdd:PRK13409 190 RGKLDEVVERLGLENILDR--DI-SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 211 LFITHNLSIVRKLADNVAVM--QNGrcveqntASTLLSapqHPYTQRL---------LDSEPsgdpvplaadstplLRVE 279
Cdd:PRK13409 265 LVVEHDLAVLDYLADNVHIAygEPG-------AYGVVS---KPKGVRVgineylkgyLPEEN--------------MRIR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 280 DLSVSF----PIRKGILRRIVDQNPVLKNI-RFSL-------RPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEI 342
Cdd:PRK13409 321 PEPIEFeerpPRDESERETLVEYPDLTKKLgDFSLeveggeiYEGEVIGIVGPNGIGKTT----FAKLLAgvlkpDEGEV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 343 FFDdmplhrwnrrqmLPVRPRMQVVFQDPNSSlnprlsvlqiIEEGLRVHQPGLSAQQREQEVMRVMA-EVGLDagtrhR 421
Cdd:PRK13409 397 DPE------------LKISYKPQYIKPDYDGT----------VEDLLRSITDDLGSSYYKSEIIKPLQlERLLD-----K 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 422 YPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQAQILA--LLKGLQEKHRLAYIFISHDL 486
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVakAIRRIAEEREATALVVDHDI 514
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-508 |
9.20e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 9.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWNRRqmlpVRPRMQVVFQD 370
Cdd:PRK13537 13 VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARH----ARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 371 PNssLNPRLSVlqiiEEGLRVHQP--GLSAQQREQEVMRVMAEVGLDAGTRHRYpAEFSGGQRQRIAIARALILKPELII 448
Cdd:PRK13537 89 DN--LDPDFTV----RENLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 449 LDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-240 |
9.94e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.13 E-value: 9.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAF-STQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILF--HGSSLLHA 81
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRGIRGNK-----IAMIFQEPMVSLNPlHSLEKQL-YEVLSLhrGMRKEAARGEILDCLERTGIRNAAkrLNDFPH 155
Cdd:PRK13631 101 TNPYSKKIKNFKelrrrVSMVFQFPEYQLFK-DTIEKDImFGPVAL--GVKKSEAKKLAKFYLNKMGLDDSY--LERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRC 235
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
....*
gi 658548496 236 VEQNT 240
Cdd:PRK13631 255 LKTGT 259
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-261 |
1.02e-17 |
|
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: 82.21 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 30 LQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHtlrgirgnkIAMIFQEPMVSLNPLH 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPA-----KGTVKVAGASPGKGWRH---------IGYVPQRHEFAWDFPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 110 SLEKQLYEVLSLHRGMRKEAARGE---ILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:TIGR03771 67 SVAHTVMSGRTGHIGWLRRPCVADfaaVRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 187 LDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVaVMQNGRCVEQNTASTLLSAPQHPYTQRLLDSEP 261
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGVSDSSP 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-230 |
1.19e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhgSSLLHADEHTLRGIRGNKIAMIFQEP 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKS----TLLKVL----------------AGVLRPTSGTVRRAGGARVAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 102 MVSlnplHSLEKQLYEVLSL----HRGMRKE---AARGEILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTR 174
Cdd:NF040873 65 EVP----DSLPLTVRDLVAMgrwaRRGLWRRltrDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 175 PELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRkLADNVAVM 230
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
278-515 |
1.32e-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: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 278 VEDLSVSFpirkgilrrIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIFFD-----DMPLHRW 352
Cdd:cd03289 5 VKDLTAKY---------TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDgvswnSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 353 nrRQMLPVRPRMQVVFQDP-NSSLNPrlsvlqiieeglrvhqpglSAQQREQEVMRVMAEVGLDAgTRHRYPAE------ 425
Cdd:cd03289 76 --RKAFGVIPQKVFIFSGTfRKNLDP-------------------YGKWSDEEIWKVAEEVGLKS-VIEQFPGQldfvlv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 426 -----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKglQEKHRLAYIFISHDLQVVRAlCHQVIVLR 500
Cdd:cd03289 134 dggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIE 210
|
250
....*....|....*
gi 658548496 501 QGEVVEQGECQRVFS 515
Cdd:cd03289 211 ENKVRQYDSIQKLLN 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-249 |
1.32e-17 |
|
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: 82.32 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHt 85
Cdd:TIGR04406 2 LVAENLIKSYKK----RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILIDGQDITHLPMH- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGnkIAMIFQEPmvSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaaKRLNDFPHQ-LSGGERQR 164
Cdd:TIGR04406 72 ERARLG--IGYLPQEA--SIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMsLSGGERRR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 165 VMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTL 244
Cdd:TIGR04406 144 VEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
....*
gi 658548496 245 LSAPQ 249
Cdd:TIGR04406 223 VANEK 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
270-509 |
1.39e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 270 ADSTPLLRVEDLSVSFpirKGIlrrivdqnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFF 344
Cdd:PRK15439 6 TTAPPLLCARSISKQY---SGV--------EVLKGIDFTLHAGEVHALLGGNGAGKST----LMKIIAgivppDSGTLEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 345 DDMPLHRWNrrqmlPVRPR---MQVVFQDPNssLNPRLSVLQIIEEGLRVHQpgLSAQQREQEVMRVMAEVGLD--AGTr 419
Cdd:PRK15439 71 GGNPCARLT-----PAKAHqlgIYLVPQEPL--LFPNLSVKENILFGLPKRQ--ASMQKMKQLLAALGCQLDLDssAGS- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 420 hrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK15439 141 ------LEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVM 213
|
250
....*....|
gi 658548496 500 RQGEVVEQGE 509
Cdd:PRK15439 214 RDGTIALSGK 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
273-513 |
1.40e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPirkgilrrivdqnPV--LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFD 345
Cdd:PRK09700 3 TPYISMAGIGKSFG-------------PVhaLKSVNLTVYPGEIHALLGENGAGKST----LMKVLSgihepTKGTITIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNRRqmLPVRPRMQVVFQDpnSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAE 425
Cdd:PRK09700 66 NINYNKLDHK--LAAQLGIGIIYQE--LSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 426 FSG----GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK09700 142 KVAnlsiSHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKD 220
|
250
....*....|..
gi 658548496 502 GEVVEQGECQRV 513
Cdd:PRK09700 221 GSSVCSGMVSDV 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
297-491 |
2.06e-17 |
|
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: 80.48 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmLPVRPRMQVVFQDP 371
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTT----LLRILAgllrpDSGEVRWNGTPLAE------QRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSLNPRLSVLqiieEGLRVHQPGLSAQQREqeVMRVMAEVGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:TIGR01189 81 LPGLKPELSAL----ENLHFWAAIHGGAQRT--IEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658548496 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-217 |
2.14e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFstQGetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpSPPVSYPQGDIlfhgssllhadeh 84
Cdd:PRK11248 1 MLQISHLYADY--GG--KPALEDINLTLESGELLVVLGPSGCGKT----TLLNLI-AGFVPYQHGSI------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLRGIR----GNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRlndFPHQLSGG 160
Cdd:PRK11248 59 TLDGKPvegpGAERGVVFQNE--GLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNL 217
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
301-515 |
3.04e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDD-----MPLHRwnrrqmlpvRPRMQVVFQDPNSS 374
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDedislLPLHA---------RARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVLQIIEEGLRVHQpGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 455 SLDRTVQAQILALLKGLQEkHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
299-497 |
3.61e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQgeiffddmplhrwnRRQM---LPVRPRMQVVFQDPNSSL 375
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKST----LLKVLAGV--------------LRPTsgtVRRAGGARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRL--SVLQIIEEGLRVHQPGLSAQQRE--QEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:NF040873 67 PDSLplTVRDLVAMGRWARRGLWRRLTRDdrAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658548496 452 PTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI 497
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVL 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
302-515 |
4.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.98 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDD--MPLHRWNRRQMLPVRPRMQVVFQDPNSS 374
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqltNGL----IISETGQTIVGDyaIPANLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LnprlsVLQIIEEGLRVHQPGLSAQQRE--QEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEP 452
Cdd:PRK13645 103 L-----FQETIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 453 TSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFS 515
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-245 |
4.19e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYPQGDILFHGSSllhaDEHTLRGIRgNKIAMIFQEPmvsln 106
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 plhslEKQLYEVLSL--------HRGMRKEAARGEILDCLERTGIrnAAKRLNDFPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK13643 94 -----ESQLFEETVLkdvafgpqNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 179 IADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLL 245
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-234 |
4.43e-17 |
|
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: 80.27 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 12 SIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhgSSLLHADEHTLRgIRG 91
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLL----------------AGIYPPDSGTVT-VRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 92 NKIAMIfqEPMVSLNPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGirnaakrLNDFPHQ----LSGGERQRVMI 167
Cdd:cd03220 84 RVSSLL--GLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSE-------LGDFIDLpvktYSSGMKARLAF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 168 AMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-249 |
5.04e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 28 LSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypqGDILFHGSSLLHADEHTLRGIRgnkiAMIFQepmvSLNP 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS------GSIQFAGQPLEAWSAAELARHR----AYLSQ----QQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 108 LHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIrnaAKRLNDFPHQLSGGERQRVMIAMALL-----TRPE--LLIA 180
Cdd:PRK03695 81 PFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 181 DEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQ 249
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-248 |
5.78e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.74 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIaFSTQGetRTVVTDLSLQIQPGETLALVGESGSGKS--VSALsiLRLLPsppvsYpQGDILFHGSSLLHADE 83
Cdd:PRK11174 350 IEAEDLEI-LSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTslLNAL--LGFLP-----Y-QGSLKINGIELRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRgirgNKIAMIFQEPmvslnplHSLEKQLYEVLSLHRgmrKEAARGEILDCLERTGIRNAAKRLN---DFPHQ---- 156
Cdd:PRK11174 419 ESWR----KHLSWVGQNP-------QLPHGTLRDNVLLGN---PDASDEQLQQALENAWVSEFLPLLPqglDTPIGdqaa 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRdeLNMSLLFITHNLSIVRKLaDNVAVMQNGRC 235
Cdd:PRK11174 485 gLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
250
....*....|...
gi 658548496 236 VEQNTASTLLSAP 248
Cdd:PRK11174 562 VQQGDYAELSQAG 574
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-267 |
6.14e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 17 TQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHGSSLLHADEHTLRGIRgNKI 94
Cdd:PRK11831 16 TRGN-RCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGqiAPDH---GEILFDGENIPAMSRSRLYTVR-KRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 95 AMIFQEP--MVSLNPLHSLEKQLYEvlslHRGMRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALL 172
Cdd:PRK11831 87 SMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 173 TRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSAPQhPY 252
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PR 238
|
250
....*....|....*
gi 658548496 253 TQRLLDSEPSGdPVP 267
Cdd:PRK11831 239 VRQFLDGIADG-PVP 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
319-520 |
7.39e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 319 GESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRWNRRQMLPV-RPRMQVVFQDpnSSLNPRLSVlqiiEEGLRVh 392
Cdd:PRK11144 31 GRSGAGKTS----LINAISgltrpQKGRIVLNGRVLFDAEKGICLPPeKRRIGYVFQD--ARLFPHYKV----RGNLRY- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 393 qpGLSAQQREQeVMRVMAEVGLDAGTRhRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQ 472
Cdd:PRK11144 100 --GMAKSMVAQ-FDKIVALLGIEPLLD-RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658548496 473 EKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPTQR 520
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-498 |
8.20e-17 |
|
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: 83.30 E-value: 8.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 33 QPGETLALVGESGSGKSvSALSIL--RLLP-----SPPVSYPqgDIL--FHGSSLLhadEHtLRGIRGNKIAmifqepmV 103
Cdd:COG1245 97 KKGKVTGILGPNGIGKS-TALKILsgELKPnlgdyDEEPSWD--EVLkrFRGTELQ---DY-FKKLANGEIK-------V 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 SLNPlhslekQLYEVLS-LHRG-----MRKEAARGEILDCLERTGIRNAAKR-LNDfphqLSGGERQRVMIAMALLTRPE 176
Cdd:COG1245 163 AHKP------QYVDLIPkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRdISE----LSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 177 LLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVM--QNGrcveqntASTLLSapqHPYTQ 254
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILygEPG-------VYGVVS---KPKSV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 255 RL---------LDSEPsgdpvplaadstplLRVEDLSVSFPIRKgiLRRIVDQNPVLK--NIR-----FSL-------RP 311
Cdd:COG1245 302 RVginqyldgyLPEEN--------------VRIRDEPIEFEVHA--PRREKEEETLVEypDLTksyggFSLeveggeiRE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 312 GESLGLVGESGSGKSTtglaLLRLIAS-----QGEIFFDdmplhrwnrrqmLPVRPRMQVVFQDPNSSlnprlsvlqiIE 386
Cdd:COG1245 366 GEVLGIVGPNGIGKTT----FAKILAGvlkpdEGEVDED------------LKISYKPQYISPDYDGT----------VE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 387 EGLR-VHQPGLSAQQREQEVMRVMaevGLDAgTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQAQIL 465
Cdd:COG1245 420 EFLRsANTDDFGSSYYKTEIIKPL---GLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLA 493
|
490 500 510
....*....|....*....|....*....|....*
gi 658548496 466 A--LLKGLQEKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:COG1245 494 VakAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-240 |
8.69e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.13 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL-RLLPSPpvsypQGDILFHGSSLLHADEHT 85
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD-----SGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LrgirGNKIAMIFQEPMVSLNplhslekqL--YEVLSL-----HRGMRKEAARGEI---LDCLERTGIRNAakrlndFPH 155
Cdd:COG4604 73 L----AKRLAILRQENHINSR--------LtvRELVAFgrfpySKGRLTAEDREIIdeaIAYLDLEDLADR------YLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRC 235
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
....*
gi 658548496 236 VEQNT 240
Cdd:COG4604 215 VAQGT 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-248 |
9.89e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 7 SIDNLSiaFSTQGetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLLHADEH 84
Cdd:PRK10575 13 ALRNVS--FRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKS----TLLKMLGrhQPPSE---GEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLrgirGNKIAMIFQEpmvsLNPLHSLekQLYEVLSLHR-------GMRKEAARGEILDCLERTGIRNAAKRLNDfphQL 157
Cdd:PRK10575 82 AF----ARKVAYLPQQ----LPAAEGM--TVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD---SL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
250
....*....|.
gi 658548496 238 QNTASTLLSAP 248
Cdd:PRK10575 229 QGTPAELMRGE 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
273-501 |
1.11e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPIRKgilrrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIffddmplhr 351
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVI--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 wNRRQMLPVRPRMQVVFQDPNSSLNprlsvlqiIEEGLRVHqPGLsaqqREQEVMRVMAEVglDAGTRHRYPAE-FSGGQ 430
Cdd:PRK09544 62 -KRNGKLRIGYVPQKLYLDTTLPLT--------VNRFLRLR-PGT----KKEDILPALKRV--QAGHLIDAPMQkLSGGE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-234 |
1.24e-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: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhgSSLLHADEHT 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI----------------AGELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGNKIAMIfqepmvslnplhslekqlyevlslhrgmrkeaargeildclertgirnaakrlndfpHQLSGGERQRV 165
Cdd:cd03221 57 VTWGSTVKIGYF---------------------------------------------------------EQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelnmSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-236 |
1.28e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHGSSLLHADEHT-LRGIRgNKIAMIFQE 100
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKS----TIMQLLnglhvPT------QGSVRVDDTLITSTSKNKdIKQIR-KKVGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PmvslnplhslEKQLYEVLSL--------HRGMRKEAARGEILDCLERTGIRNAAKRLNdfPHQLSGGERQRVMIAMALL 172
Cdd:PRK13649 94 P----------ESQLFEETVLkdvafgpqNFGVSQEEAEALAREKLALVGISESLFEKN--PFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 173 TRPELLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-457 |
2.07e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvSALSIL---RLLPSPPVSYPQGDIlfhgssllhADEHTLRGIrGNKIAMIFQepmv 103
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKS-SLLSLIagaRKIQQGRVEVLGGDM---------ADARHRRAV-CPRIAYMPQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 slnplhSLEKQLYEVLSLHR---------GMRKEAARGEILDCLERTGI-----RNAAKrlndfphqLSGGERQRVMIAM 169
Cdd:NF033858 84 ------GLGKNLYPTLSVFEnldffgrlfGQDAAERRRRIDELLRATGLapfadRPAGK--------LSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 170 ALLTRPELLIADEPTTALDVTVQAQILTLLRELRDEL-NMSLLFIThnlsivrklA--------DNVAVMQNGRCVEQNT 240
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT---------AymeeaerfDWLVAMDAGRVLATGT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 241 ASTLLSAPQHP-----YTqRLLDSEPSGDPVPLAAdsTPllRVEDLSVSFPIR-KGILRRI-----VDqnpvlkNIRFSL 309
Cdd:NF033858 221 PAELLARTGADtleaaFI-ALLPEEKRRGHQPVVI--PP--RPADDDDEPAIEaRGLTMRFgdftaVD------HVSFRI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 310 RPGESLGLVGESGSGKST-----TGLallrLIASQGEIF-FDDmplhrwnrrqmlPVRP-----RMQVVFQDPNSSLNPR 378
Cdd:NF033858 290 RRGEIFGFLGSNGCGKSTtmkmlTGL----LPASEGEAWlFGQ------------PVDAgdiatRRRVGYMSQAFSLYGE 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 379 LSVLQIIEegLRVHQPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:NF033858 354 LTVRQNLE--LHARLFHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-201 |
2.36e-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: 77.40 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAfstQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLlhade 83
Cdd:TIGR01189 1 LAARNLACS---RGE-RMLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILAglLRPDS---GEVRWNGTPL----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRGNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLHRGmrkeaARGEILDCLERTGIRNAAKRLndfPHQLSGGERQ 163
Cdd:TIGR01189 65 AEQRDEPHENILYLGHLP--GLKPELSALENLHFWAAIHGG-----AQRTIEDALAAVGLTGFEDLP---AAQLSAGQQR 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRE 201
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-236 |
3.06e-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: 78.08 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 18 QGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYpqGDILFHGSSLlhaDEHTLRGIrgnkIAMI 97
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPR---KPDQFQKC----VAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 98 FQEPMvsLNPLHSLEKQLY--EVLSLHRGMRKEAARGEILDCLER----TGIRNAAKRlndfphQLSGGERQRVMIAMAL 171
Cdd:cd03234 87 RQDDI--LLPGLTVRETLTytAILRLPRKSSDAIRKKRVEDVLLRdlalTRIGGNLVK------GISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 172 LTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
292-485 |
4.41e-16 |
|
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: 81.13 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQN-PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMplhrwNRRQMLPvrprmq 365
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkdFNGEARPQPG-----IKVGYLP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 366 vvfQDPnsSLNPRLSVLQIIEEGLrvhQPGLSAQQREQEVMRVMAEVG----------------LDAGTRH--------- 420
Cdd:TIGR03719 75 ---QEP--QLDPTKTVRENVEEGV---AEIKDALDRFNEISAKYAEPDadfdklaaeqaelqeiIDAADAWdldsqleia 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 421 ----RYP------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILALLkglqEKHRLAY----IFISHD 485
Cdd:TIGR03719 147 mdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWL----ERHLQEYpgtvVAVTHD 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-248 |
4.53e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 25 VTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsyPQ-GDILFHGSSLlhADEHTLRGIRgNKIAMIFQEPmv 103
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR------PQkGKVLVSGIDT--GDFSKLQGIR-KLVGIVFQNP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 slnplhslEKQLyevlsLHRGMRKEAARGEILDCLERTGIRNAAKR------LNDF----PHQLSGGERQRVMIAMALLT 173
Cdd:PRK13644 87 --------ETQF-----VGRTVEEDLAFGPENLCLPPIEIRKRVDRalaeigLEKYrhrsPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 174 RPELLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRkLADNVAVMQNGRCVEQNTASTLLSAP 248
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-247 |
5.49e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIafsTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSllh 80
Cdd:PRK15056 2 MQQAGIVVNDVTV---TWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-----VRLASGKISILGQP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 adehTLRGIRGNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMRKEAA---RGEILDCLERTGirnaakrLNDFPH-- 155
Cdd:PRK15056 71 ----TRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKkrdRQIVTAALARVD-------MVEFRHrq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADnVAVMQNG 233
Cdd:PRK15056 140 igELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
250
....*....|....
gi 658548496 234 RCVEQNTASTLLSA 247
Cdd:PRK15056 218 TVLASGPTETTFTA 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
300-505 |
5.62e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEIFFDDmplHRWNRRQMLPVrPRMQvvfQDPnsslnPRL 379
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKST----LMKILN--GEVLLDD---GRIIYEQDLIV-ARLQ---QDP-----PRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 ---SVLQIIEEGL--------RVHQ-----------PGLSAQQREQEVM-------------RVMAEVGLDAGTRHrypA 424
Cdd:PRK11147 79 vegTVYDFVAEGIeeqaeylkRYHDishlvetdpseKNLNELAKLQEQLdhhnlwqlenrinEVLAQLGLDPDAAL---S 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEkhrlAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
.
gi 658548496 505 V 505
Cdd:PRK11147 232 V 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
272-516 |
5.70e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFpiRKGilrrivdqNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLH 350
Cdd:PRK15056 3 QQAGIVVNDVTVTW--RNG--------HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKISILGQPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 351 RWNRRQMLPVRPRMQVVfqdpNSSLnPRLsVLQIIEEGLRVHQPGLS-AQQREQE-VMRVMAEVGLdAGTRHRYPAEFSG 428
Cdd:PRK15056 73 QALQKNLVAYVPQSEEV----DWSF-PVL-VEDVVMMGRYGHMGWLRrAKKRDRQiVTAALARVDM-VEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 429 GQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRqGEVVEQG 508
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
....*...
gi 658548496 509 ECQRVFSA 516
Cdd:PRK15056 224 PTETTFTA 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-485 |
5.80e-16 |
|
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: 80.75 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL-----------RLLPSPPVSY----PQGDilfhgssllhaDEHTL 86
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkdfngeaRPQPGIKVGYlpqePQLD-----------PTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 87 RGI-------------RGNKIAMIFQEPMVSLNPLhsLEKQ--LYEVLslhrgmrkEAARGEILDclERTGIRNAAKRL- 150
Cdd:TIGR03719 86 RENveegvaeikdaldRFNEISAKYAEPDADFDKL--AAEQaeLQEII--------DAADAWDLD--SQLEIAMDALRCp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 151 -NDFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDvtvqAQILTLLRELRDELNMSLLFITHNlsivRKLADNVA 228
Cdd:TIGR03719 154 pWDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD----RYFLDNVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 229 ----VMQNGRCV----------EQNTASTLLSAPQHPYTQRLLDSE-------PSGDPVP-----------LAADSTPll 276
Cdd:TIGR03719 226 gwilELDRGRGIpwegnysswlEQKQKRLEQEEKEESARQKTLKRElewvrqsPKGRQAKskarlaryeelLSQEFQK-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 277 RVEDLSVSFP---------IRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-----GEI 342
Cdd:TIGR03719 304 RNETAEIYIPpgprlgdkvIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMITGQeqpdsGTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 343 FFDDMplhrwnrrqmlpvrprMQVVFQDPN-SSLNPRLSVLQIIEEGLRVHQPGlsaqQREqevMRVMAEVG---LDAGT 418
Cdd:TIGR03719 380 EIGET----------------VKLAYVDQSrDALDPNKTVWEEISGGLDIIKLG----KRE---IPSRAYVGrfnFKGSD 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 419 RHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQaqilALLKGLQEKHRLAYIfISHD 485
Cdd:TIGR03719 437 QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDvETLR----ALEEALLNFAGCAVV-ISHD 499
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-508 |
6.08e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.41 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEIFFD-----DM 347
Cdd:cd03217 1 LEIKDLHVS-----------VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKgeditDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PLHRWNRRQMLpvrprmqVVFQDPnsslnPRLsvlqiieEGLRVhqpglsaqqreQEVMRvmaevGLDAGtrhrypaeFS 427
Cdd:cd03217 70 PPEERARLGIF-------LAFQYP-----PEI-------PGVKN-----------ADFLR-----YVNEG--------FS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVI-VLRQGEVVE 506
Cdd:cd03217 107 GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVhVLYDGRIVK 185
|
..
gi 658548496 507 QG 508
Cdd:cd03217 186 SG 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-489 |
6.58e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL--------------------RLLPSPPv 64
Cdd:PRK11147 3 LISIHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKS-TLMKILngevllddgriiyeqdlivaRLQQDPP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 65 SYPQGDI-------LFHGSSLLHADEHTLRgirgnkiaMIFQEPMVSLnpLHSLEkQLYEVLSLHRGMRKEAargEILDC 137
Cdd:PRK11147 77 RNVEGTVydfvaegIEEQAEYLKRYHDISH--------LVETDPSEKN--LNELA-KLQEQLDHHNLWQLEN---RINEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 138 LERTGIrNAAKRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelnmSLLFITHNL 217
Cdd:PRK11147 143 LAQLGL-DPDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 218 SIVRKLADNVAVMQNGRcveqntastLLSAPQHpYTQRLLDSEPSgdpvplaadstplLRVEDL-SVSFP---------I 287
Cdd:PRK11147 214 SFIRNMATRIVDLDRGK---------LVSYPGN-YDQYLLEKEEA-------------LRVEELqNAEFDrklaqeevwI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 288 RKGI----------------LRR------------------------IV----------DQNPVLKNIRFSLRPGESLGL 317
Cdd:PRK11147 271 RQGIkarrtrnegrvralkaLRRerserrevmgtakmqveeasrsgkIVfemenvnyqiDGKQLVKDFSAQVQRGDKIAL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 318 VGESGSGKSTtglaLLRLIASQ-----GEI---------FFDDmplHRwnrrqmlpvrprmqvvfqdpnSSLNPRLSVLQ 383
Cdd:PRK11147 351 IGPNGCGKTT----LLKLMLGQlqadsGRIhcgtklevaYFDQ---HR---------------------AELDPEKTVMD 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 384 IIEEGlrvhqpglsaqqrEQEVMrvmaevgLDAGTRH--RYPAEF--------------SGGQRQRIAIARaLILKP-EL 446
Cdd:PRK11147 403 NLAEG-------------KQEVM-------VNGRPRHvlGYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPsNL 461
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 658548496 447 IILDEPTSSLDrtvqAQILALLKGLQEKHRLAYIFISHDLQVV 489
Cdd:PRK11147 462 LILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
297-465 |
7.04e-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: 81.11 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIFFD-----DMPLHRWnrRQMLPVRPRMQVVFQDP 371
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDgvswnSVTLQTW--RKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 -NSSLNPRlsvlqiieeglrvhqpglsAQQREQEVMRVMAEVGLDAgTRHRYPAE-----------FSGGQRQRIAIARA 439
Cdd:TIGR01271 1308 fRKNLDPY-------------------EQWSDEEIWKVAEEVGLKS-VIEQFPDKldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180
....*....|....*....|....*.
gi 658548496 440 LILKPELIILDEPTSSLDrTVQAQIL 465
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD-PVTLQII 1392
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
271-529 |
1.12e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 271 DSTPLL--RVEDLSVSFPIRkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtgLALLRL---IASQGEIFFD 345
Cdd:PRK10790 332 DDRPLQsgRIDIDNVSFAYR--------DDNLVLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyyPLTEGEIRLD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 DMPLHRWNRRQMlpvRPRMQVVFQDP---------NSSLNPRLSvlqiieeglrvhqpglsaqqrEQEVMRVMAEVGLDA 416
Cdd:PRK10790 402 GRPLSSLSHSVL---RQGVAMVQQDPvvladtflaNVTLGRDIS---------------------EEQVWQALETVQLAE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 417 GTR------HRYPAE----FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLayIFISHDL 486
Cdd:PRK10790 458 LARslpdglYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRL 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 658548496 487 Q-VVRAlcHQVIVLRQGEVVEQGECQRVFSAPT---QRYTRQLLSAD 529
Cdd:PRK10790 536 StIVEA--DTILVLHRGQAVEQGTHQQLLAAQGrywQMYQLQLAGEE 580
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
272-508 |
1.20e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSFpirKGILrrIVDqnpvlkNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDD 346
Cdd:PRK11300 2 SQPLLSVSGLMMRF---GGLL--AVN------NVNLEVREQEIVSLIGPNGAGKTTvfnclTGF----YKPTGGTILLRG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNRRQMlpvrPRMQVV--FQdpNSSLNPRLSVLqiieEGLRVHQ---------PGL----SAQQREQEVMRVMAE 411
Cdd:PRK11300 67 QHIEGLPGHQI----ARMGVVrtFQ--HVRLFREMTVI----ENLLVAQhqqlktglfSGLlktpAFRRAESEALDRAAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 412 ----VGL------DAGTrhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIF 481
Cdd:PRK11300 137 wlerVGLlehanrQAGN-------LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLL 209
|
250 260
....*....|....*....|....*..
gi 658548496 482 ISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK11300 210 IEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
307-518 |
1.50e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 307 FSLRPGESLGLVGESGSGKSTTGLALLRLIASQGEIFFDDMPLHRWNRRQMlpVRPRMQVVFQDPNSSLNPrlsVLQIie 386
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAEL--ARHRAYLSQQQTPPFAMP---VFQY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 387 egLRVHQPGLSAQQREQEVMRVMAE-VGLDaGTRHRYPAEFSGGQRQRIAIARALI-----LKPE--LIILDEPTSSLDR 458
Cdd:PRK03695 90 --LTLHQPDKTRTEAVASALNEVAEaLGLD-DKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 459 TVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PRK03695 167 AQQAALDRLLSELCQQGI-AVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-248 |
1.85e-15 |
|
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: 75.66 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLLHADEHT 85
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-----VKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 lRGIRGnkIAMIFQEPMV--SLnplhSLEKQLYEVLSLHRGMRKEAARgEILDCLERTGIRNAAKRLNDfphQLSGGERQ 163
Cdd:cd03218 72 -RARLG--IGYLPQEASIfrKL----TVEENILAVLEIRGLSKKEREE-KLEELLEEFHITHLRKSKAS---SLSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDeLNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAST 243
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
....*
gi 658548496 244 LLSAP 248
Cdd:cd03218 220 IAANE 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
300-508 |
1.99e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWNRRqmlpVRPRMQVVFQDPNssLNPR 378
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARL----ARARIGVVPQFDN--LDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LSVlqiiEEGLRVHQP--GLSAQQREQEVMRVMAEVGLDAGTRHRYpAEFSGGQRQRIAIARALILKPELIILDEPTSSL 456
Cdd:PRK13536 129 FTV----RENLLVFGRyfGMSTREIEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658548496 457 DRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-246 |
2.07e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFstqGETRtVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPVSyPQGDILFHGSSLlh 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY---GKIQ-ALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRA-TSGRIVFDGKDI-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRgNKIAM------IFQEPMVSLNPLHS---LEKQLYEvlslhrgMRKEAARGEILDCLERTGIRNAAkrln 151
Cdd:PRK11614 70 TDWQTAKIMR-EAVAIvpegrrVFSRMTVEENLAMGgffAERDQFQ-------ERIKWVYELFPRLHERRIQRAGT---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 dfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQ 231
Cdd:PRK11614 138 -----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLE 211
|
250
....*....|....*
gi 658548496 232 NGRCVEQNTASTLLS 246
Cdd:PRK11614 212 NGHVVLEDTGDALLA 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-246 |
2.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 8 IDNLSIAFS--TQGETRTVvTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPVSYPQGDILfhGSSLLHADEHT 85
Cdd:PRK13645 9 LDNVSYTYAkkTPFEFKAL-NNTSLTFKKNKVTCVIGTTGSGKS----TMIQLTNGLIISETGQTIV--GDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRG--NKIAMIFQEPMVSLNPlHSLEKQLyEVLSLHRGMRKEAARGEILDCLERTGI-RNAAKRlndFPHQLSGGER 162
Cdd:PRK13645 82 IKEVKRlrKEIGLVFQFPEYQLFQ-ETIEKDI-AFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAS 242
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
....
gi 658548496 243 TLLS 246
Cdd:PRK13645 237 EIFS 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-268 |
2.40e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 9 DNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLH-ADEHTLR 87
Cdd:PRK10253 11 EQLTLGYGK----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT--PAH---GHVWLDGEHIQHyASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 88 girgnKIAMIFQEPM----VSLNPLhsLEKQLYEVLSLHRGMRKEAARGeILDCLERTGIRNAAKRLNDfphQLSGGERQ 163
Cdd:PRK10253 82 -----RIGLLAQNATtpgdITVQEL--VARGRYPHQPLFTRWRKEDEEA-VTKAMQATGITHLADQSVD---TLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAST 243
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
250 260 270
....*....|....*....|....*....|.
gi 658548496 244 LLSAP--QHPYTQR--LLDSEPSGDP--VPL 268
Cdd:PRK10253 231 IVTAEliERIYGLRcmIIDDPVAGTPlvVPL 261
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-247 |
2.53e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQpLLSIDNLSIAF------------------STQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL--- 59
Cdd:COG1134 1 MSS-MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKS----TLLKLIagi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 60 --PSppvsypQGDILFHG--SSLLhadehtlrgirgnkiamifqEPMVSLNPLHSLEKQLYEVLSLHrGMRKEAARGEIL 135
Cdd:COG1134 76 lePT------SGRVEVNGrvSALL--------------------ELGAGFHPELTGRENIYLNGRLL-GLSRKEIDEKFD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 136 DCLERTGIRnaakrlnDFPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLL 211
Cdd:COG1134 129 EIVEFAELG-------DFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVI 200
|
250 260 270
....*....|....*....|....*....|....*.
gi 658548496 212 FITHNLSIVRKLADNVAVMQNGRCVEQNTASTLLSA 247
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-234 |
2.90e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQgetrTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFhg 75
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKT----TVFNCLtgfykPT------GGTILL-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 ssllhaDEHTLRGIRGNKIAM-----------IFQEPMVSLNPLHSLEKQLYEvlSLHRGMRKEAA----RGEILD---- 136
Cdd:PRK11300 65 ------RGQHIEGLPGHQIARmgvvrtfqhvrLFREMTVIENLLVAQHQQLKT--GLFSGLLKTPAfrraESEALDraat 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 137 CLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHN 216
Cdd:PRK11300 137 WLERVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
250
....*....|....*...
gi 658548496 217 LSIVRKLADNVAVMQNGR 234
Cdd:PRK11300 214 MKLVMGISDRIYVVNQGT 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-215 |
3.60e-15 |
|
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: 73.34 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL----PsppvsYPQGDILFHgssllha 81
Cdd:cd03223 1 IELENLSLATPDG---RVLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRALaglwP-----WGSGRIGMP------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 dehtlrgiRGNKIAMIFQEPMVslnPLHSLEKQLYevlslhrgmrkeaargeildclertgirnaakrlndFP--HQLSG 159
Cdd:cd03223 62 --------EGEDLLFLPQRPYL---PLGTLREQLI------------------------------------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRdelnMSLLFITH 215
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
292-485 |
5.80e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQN-PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFddMPLHrwnRRQMLPvrprmq 365
Cdd:PRK11819 12 VSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkeFEGEARP--APGI---KVGYLP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 366 vvfQDPnsSLNPRLSVLQIIEEGLrvhQPGLSAQQREQEVMRVMAEVG----------------LDAGTRH--------- 420
Cdd:PRK11819 77 ---QEP--QLDPEKTVRENVEEGV---AEVKAALDRFNEIYAAYAEPDadfdalaaeqgelqeiIDAADAWdldsqleia 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 421 ----RYP------AEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtvqAQILALLkglqEKHRLAY----IFISHD 485
Cdd:PRK11819 149 mdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWL----EQFLHDYpgtvVAVTHD 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
301-508 |
6.21e-15 |
|
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: 74.23 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--------GEIFFDDMPLHRWNrrqmlpVRPRMQVVFQDPN 372
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTT----LLDAISGRvegggttsGQILFNGQPRKPDQ------FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 373 --SSLNPRLSVLQIIEEGLRVHQPGLSAQQR-EQEVMRVMAevglDAGTRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03234 92 llPGLTVRETLTYTAILRLPRKSSDAIRKKRvEDVLLRDLA----LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 450 DEPTSSLDRTVQAQILALLKGLQEKHRLAYIFIshdlqvvralcHQ-----------VIVLRQGEVVEQG 508
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTI-----------HQprsdlfrlfdrILLLSSGEIVYSG 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-234 |
6.44e-15 |
|
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: 74.29 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 19 GETRTV--VTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhgSSLLHADEHTLRgIRGN---- 92
Cdd:cd03267 29 RKYREVeaLKGISFTIEKGEIVGFIGPNGAGKT----TTLKIL----------------SGLLQPTSGEVR-VAGLvpwk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 93 -------KIAMIF-QEPMVS--LNPLHSLE--KQLYEVLSLHRGMRKEaargEILDCLERTGIRNAAKRlndfphQLSGG 160
Cdd:cd03267 88 rrkkflrRIGVVFgQKTQLWwdLPVIDSFYllAAIYDLPPARFKKRLD----ELSELLDLEELLDTPVR------QLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-248 |
6.87e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.45 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 14 AFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpsppvSYPQGDILFHGSSLLHADEHTLRGirgnK 93
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF-----DVSEGDIRFHDIPLTKLQLDSWRS----R 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 94 IAMIFQEPM---------VSLNPLHSLEKQLYEV----------LSLHRGMRKEAArgeildclERtGIrnaakrlndfp 154
Cdd:PRK10789 391 LAVVSQTPFlfsdtvannIALGRPDATQQEIEHVarlasvhddiLRLPQGYDTEVG--------ER-GV----------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElnMSLLFITHNLSIVRKlADNVAVMQNGR 234
Cdd:PRK10789 451 -MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGH 526
|
250
....*....|....
gi 658548496 235 CVEQNTASTLLSAP 248
Cdd:PRK10789 527 IAQRGNHDQLAQQS 540
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-245 |
7.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 28 LSLQIQPGETLALVGESGSGKSVSALSILRL-LPSppvsypQGDILFHGSSLLHADEHTLRgirgNKIAMIFQEPMVSLN 106
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQ------RGRVKVMGREVNAENEKWVR----SKVGLVFQDPDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 PLHSLEKQLYEVLSLhrGMRKEaargEILdclERTGIRNAAKRLNDF----PHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:PRK13647 94 SSTVWDDVAFGPVNM--GLDKD----EVE---RRVEEALKAVRMWDFrdkpPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 183 PTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLL 245
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-234 |
8.59e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSiafstqGETrtvVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpSPPVSypqGDILFHGssllhad 82
Cdd:PRK15439 266 APVLTVEDLT------GEG---FRNISLEVRAGEILGLAGVVGAGRTELAETLYGL--RPARG---GRIMLNG------- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 ehtlRGIRGNKIAMIFQEPMVSL------NPLHsLEKQLY-EVLSLHRGMR-------KEAARgeildcLER-------- 140
Cdd:PRK15439 325 ----KEINALSTAQRLARGLVYLpedrqsSGLY-LDAPLAwNVCALTHNRRgfwikpaRENAV------LERyrralnik 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 141 -TGIRNAAKRLndfphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSI 219
Cdd:PRK15439 394 fNHAEQAARTL-------SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEE 465
|
250
....*....|....*
gi 658548496 220 VRKLADNVAVMQNGR 234
Cdd:PRK15439 466 IEQMADRVLVMHQGE 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
297-491 |
1.01e-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: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDDMPLHRwnrrqmlpVRPRMQ--VVFQ 369
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTT----LLRILAglsppLAGRVLLNGGPLDF--------QRDSIArgLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 370 DPNSSLNPRLSVLqiieEGLRVHQPGLSAQQREQevmrVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARALILKPELIIL 449
Cdd:cd03231 79 GHAPGIKTTLSVL----ENLRFWHADHSDEQVEE----ALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658548496 450 DEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRA 491
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
294-509 |
1.12e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 294 RIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS--QGEIFFDDMPLHrwNRRQMLPVRPRMQVVFQDp 371
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKST----LLNALAGriQGNNFTGTILAN--NRKPTKQILKRTGFVTQD- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 nSSLNPRLSVLQ--IIEEGLRVHQpGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEF----SGGQRQRIAIARALILKPE 445
Cdd:PLN03211 149 -DILYPHLTVREtlVFCSLLRLPK-SLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 446 LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGE 509
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
295-468 |
1.25e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 295 IVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEIFFDDMPLHRwnrrqmlpVRPrmqvvfq 369
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTS----LLRILAGlarpdAGEVLWQGEPIRR--------QRD------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 370 DPNSSL---------NPRLSVlqiiEEGLRVHQPgLSAQQREQEVMRVMAEVGLdAGTRHRYPAEFSGGQRQRIAIARAL 440
Cdd:PRK13538 71 EYHQDLlylghqpgiKTELTA----LENLRFYQR-LHGPGDDEALWEALAQVGL-AGFEDVPVRQLSAGQQRRVALARLW 144
|
170 180
....*....|....*....|....*...
gi 658548496 441 ILKPELIILDEPTSSLDRTVQAQILALL 468
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
272-508 |
1.26e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-------QGEIFF 344
Cdd:CHL00131 4 NKPILEIKNLHAS-----------VNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAGhpaykilEGDILF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 345 DDmplhrwnrRQMLPVRPRMQ------VVFQDP----------------NS--------SLNPrLSVLQIIEEGLRVhqp 394
Cdd:CHL00131 69 KG--------ESILDLEPEERahlgifLAFQYPieipgvsnadflrlayNSkrkfqglpELDP-LEFLEIINEKLKL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 395 glsaqqreqevmrvmaeVGLDAGTRHRYPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLD----RTVQAQILALLK 469
Cdd:CHL00131 137 -----------------VGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMT 199
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 658548496 470 glQEKhrlAYIFISHdLQvvRALCH----QVIVLRQGEVVEQG 508
Cdd:CHL00131 200 --SEN---SIILITH-YQ--RLLDYikpdYVHVMQNGKIIKTG 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-236 |
1.71e-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: 72.30 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 21 TRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPVSY--PQGDILFHGSSLLHADEHTLRGIrgnkiamIF 98
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCS----TLLKALANRTEGNvsVEGDIHYNGIPYKEFAEKYPGEI-------IY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 99 qepmVSLNPLHSLEKQLYEVLslhrgmrkEAArgeiLDClertgirnaakRLNDFPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03233 88 ----VSEEDVHFPTLTVRETL--------DFA----LRC-----------KGNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 179 IADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLS-IVRKLADNVAVMQNGRCV 236
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-242 |
2.05e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.14 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPvSYP--QGDILFHGSSL 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKS----TLSKVIAGHP-AYKilEGDILFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 LHADEhTLRGIRGnkIAMIFQEPM----VS--------------------LNPLhslekQLYEVLSlhrgmrkeaargEI 134
Cdd:CHL00131 74 LDLEP-EERAHLG--IFLAFQYPIeipgVSnadflrlaynskrkfqglpeLDPL-----EFLEIIN------------EK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 135 LDCLERTGI---RNaakrLNDfphQLSGGERQRVMI-AMALLtRPELLIADEPTTALDVTVQAQILTLLRELRDELNmSL 210
Cdd:CHL00131 134 LKLVGMDPSflsRN----VNE---GFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SI 204
|
250 260 270
....*....|....*....|....*....|....*.
gi 658548496 211 LFITHnlsIVRKL----ADNVAVMQNGRCVEQNTAS 242
Cdd:CHL00131 205 ILITH---YQRLLdyikPDYVHVMQNGKIIKTGDAE 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-237 |
2.35e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLL-----PSppvsypQGDILFHgssl 78
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLagelePD------SGTVKLG---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 79 lhadeHTLrgirgnKIAMIFQEPMvSLNPlhslEKQLYEVLS-LHRGMRKEAARGeildCLERTGIRNAakRLNDFPHQL 157
Cdd:COG0488 376 -----ETV------KIGYFDQHQE-ELDP----DKTVLDELRdGAPGGTEQEVRG----YLGRFLFSGD--DAFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVtvqaqiltllrELRDELNMSL-------LFITHNLSIVRKLADNVAVM 230
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDI-----------ETLEALEEALddfpgtvLLVSHDRYFLDRVATRILEF 502
|
....*..
gi 658548496 231 QNGRCVE 237
Cdd:COG0488 503 EDGGVRE 509
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-270 |
2.43e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.32 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSYP---QGDILFHGSSLLHADEHTLRGIRgnkiAMIF 98
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGarvTGDVTLNGEPLAAIDAPRLARLR----AVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 99 Q--EPMVSLNplhslekqLYEVLSL------HRGMRKEAARGEILDC-LERTGIRNAAKRlnDFPhQLSGGERQRVMIAM 169
Cdd:PRK13547 90 QaaQPAFAFS--------AREIVLLgryphaRRAGALTHRDGEIAWQaLALAGATALVGR--DVT-TLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 170 AL---------LTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNT 240
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250 260 270
....*....|....*....|....*....|....*
gi 658548496 241 ASTLLSaPQH-----PYTQRLLDSEPSGDPVPLAA 270
Cdd:PRK13547 239 PADVLT-PAHiarcyGFAVRLVDAGDGVPPVIVPA 272
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-249 |
2.58e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.37 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTqgetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsyP-QGDILFHGSSLLHAD 82
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK------PdSGRIFLDGEDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHtLRGIRGnkIAMIFQEPMV--SLnplhSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGG 160
Cdd:COG1137 72 MH-KRARLG--IGYLPQEASIfrKL----TVEDNILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAY---SLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALD-VTVqAQILTLLRELRDElNMSLLfIT-HN----LSIVrklaDNVAVMQNGR 234
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIGVL-ITdHNvretLGIC----DRAYIISEGK 213
|
250
....*....|....*
gi 658548496 235 CVEQNTASTLLSAPQ 249
Cdd:COG1137 214 VLAEGTPEEILNNPL 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
3.60e-14 |
|
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: 71.35 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAF-STQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLP--------SPPVSY-PQGDILFHG 75
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEklsgsvsvPGSIAYvSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 76 SsllhadehtlrgIRGNkiaMIFQEPMvslnplhslEKQLYE-VL---SLHRGMrkeaargEILDCLERTGIrnAAKRLN 151
Cdd:cd03250 81 T------------IREN---ILFGKPF---------DEERYEkVIkacALEPDL-------EILPDGDLTEI--GEKGIN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 dfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILT--LLRELRDelNMSLLFITHNLSIVRKlADNVAV 229
Cdd:cd03250 128 -----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH-ADQIVV 199
|
....*
gi 658548496 230 MQNGR 234
Cdd:cd03250 200 LDNGR 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-279 |
5.26e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFstqGEtRTVVTDLSLQIQPGETLALVGESGSGKSVSalsiLRLLPSppVSYPQ-GDILFHGSSLL 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRY---GD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTT----LRMLLG--LTHPDaGSISLCGEPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRgirgnKIAMIFQepMVSLNPLHSLEKQLyEVLSLHRGMRKEAARGEILDCLERTGIRNAAkrlnDFP-HQLS 158
Cdd:PRK13537 73 SRARHARQ-----RVGVVPQ--FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKA----DAKvGELS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 658548496 239 ntastllSAPqhpytQRLLDSEPSGDPVPLAADSTPLLRVE 279
Cdd:PRK13537 220 -------GAP-----HALIESEIGCDVIEIYGPDPVALRDE 248
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-234 |
5.63e-14 |
|
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: 74.40 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAfsTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLLHADE 83
Cdd:COG4618 331 LSVENLTVV--PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKS----TLARLLVgvWPPTA---GSVRLDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRG---------------IRGNkIAMiFQEPmvslNPlhslEKqlyeVLslhrgmrkEAARgeildcleRTGIRNAAK 148
Cdd:COG4618 402 EELGRhigylpqdvelfdgtIAEN-IAR-FGDA----DP----EK----VV--------AAAK--------LAGVHEMIL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 149 RLND--------FPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIV 220
Cdd:COG4618 452 RLPDgydtrigeGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL 530
|
250
....*....|....
gi 658548496 221 RkLADNVAVMQNGR 234
Cdd:COG4618 531 A-AVDKLLVLRDGR 543
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
276-503 |
5.85e-14 |
|
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: 70.58 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 276 LRVEDLSVSFPirkgilRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEIFfddmplhrwnr 354
Cdd:cd03250 1 ISVEDASFTWD------SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVS----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 355 rqmlpVRPRMQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPglSAQQREQEVMRV--------------MAEVGlDAG 417
Cdd:cd03250 64 -----VPGSIAYVSQEPwiqNGT----------IRENILFGKP--FDEERYEKVIKAcalepdleilpdgdLTEIG-EKG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 418 TrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILA-LLKGLQEKHRlAYIFISHDLQVVRAlCHQV 496
Cdd:cd03250 126 I------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNK-TRILVTHQLQLLPH-ADQI 197
|
....*..
gi 658548496 497 IVLRQGE 503
Cdd:cd03250 198 VVLDNGR 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
302-506 |
7.78e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglalLRLIAS--------QGEIFFDDMPLHrwnrrqmlpvrprmqvvFQDPNS 373
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST-----LMKVLSgvyphgsyEGEILFDGEVCR-----------------FKDIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 374 S-------------LNPRLSVLQIIEEGLRVHQPGL-SAQQREQEVMRVMAEVGLD--AGTRhryPAEFSGGQRQRIAIA 437
Cdd:NF040905 75 SealgiviihqelaLIPYLSIAENIFLGNERAKRGViDWNETNRRARELLAKVGLDesPDTL---VTDIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 438 RALILKPELIILDEPTSSLDRTVQAQILALLKGLQEkHRLAYIFISHDLQVVRALCHQVIVLRQGEVVE 506
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
300-506 |
1.17e-13 |
|
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: 71.09 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFD-----DMPLHrwnrrqmlPVRPRMQVVFQDP-- 371
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVdIFDGKIVIDgidisKLPLH--------TLRSRLSIILQDPil 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 -----NSSLNPRLSVL-QIIEEGLRVHQPGLSAQQREQEVMRVMAEVGldagtrhrypAEFSGGQRQRIAIARALILKPE 445
Cdd:cd03288 107 fsgsiRFNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 446 LIILDEPTSSLDrtvqaqiLALLKGLQEKHRLAY-----IFISHDLQVVRAlCHQVIVLRQGEVVE 506
Cdd:cd03288 177 ILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
273-510 |
1.18e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 273 TPLLRVEDLSVSFPIRKGilrrivdqnpvLKNIRFSLRPGESLGLVGESGSGKST-----TGLallrLIASQGEIFFDDM 347
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKA-----------LSGAALNVYPGRVMALVGENGAGKSTmmkvlTGI----YTRDAGSILYLGK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 348 PlhrwnrrqmlpvrprmqVVFQDPNSS-----------LN--PRLSVLQIIEEGLRVHQP--GLSAQQREQEVMRVMAEV 412
Cdd:PRK10762 67 E-----------------VTFNGPKSSqeagigiihqeLNliPQLTIAENIFLGREFVNRfgRIDWKKMYAEADKLLARL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 413 GLDAGTrHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRAL 492
Cdd:PRK10762 130 NLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRLKEIFEI 207
|
250
....*....|....*...
gi 658548496 493 CHQVIVLRQGEVVeqGEC 510
Cdd:PRK10762 208 CDDVTVFRDGQFI--AER 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-232 |
1.23e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 10 NLSIAFSTQGETRtVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPvsypQGDILFHgssllhaDEHTLRGI 89
Cdd:PTZ00265 387 NVRFHYDTRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPT----EGDIIIN-------DSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 90 R----GNKIAMIFQEPMV--------------SLNPLHSLEKQL-------YEVLSLHRGMRKEAAR--GEILDCLERTG 142
Cdd:PTZ00265 454 NlkwwRSKIGVVSQDPLLfsnsiknnikyslySLKDLEALSNYYnedgndsQENKNKRNSCRAKCAGdlNDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 143 IRNAAKRLN-----------------DF---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVT 190
Cdd:PTZ00265 534 LIEMRKNYQtikdsevvdvskkvlihDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 658548496 191 VQAQILTLLRELRDELNMSLLFITHNLSIVRkLADNVAVMQN 232
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSN 654
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-200 |
1.37e-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: 69.44 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLlhadeHTLRGIRGNKIAMIFQ 99
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAglSPPLA---GRVLLNGGPL-----DFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 100 EPMVslnplhsleKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNaakrLNDFP-HQLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03231 81 APGI---------KTTLSVLENLRFWHADHSDEQVEEALARVGLNG----FEDRPvAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180
....*....|....*....|..
gi 658548496 179 IADEPTTALDVTVQAQILTLLR 200
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMA 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-249 |
1.76e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLP--SPPVSYPQGDIlfhgsSLLHAD 82
Cdd:PRK10895 3 TLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrdAGNIIIDDEDI-----SLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGIrgnkiAMIFQEPmvSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTGIRNAAKRLNdfpHQLSGGER 162
Cdd:PRK10895 74 ARARRGI-----GYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTAS 242
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
....*..
gi 658548496 243 TLLSAPQ 249
Cdd:PRK10895 223 EILQDEH 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
291-506 |
2.00e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 291 ILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHR---WNRRQMLPVRPRMQV 366
Cdd:PLN03130 1244 VLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKfglMDLRKVLGIIPQAPV 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 367 VFQ-------DPNSSLNPrlsvLQIIEEGLRVHQpglsaqqreQEVMRVMAeVGLDAGTrhrypAE----FSGGQRQRIA 435
Cdd:PLN03130 1324 LFSgtvrfnlDPFNEHND----ADLWESLERAHL---------KDVIRRNS-LGLDAEV-----SEagenFSVGQRQLLS 1384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 436 IARALILKPELIILDEPTSSLDRTVQAQIlalLKGLQEKHR-LAYIFISHDLQVVRAlCHQVIVLRQGEVVE 506
Cdd:PLN03130 1385 LARALLRRSKILVLDEATAAVDVRTDALI---QKTIREEFKsCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-234 |
2.16e-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: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAfsTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPS--PPVSypqGDILFHGSSLLHADE 83
Cdd:TIGR01842 317 LSVENVTIV--PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS----TLARLIVGiwPPTS---GSVRLDGADLKQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLrgirGNKIAMIFQEpmvslnplhslekqlyevLSLHRGMRKE-AARGEilDCLERTGIRNAAK------RLNDFPH- 155
Cdd:TIGR01842 388 ETF----GKHIGYLPQD------------------VELFPGTVAEnIARFG--ENADPEKIIEAAKlagvheLILRLPDg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 ----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVrKLAD 225
Cdd:TIGR01842 444 ydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVD 521
|
....*....
gi 658548496 226 NVAVMQNGR 234
Cdd:TIGR01842 522 KILVLQDGR 530
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-231 |
6.42e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNlsIAFSTqgETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSILRLLPSPPVsypqGDILFHGSSLLHADE 83
Cdd:PRK10247 6 PLLQLQN--VGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPTS----GTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRgirgNKIAMIFQEPMVslnplhsLEKQLYEVLSLHRGMRKEAA-RGEILDCLERTGIRNA--AKRLNDfphqLSGG 160
Cdd:PRK10247 77 EIYR----QQVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPdPAIFLDDLERFALPDTilTKNIAE----LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVrKLADNVAVMQ 231
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQ 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
300-508 |
6.95e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.67 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--------GEIFFDDMPLHRWNRRqmlpvrPRMQVVFQDP 371
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCST----LLKALANRtegnvsveGDIHYNGIPYKEFAEK------YPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSLNPRLSVLQIIEeglrvhqpgLSAQQREQEVMRVmaevgldagtrhrypaeFSGGQRQRIAIARALILKPELIILDE 451
Cdd:cd03233 91 EDVHFPTLTVRETLD---------FALRCKGNEFVRG-----------------ISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIF-ISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-230 |
7.74e-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: 68.55 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 33 QPGETLALVGESGSGKSvSALSIL--RLLP------SPPvSYPqgDIL--FHGSSLlhadEHTLRGIRGNKIAMIFQEPM 102
Cdd:cd03236 24 REGQVLGLVGPNGIGKS-TALKILagKLKPnlgkfdDPP-DWD--EILdeFRGSEL----QNYFTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 VSLNPlHSLEKQLYEVLSlhrgmrKEAARGEILDCLERTGIRNAAKRLNDfphQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:cd03236 96 VDLIP-KAVKGKVGELLK------KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 658548496 183 PTTALDVTVQAQILTLLRELRDELNmSLLFITHNLSIVRKLADNVAVM 230
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-230 |
8.29e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 21 TRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqgdilfhgssllhadehtLRGIRGNKIAMIFQE 100
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL--------------------------AGALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PmvslnplhslEKQLYEVLSlhrgmrkeaargeILDCLERTGIRNAAKR------LNDF------PHQLSGGERQRVMIA 168
Cdd:COG2401 92 P----------DNQFGREAS-------------LIDAIGRKGDFKDAVEllnavgLSDAvlwlrrFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 169 MALLTRPELLIADEPTTALDVTVqAQILTL-LRELRDELNMSLLFITHNLSIVRKLADNVAVM 230
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
301-508 |
8.62e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.35 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFDDMPLHRWNRRQMlpvRPRMQVVFQDP---NSSLn 376
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVeVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPvlfDGTV- 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 377 pRLSVlqiieeglrvhQPGLSAQqrEQEVMRVMAEVGLdagtRHRYPAE--------------FSGGQRQRIAIARALIL 442
Cdd:PTZ00243 1401 -RQNV-----------DPFLEAS--SAEVWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 443 KPE-LIILDEPTSS----LDRTVQAQILALLKglqekhrlAY--IFISHDLQVVrALCHQVIVLRQGEVVEQG 508
Cdd:PTZ00243 1463 KGSgFILMDEATANidpaLDRQIQATVMSAFS--------AYtvITIAHRLHTV-AQYDKIIVMDHGAVAEMG 1526
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-238 |
1.25e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLL-PSppvsypQGDILFHGSSLlhadEHTLRGIRG--NKIAMIFQE 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ------KGAVLWQGKPL----DYSKRGLLAlrQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PmvslnplhslEKQLYEVlslhrgmrkeAARGEILDCLERTGIRNA--AKRLND---------FPHQ----LSGGERQRV 165
Cdd:PRK13638 86 P----------EQQIFYT----------DIDSDIAFSLRNLGVPEAeiTRRVDEaltlvdaqhFRHQpiqcLSHGQKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 166 MIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNmSLLFITHNLSIVRKLADNVAVMQNGRCVEQ 238
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
301-490 |
1.41e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMplHRWNRRQMLPVRPRMQVVFQDP---- 371
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIINDS--HNLKDINLKWWRSKIGVVSQDPllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSLNP------RLSVLQIIEEGLrvHQPGLSAQQ--------------------------------------REQEVMR 407
Cdd:PTZ00265 474 NSIKNNikyslySLKDLEALSNYY--NEDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtiKDSEVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 408 VMAEVGLD---AGTRHRY-------PAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRL 477
Cdd:PTZ00265 552 VSKKVLIHdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250
....*....|...
gi 658548496 478 AYIFISHDLQVVR 490
Cdd:PTZ00265 632 ITIIIAHRLSTIR 644
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-201 |
1.51e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLsiAFStQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGSSLLHAD 82
Cdd:PRK13538 1 MLEARNL--ACE-RDE-RILFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILAglARPDA---GEVLWQGEPIRRQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLR---------GIRGnkiamifqepmvSLNPLhslekqlyEVLSLHRGMRKEAARGEILDCLERTGIRnaakRLNDF 153
Cdd:PRK13538 70 DEYHQdllylghqpGIKT------------ELTAL--------ENLRFYQRLHGPGDDEALWEALAQVGLA----GFEDV 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 658548496 154 P-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRE 201
Cdd:PRK13538 126 PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-504 |
2.00e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHGSSL-LHADEHTLRgirgNKIAMIFQEpmvsL 105
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKS----TLLKCLFGI-YQKDSGSILFQGKEIdFKSSKEALE----NGISMVHQE----L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 106 NPLhsLEKQLYEVLSL-----------HRGMRKEAARgeILDCLErTGIRNAAKRLNdfphqLSGGERQRVMIAMALLTR 174
Cdd:PRK10982 83 NLV--LQRSVMDNMWLgryptkgmfvdQDKMYRDTKA--IFDELD-IDIDPRAKVAT-----LSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 175 PELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTLlSAPQ----- 249
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL-TMDKiiamm 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 250 --HPYTQRLldsePSGDPVPlaadSTPLLRVEDLSVSfpirkgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSgKST 327
Cdd:PRK10982 231 vgRSLTQRF----PDKENKP----GEVILEVRNLTSL-------------RQPSIRDVSFDLHKGEILGIAGLVGA-KRT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 328 TGLALLRLI--ASQGEIFFDDMPLHrwNRRQMLPVRPRMQVVFQDPNSS---------LNPRLSVLQIIEEGLRVhqpgL 396
Cdd:PRK10982 289 DIVETLFGIreKSAGTITLHGKKIN--NHNANEAINHGFALVTEERRSTgiyayldigFNSLISNIRNYKNKVGL----L 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 397 SAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHR 476
Cdd:PRK10982 363 DNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK 442
|
490 500
....*....|....*....|....*...
gi 658548496 477 lAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK10982 443 -GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
279-505 |
2.07e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 279 EDLSVSFPIRKGilrrivdqnpvLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLIA-SQGEIFFDDMPLHRWNRRQM 357
Cdd:PRK10982 2 SNISKSFPGVKA-----------LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkDSGSILFQGKEIDFKSSKEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 358 LPVRPRMqvVFQDPNSSLnpRLSVLQIIEEGlRVHQPGLSAQQRE--QEVMRVMAEVGLDAGTRHRYpAEFSGGQRQRIA 435
Cdd:PRK10982 71 LENGISM--VHQELNLVL--QRSVMDNMWLG-RYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKV-ATLSVSQMQMIE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 436 IARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHrLAYIFISHDLQVVRALCHQVIVLRQGEVV 505
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
301-505 |
2.28e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLI-----ASQGEIFFDDMPLHRWNR----RQMLPVRPRMQVVFQdp 371
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLcgdprATSGRIVFDGKDITDWQTakimREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 nsslnpRLSVlqiiEEGLRVHQPGLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PRK11614 94 ------RMTV----EENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658548496 452 PTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRaLCHQVIVLRQGEVV 505
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALK-LADRGYVLENGHVV 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-247 |
2.72e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.59 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTLRgirgNKIAMIFQEPMV 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGLNIAKIGLHDLR----FKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 -------SLNPLHSL-EKQLYEVLSLHRGMRKEAARGEILD--CLErtGIRNaakrlndfphqLSGGERQRVMIAMALLT 173
Cdd:TIGR00957 1372 fsgslrmNLDPFSQYsDEEVWWALELAHLKTFVSALPDKLDheCAE--GGEN-----------LSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 174 RPELLIADEPTTALDVTVQAQILTLLRELRDELnmSLLFITHNLSIVRKLAdNVAVMQNGRCVEQNTASTLLSA 247
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
288-508 |
2.77e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.59 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 288 RKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRLI-ASQGEIFFD-----DMPLHRwnrrqmlpVR 361
Cdd:TIGR00957 1288 RNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDglniaKIGLHD--------LR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 362 PRMQVVFQDPnsslnprlsvlqIIEEG-LRVHQPGLSAQQREQ-----EVMRVMAEV-GLDAGTRHRYpAE----FSGGQ 430
Cdd:TIGR00957 1360 FKITIIPQDP------------VLFSGsLRMNLDPFSQYSDEEvwwalELAHLKTFVsALPDKLDHEC-AEggenLSVGQ 1426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 431 RQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKhrLAYIFISHDLQVVRALChQVIVLRQGEVVEQG 508
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-236 |
5.62e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPPVSypqGDILFHGSSLlhaD 82
Cdd:PLN03211 62 KRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT---GTILANNRKP---T 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRgirgnKIAMIFQEPMvsLNPLHSLEKQLY--EVLSLHRGMRKEAARGEILDCLERTGIRNAAKRL--NDFPHQLS 158
Cdd:PLN03211 136 KQILK-----RTGFVTQDDI--LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-234 |
7.36e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 27 DLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPvSYPQGDiLFHGSSLLHADEHTLRGIrgnkiAMIFQEpmvsln 106
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLE-DITSGD-LFIGEKRMNDVPPAERGV-----GMVFQS------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 107 plhsleKQLYEVLSLHRGMR-----KEAARGEILDCLERTG-IRNAAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK11000 84 ------YALYPHLSVAENMSfglklAGAKKEEINQRVNQVAeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 658548496 181 DEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
1.07e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNLSIAFSTQGetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpSPPVsypqGDIlfhgsSLLH 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-SPDA----GKI-----TVLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEHTLRGIRGNKIAMIFQepMVSLNPLHSLEKQLYeVLSLHRGMRKEAARGEILDCLERTGIRNAAK-RLNDfphqLSG 159
Cdd:PRK13536 103 VPVPARARLARARIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADaRVSD----LSG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 160 GERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-238 |
1.23e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.02 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSvsalSILRL---LPSppVSypQGDILFhGSSLLHADEHTLRGIrgnkiAMIFQE 100
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMvagLER--IT--SGEIWI-GGRVVNELEPADRDI-----AMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 pmVSLNPLHSLEKQLYEVLSLhRGMRKEaargEIldcleRTGIRNAAK--RLNDF----PHQLSGGERQRVMIAMALLTR 174
Cdd:PRK11650 85 --YALYPHMSVRENMAYGLKI-RGMPKA----EI-----EERVAEAARilELEPLldrkPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 175 PELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQNGRcVEQ 238
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQ 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
297-508 |
2.25e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKST---------TGLALLRLIASQGEIFFDDMPLHRWNRRQMlpvrPRMQVV 367
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTllkalagdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRL----ARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 368 FQDPNSSLNPrLSVLQIIEEGLRVH-QPGLSAQQREQEVM-RVMAEVGLDAGTRhRYPAEFSGGQRQRIAIARAL----- 440
Cdd:PRK13547 88 LPQAAQPAFA-FSAREIVLLGRYPHaRRAGALTHRDGEIAwQALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 441 ----ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-234 |
2.57e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSiAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRllpsppvSYP---QGDILFHGSSLlhA 81
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-------AYPgkfEGNVFINGKPV--D 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 DEHTLRGIRgNKIAMIFQE-PMVSLNPLHSLEKQLyeVLSLhrgMRKEAARGEILDCLERTGIRNAAKRLN------DFP 154
Cdd:TIGR02633 327 IRNPAQAIR-AGIAMVPEDrKRHGIVPILGVGKNI--TLSV---LKSFCFKMRIDAAAELQIIGSAIQRLKvktaspFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNG 233
Cdd:TIGR02633 401 iGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
.
gi 658548496 234 R 234
Cdd:TIGR02633 480 K 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
297-523 |
3.48e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIrfslrpgESLGLVGESGSGKSTTglallrLIASQGEIFFDDMPLHRWNRRQMlpvRPRMQVVFQDPnssLN 376
Cdd:PTZ00265 1247 EQNVGMKNV-------NEFSLTKEGGSGEDST------VFKNSGKILLDGVDICDYNLKDL---RNLFSIVSQEP---ML 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 377 PRLSVLQIIEEGlrvhqpglSAQQREQEVMRVMAEVGLDAGTRH----------RYPAEFSGGQRQRIAIARALILKPEL 446
Cdd:PTZ00265 1308 FNMSIYENIKFG--------KEDATREDVKRACKFAAIDEFIESlpnkydtnvgPYGKSLSGGQKQRIAIARALLREPKI 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 447 IILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRAlCHQVIVL----RQGEVVE-QGECQRVFSAPTQRY 521
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVY 1458
|
..
gi 658548496 522 TR 523
Cdd:PTZ00265 1459 KK 1460
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
157-247 |
4.70e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRC- 235
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIs 474
|
90
....*....|....*.
gi 658548496 236 ----VEQNTASTLLSA 247
Cdd:PRK10762 475 geftREQATQEKLMAA 490
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-244 |
5.07e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 23 TVVTDLSLQIQPGETLALVGESGSGKS--VSALSILrLLPSppvsypQGDILFhgsslLHADEHTlrgirgNKIAMIFQE 100
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPD------TGTIEW-----IFKDEKN------KKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 PMVSLNPLHSLEKQLYEVLSLHR-----------------------------GMRKEAARGEILDCLERTGIrnAAKRLN 151
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRrvgvvfqfaeyqlfeqtiekdiifgpvsmGVSKEEAKKRAAKYIELVGL--DESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 152 DFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQ 231
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....
gi 658548496 232 NGRCV-EQNTASTL 244
Cdd:PRK13651 240 DGKIIkDGDTYDIL 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-234 |
5.71e-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: 65.42 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQGetRTVVTDLSLQIQPGETLALVGESGSGKSVSaLSILRLLpSPPVSypqGDILFHGSSLlhadE 83
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTGL-LPPTS---GTVLVGGKDI----E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRgNKIAMIFQEPMVsLNPLHSLEKQLYevLSLHRGMRKEAARGEILDCLERTGIRNaaKRlNDFPHQLSGGERQ 163
Cdd:TIGR01257 996 TNLDAVR-QSLGMCPQHNIL-FHHLTVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTGLHH--KR-NEEAQDLSGGMQR 1068
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDelNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-504 |
7.87e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 21 TRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDILFHGSSLLhadehtlrgirgnkiAMIFQE 100
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKS----TLLALLKNE-ISADGGSYTFPGNWQL---------------AWVNQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 101 -PMVSLNPL----------HSLEKQLYEVLSLHRGMRKEAARGEiLDCLERTGIRNAAKRLND---FPHQ--------LS 158
Cdd:PRK10636 73 tPALPQPALeyvidgdreyRQLEAQLHDANERNDGHAIATIHGK-LDAIDAWTIRSRAASLLHglgFSNEqlerpvsdFS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVqaqILTLLRELRDeLNMSLLFITHNLSIVRKLADNVAVMQ------- 231
Cdd:PRK10636 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKS-YQGTLILISHDRDFLDPIVDKIIHIEqqslfey 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 232 --NGRCVEQNTASTL---------------------------------------------LSAPQH-----PYTQRLLDS 259
Cdd:PRK10636 228 tgNYSSFEVQRATRLaqqqamyesqqervahlqsyidrfrakatkakqaqsrikmlermeLIAPAHvdnpfHFSFRAPES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 260 EPSgdpvplaadstPLLRVEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ 339
Cdd:PRK10636 308 LPN-----------PLLKMEKVSAGY-----------GDRIILDSIKLNLVPGSRIGLLGRNGAGKST----LIKLLAGE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 340 GEIFFDDMPLHRWNRrqmLPVRPRMQVVFqdpnssLNPRLSVLQiieeglrvHQPGLSAQQREQEVMRVMAEVGLDAGTR 419
Cdd:PRK10636 362 LAPVSGEIGLAKGIK---LGYFAQHQLEF------LRADESPLQ--------HLARLAPQELEQKLRDYLGGFGFQGDKV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 420 HRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTV-QAQILALLkglqeKHRLAYIFISHDLQVVRALCHQVIV 498
Cdd:PRK10636 425 TEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALI-----DFEGALVVVSHDRHLLRSTTDDLYL 499
|
....*.
gi 658548496 499 LRQGEV 504
Cdd:PRK10636 500 VHDGKV 505
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-246 |
9.11e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLLHADEHTLRGIrgnkIAMIFQEPMV 103
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI-----VELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 -------SLNPLhslekqlyevlslhrgmrKEAARGEILDCLERTGIRNAAKRlNDFP---------HQLSGGERQRVMI 167
Cdd:PLN03232 1322 fsgtvrfNIDPF------------------SEHNDADLWEALERAHIKDVIDR-NPFGldaevseggENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 168 AMALLTRPELLIADEPTTALDVTVQAQIltlLRELRDEL-NMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLI---QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-233 |
1.77e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGETRTVvtdlSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPV--SYPQGDILFHGSSLLH 80
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAV----DLNIHHGEMVALLGPSGSGKS----TLLRHLSGLITgdKSAGSHIELLGRTVQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 81 ADEhTLRGIRGNK--IAMIFQEPMVsLNPLHSLEKQLYEVLSLHRGMR------KEAARGEILDCLERTGIRNaakrlnd 152
Cdd:PRK09984 74 EGR-LARDIRKSRanTGYIFQQFNL-VNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVGMVH------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 153 FPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVA 228
Cdd:PRK09984 145 FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
....*
gi 658548496 229 VMQNG 233
Cdd:PRK09984 225 ALRQG 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-253 |
1.93e-10 |
|
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: 61.46 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQgeTRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLLHADEHT 85
Cdd:cd03288 20 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM-----VDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRgirgNKIAMIFQEPMV-------SLNP-LHSLEKQLYEVLSLH--RGMRKEAARGeiLDCLERTGIRNaakrlndfph 155
Cdd:cd03288 93 LR----SRLSIILQDPILfsgsirfNLDPeCKCTDDRLWEALEIAqlKNMVKSLPGG--LDAVVTEGGEN---------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 qLSGGERQRVMIAMALLTRPELLIADEPTTALDVT----VQAQILTLLRElrdelnMSLLFITHNLSIVRKlADNVAVMQ 231
Cdd:cd03288 157 -FSVGQRQLFCLARAFVRKSSILIMDEATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTILD-ADLVLVLS 228
|
250 260
....*....|....*....|..
gi 658548496 232 NGRCVEQNTASTLLSAPQHPYT 253
Cdd:cd03288 229 RGILVECDTPENLLAQEDGVFA 250
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-254 |
2.05e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLL-----------------------------------------PSP 62
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 63 PVSYPQGDILFHGSSLLHAD-----EHTLRGIRgNKIAMIFQEPMVSLNPLHSLEKQLYEVLSLHRGMR--KEAARGEIL 135
Cdd:PTZ00265 1263 EGGSGEDSTVFKNSGKILLDgvdicDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRacKFAAIDEFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 136 DCLERTGIRNAAKrlndFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITH 215
Cdd:PTZ00265 1342 ESLPNKYDTNVGP----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 658548496 216 NLSIVRKlADNVAVMQN----GRCVE-QNTASTLLSAPQHPYTQ 254
Cdd:PTZ00265 1418 RIASIKR-SDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKK 1460
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
156-246 |
2.39e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRC 235
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
90
....*....|.
gi 658548496 236 VEQNTASTLLS 246
Cdd:PRK09700 488 TQILTNRDDMS 498
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
287-513 |
2.42e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 287 IRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ---------GEIFFDDMPLHRWNRRQm 357
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCST----LLKTIASNtdgfhigveGVITYDGITPEEIKKHY- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 358 lpvrpRMQVVFQDPNSSLNPRLSVLQIIEEGLRVHQP-----GLSAQQR-EQEVMRVMAEVGLDAGTRHRYPAEF----S 427
Cdd:TIGR00956 137 -----RGDVVYNAETDVHFPHLTVGETLDFAARCKTPqnrpdGVSREEYaKHIADVYMATYGLSHTRNTKVGNDFvrgvS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 428 GGQRQRIAIARALILKPELIILDEPTSSLDrtvQAQILALLKGLQEKHRL----AYIFISHDLQVVRALCHQVIVLRQGE 503
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLD---SATALEFIRALKTSANIldttPLVAIYQCSQDAYELFDKVIVLYEGY 288
|
250
....*....|
gi 658548496 504 VVEQGECQRV 513
Cdd:TIGR00956 289 QIYFGPADKA 298
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-246 |
4.36e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLLHADEHTLRGIRGnkiaMIFQEPMV 103
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI-----VELERGRILIDGCDISKFGLMDLRKVLG----IIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 104 -------SLNPL--HSlEKQLYEvlSLHRGMRKEAargeildclertgIRNAAKRLN----DFPHQLSGGERQRVMIAMA 170
Cdd:PLN03130 1325 fsgtvrfNLDPFneHN-DADLWE--SLERAHLKDV-------------IRRNSLGLDaevsEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 171 LLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMslLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTLLS 246
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
302-513 |
4.88e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQgeiffdDMPlhrwnRRQMLPVRPRMQVVfqDPNSSLNPRLSV 381
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST----LSNLIAGV------TMP-----NKGTVDIKGSAALI--AISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 382 LQIIE-EGLRVhqpGLSAQQREQEVMRVM--AEVGldaGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDR 458
Cdd:PRK13545 103 IENIElKGLMM---GLTKEKIKEIIPEIIefADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 459 TVQAQILALLKGLQEKHRLAYiFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-237 |
6.43e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSilrLLPSPPVSYPQGDILFHGSSLLHADEH 84
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 85 TLrgiRGNKIAMIFQEPMvslnPLHSLEKQLYEVLSLH--RGMRKEAArgeiLDCLERTGIRNAAKRLNDFPHQL----- 157
Cdd:PRK09580 74 DR---AGEGIFMAFQYPV----EIPGVSNQFFLQTALNavRSYRGQEP----LDRFDFQDLMEEKIALLKMPEDLltrsv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 158 ----SGGERQRVMI-AMALLtRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLA-DNVAVMQ 231
Cdd:PRK09580 143 nvgfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLY 220
|
....*.
gi 658548496 232 NGRCVE 237
Cdd:PRK09580 221 QGRIVK 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-201 |
1.17e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAfstQGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLP--SPPVSypqGDILFHGS----S 77
Cdd:PRK13539 1 MMLEGEDLACV---RGG-RVLFSGLSFTLAAGEALVLTGPNGSGKT----TLLRLIAglLPPAA---GTIKLDGGdiddP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 78 LLHADEHTLrgirGNKIAMifqepmvslNPLHSLEkqlyEVLSLHRGMRKeAARGEILDCLERTGIRNAAkrlnDFPHQ- 156
Cdd:PRK13539 70 DVAEACHYL----GHRNAM---------KPALTVA----ENLEFWAAFLG-GEELDIAAALEAVGLAPLA----HLPFGy 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRE 201
Cdd:PRK13539 128 LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-242 |
2.08e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFsTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPPVSYPQGDilfhgSSLLHAD 82
Cdd:TIGR00956 56 KILTRGFRKLKKF-RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCS----TLLKTIASNTDGFHIGV-----EGVITYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGIRGNKIAMIFqepMVSLNPLHSLEKQLYEVLSLHRGMRKEAARGEILDCLERTG-IRNAAKRL----------- 150
Cdd:TIGR00956 126 GITPEEIKKHYRGDVV---YNAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEYAKhIADVYMATyglshtrntkv 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 151 -NDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSI-VRKLADNVA 228
Cdd:TIGR00956 203 gNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVI 282
|
250
....*....|....
gi 658548496 229 VMQNGRCVEQNTAS 242
Cdd:TIGR00956 283 VLYEGYQIYFGPAD 296
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
114-504 |
2.82e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 114 QLYEVLSLHRGMRKEAARGEILDCLERTGiRNAAKRLNDFphqlSGGERQRVMIAMALLTRPELLIADEPTTALDV---- 189
Cdd:PLN03073 307 EIYKRLELIDAYTAEARAASILAGLSFTP-EMQVKATKTF----SGGWRMRIALARALFIEPDLLLLDEPTNHLDLhavl 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 190 ------TVQAQILTLLRELRDELNMSLLFITH--NLSIV----------RKLADNVAVMQNGRCVEQNTASTLLS----- 246
Cdd:PLN03073 382 wletylLKWPKTFIVVSHAREFLNTVVTDILHlhGQKLVtykgdydtfeRTREEQLKNQQKAFESNERSRSHMQAfidkf 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 247 ---APQHPYTQ---RLLDSEPSGD------------PVPLAADSTPLLRVEDLSVSFPirkgilrrivdQNPVL-KNIRF 307
Cdd:PLN03073 462 rynAKRASLVQsriKALDRLGHVDavvndpdykfefPTPDDRPGPPIISFSDASFGYP-----------GGPLLfKNLNF 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 308 SLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFfddmplhrwnrrqmLPVRPRMQVVFQDP----NSSLNPR 378
Cdd:PLN03073 531 GIDLDSRIAMVGPNGIGKST----ILKLISgelqpSSGTVF--------------RSAKVRMAVFSQHHvdglDLSSNPL 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LSVLQ----IIEEGLRVHqpglsaqqreqevmrvMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTS 454
Cdd:PLN03073 593 LYMMRcfpgVPEQKLRAH----------------LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 658548496 455 SLD-RTVQAQI--LALLKGlqekhrlAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PLN03073 657 HLDlDAVEALIqgLVLFQG-------GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
269-502 |
3.65e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 269 AADSTPLLRVEDLSVSFPirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTglalLRLIASQGEIFFDDMP 348
Cdd:TIGR01257 1931 GGNKTDILRLNELTKVYS---------GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDAT 1997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 349 LHRWNrrqmlpVRPRMQVVFQdpNSSLNPRLSVLQIIEEG-----LRVHQPGLSAQQREQEVMRVMAEVGLDAgTRHRYP 423
Cdd:TIGR01257 1998 VAGKS------ILTNISDVHQ--NMGYCPQFDAIDDLLTGrehlyLYARLRGVPAEEIEKVANWSIQSLGLSL-YADRLA 2068
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 424 AEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIVLRQG 502
Cdd:TIGR01257 2069 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
300-487 |
5.05e-09 |
|
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: 56.57 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEIFFDDMpLHRWNRRQMLPVRPRMQVVFqdpnSSLNPR 378
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAY----AAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 379 LsVLQIIEEGLRVHQPglSAQQREQEVM---RVMAEVGL-------DAGTRHrypAEFSGGQRQRIAIARALILKPELII 448
Cdd:cd03290 90 L-LNATVEENITFGSP--FNKQRYKAVTdacSLQPDIDLlpfgdqtEIGERG---INLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 658548496 449 LDEPTSSLDRTVQAQIL--ALLKGLQEKHRlAYIFISHDLQ 487
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqeGILKFLQDDKR-TLVLVTHKLQ 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
302-457 |
9.32e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEI--FFDDMPLHRWNRRqmlpVRPRMQVVFQDPNSS 374
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAgarkiQQGRVevLGGDMADARHRRA----VCPRIAYMPQGLGKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRLSVlqiiEEGLRVHQP--GLSAQQREQEVMRVMAEVGLDAgTRHRyPA-EFSGGQRQRIAIARALILKPELIILDE 451
Cdd:NF033858 89 LYPTLSV----FENLDFFGRlfGQDAAERRRRIDELLRATGLAP-FADR-PAgKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
....*.
gi 658548496 452 PTSSLD 457
Cdd:NF033858 163 PTTGVD 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-236 |
9.35e-09 |
|
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: 55.33 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVsalsILRLLPS-PPVSYPQGDILFHGSSLlha 81
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGrKTAGVITGEILINGRPL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 82 dEHTLRGIRGnkiamifqepMVSLNPLHSLEKQLYEVLSLHRGMRkeaargeildclertgirnaakrlndfphQLSGGE 161
Cdd:cd03232 74 -DKNFQRSTG----------YVEQQDVHSPNLTVREALRFSALLR-----------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 162 RQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSI-VRKLADNVAVMQ-NGRCV 236
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSAsIFEKFDRLLLLKrGGKTV 189
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
311-492 |
9.57e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 311 PGESLGLVGESGSGKSTTGLALLRLIASQGEiffddmplhrwnrrqmlpvrprmQVVFQDPNSSLNPRLSVLQIIEeglr 390
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-----------------------GVIYIDGEDILEEVLDQLLLII---- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 391 vhqpglsaqqreqevmrvmaevgldagtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILAL--- 467
Cdd:smart00382 54 ----------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170 180
....*....|....*....|....*..
gi 658548496 468 --LKGLQEKHRLAYIFISHDLQVVRAL 492
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
299-503 |
1.06e-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: 56.40 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 299 NPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEIFFDDM----PLHRWnrrqMLPVRPRMQVVFQDPNS 373
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRisfsSQFSW----IMPGTIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 374 SLNPRlSVLQiieeglrvhqpglsAQQREQEVMR-------VMAEVGLDagtrhrypaeFSGGQRQRIAIARALILKPEL 446
Cdd:cd03291 126 EYRYK-SVVK--------------ACQLEEDITKfpekdntVLGEGGIT----------LSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 447 IILDEPTSSLDRTVQAQIL--ALLKGLQEKHRlayIFISHDLQVVRAlCHQVIVLRQGE 503
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFesCVCKLMANKTR---ILVTSKMEHLKK-ADKILILHEGS 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-243 |
1.12e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
....*...
gi 658548496 237 E-QNTAST 243
Cdd:PRK10982 471 GiVDTKTT 478
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-485 |
2.36e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 19 GETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL-----------RLLPSPPVSY----PQGDilfhgssllhaDE 83
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkefegeaRPAPGIKVGYlpqePQLD-----------PE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGI-------------RGNKIAMIFQEPMVSLNPLhsLEKQ--LYEVLslhrgmrkEAARGEILDC-LERtgirnAA 147
Cdd:PRK11819 85 KTVRENveegvaevkaaldRFNEIYAAYAEPDADFDAL--AAEQgeLQEII--------DAADAWDLDSqLEI-----AM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 148 KRLN----DFP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDvtvqAQ-ILTLLRELRDeLNMSLLFITHNlsivR 221
Cdd:PRK11819 150 DALRcppwDAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHD-YPGTVVAVTHD----R 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 222 KLADNVA----VMQNGRC-------------------VEQNTASTLL-----------SAP------------------Q 249
Cdd:PRK11819 221 YFLDNVAgwilELDRGRGipwegnysswleqkakrlaQEEKQEAARQkalkrelewvrQSPkarqakskarlaryeellS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 250 HPYTQRLLDSE---PS----GDPVplaadstplLRVEDLSVSFPIRkgilrrivdqnpVL-KNIRFSLRPGESLGLVGES 321
Cdd:PRK11819 301 EEYQKRNETNEifiPPgprlGDKV---------IEAENLSKSFGDR------------LLiDDLSFSLPPGGIVGIIGPN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 322 GSGKSTtglaLLRLIASQ-----GEIffddmplhrwnrrqmlPVRPRMQVVFQDPN-SSLNPRLSVLQIIEEGLRVHQPG 395
Cdd:PRK11819 360 GAGKST----LFKMITGQeqpdsGTI----------------KIGETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKVG 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 396 lsaqQREqevMRVMAEVG---LDAGTRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQaqilALLKGL 471
Cdd:PRK11819 420 ----NRE---IPSRAYVGrfnFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDvETLR----ALEEAL 488
|
570
....*....|....
gi 658548496 472 QEKHRLAYIfISHD 485
Cdd:PRK11819 489 LEFPGCAVV-ISHD 501
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
308-457 |
2.99e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 308 SLRPGESLGLVGESGSGKSTtglaLLRLIASQGeifFDDMPlhrwNRRQMLPVRprmQVVFQDPNSSLNPRLSV----LQ 383
Cdd:PLN03073 199 TLAFGRHYGLVGRNGTGKTT----FLRYMAMHA---IDGIP----KNCQILHVE---QEVVGDDTTALQCVLNTdierTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 384 IIEEGLRVHQ-------PGLSAQ---------------QREQEVMR----------------VMAEVGLDAGTRHRYPAE 425
Cdd:PLN03073 265 LLEEEAQLVAqqrelefETETGKgkgankdgvdkdavsQRLEEIYKrlelidaytaearaasILAGLSFTPEMQVKATKT 344
|
170 180 190
....*....|....*....|....*....|..
gi 658548496 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 ... |
279-471 |
5.22e-08 |
|
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: 53.02 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 279 EDLSVSFPIRKGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ-------GEIFFDDMPLHR 351
Cdd:cd03232 7 KNLNYTVPVKGGKRQ-------LLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGRktagvitGEILINGRPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 WNRRQMLPVRprmQVVFQDPNSSlnprlsvlqiIEEGLRvhqpgLSAQQReqevmrvmaevGLdagtrhrypaefSGGQR 431
Cdd:cd03232 76 NFQRSTGYVE---QQDVHSPNLT----------VREALR-----FSALLR-----------GL------------SVEQR 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 658548496 432 QRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGL 471
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
302-490 |
5.54e-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: 52.71 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTTglaLLRLIASQGEIFFDDMplhrwnrrqmLPVRPRMQVVFQDPnsslnprlsv 381
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---VNEGLYASGKARLISF----------LPKFSRNKLIFIDQ---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 382 lqiieeglrvhqpglsaqqreqevMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALILKPE--LIILDEPTSSLDRT 459
Cdd:cd03238 68 ------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|..
gi 658548496 460 VQAQILALLKGL-QEKHRLayIFISHDLQVVR 490
Cdd:cd03238 124 DINQLLEVIKGLiDLGNTV--ILIEHNLDVLS 153
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
297-491 |
6.79e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQnPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDdmplhRWNRRQMLPVRPRmQVVFQDP 371
Cdd:PRK13540 13 DQ-PLLQQISFHLPAGGLLHLKGSNGAGKTT----LLKLIAgllnpEKGEILFE-----RQSIKKDLCTYQK-QLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSLNPRLSVLQIIEEGLRVHQPGLSAqqreQEVMRVMA-EVGLDagtrhrYPAE-FSGGQRQRIAIARALILKPELIIL 449
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVGI----TELCRLFSlEHLID------YPCGlLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 658548496 450 DEPTSSLDrtvQAQILALLKGLQEkHRL---AYIFISH-DLQVVRA 491
Cdd:PRK13540 152 DEPLVALD---ELSLLTIITKIQE-HRAkggAVLLTSHqDLPLNKA 193
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-234 |
7.35e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFstqGEtRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSPpVSYPQGDI-LFHGSSLLHAD 82
Cdd:PRK10636 311 PLLKMEKVSAGY---GD-RIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLLAGE-LAPVSGEIgLAKGIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTLRGIRGNKIAMifqEPMVSLNPlHSLEKQLYEVLSlhrgmrkeaargeildclertGIRNAAKRLNDFPHQLSGGER 162
Cdd:PRK10636 382 QHQLEFLRADESPL---QHLARLAP-QELEQKLRDYLG---------------------GFGFQGDKVTEETRRFSGGEK 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQaQILTllrELRDELNMSLLFITHNLSIVRKLADNVAVMQNGR 234
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMR-QALT---EALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-192 |
7.92e-08 |
|
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: 55.30 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQGetRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSppvsypQGDILFHGSSLLHADEHT 85
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LR---GIRGNKIAMIFQEPMVSLNPLHSLEKQlyevlslhrgmrkeaargEILDCLERTGIRNAAKR--------LNDFP 154
Cdd:TIGR01271 1290 WRkafGVIPQKVFIFSGTFRKNLDPYEQWSDE------------------EIWKVAEEVGLKSVIEQfpdkldfvLVDGG 1351
|
170 180 190
....*....|....*....|....*....|....*....
gi 658548496 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VTVQ 192
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-217 |
9.61e-08 |
|
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: 51.59 E-value: 9.61e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 155 HQLSGGERQRVMIAMAL----LTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMsLLFITHNL 217
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLP 141
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-228 |
1.08e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 20 ETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypQGDilfhgsslLHADEHTLRgiRGNK--IAMI 97
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKT----TLLKLM--------LGQ--------LQADSGRIH--CGTKleVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 98 FQepmvslnplhslekqlyevlslHRgmrkeaargEILDcLERTGIRNAA-----------KR-----LNDF---PHQ-- 156
Cdd:PRK11147 388 DQ----------------------HR---------AELD-PEKTVMDNLAegkqevmvngrPRhvlgyLQDFlfhPKRam 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 157 -----LSGGERQRVMIAMALLTRPELLIADEPTTALDVtvqaQILTLLRELRDELNMSLLFITHNlsivRKLADNVA 228
Cdd:PRK11147 436 tpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD----RQFVDNTV 504
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
287-515 |
1.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 287 IRKGILRriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEIffddmpLHRWNRRQMLPVRPRMQ 365
Cdd:PRK10938 6 ISQGTFR--LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAgELPLLSGER------QSQFSHITRLSFEQLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 366 VV---FQDPNSSL------NPRLSVLQIIEEGlrVHQPGLSAQQREQevmrvmaeVGLDA--GTRHRYpaeFSGGQRQRI 434
Cdd:PRK10938 78 LVsdeWQRNNTDMlspgedDTGRTTAEIIQDE--VKDPARCEQLAQQ--------FGITAllDRRFKY---LSTGETRKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 435 AIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQGECQRVF 514
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
.
gi 658548496 515 S 515
Cdd:PRK10938 224 Q 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-244 |
1.15e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 125 MRKEAARGEILDCLERTGIRNAAKRLndfPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLREL-R 203
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRA---AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvR 192
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 658548496 204 DelNMSLLFITHNLSIVRKLADNVAVMQNGRCVEQNTASTL 244
Cdd:NF000106 193 D--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-225 |
1.24e-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: 54.63 E-value: 1.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 157 LSGGERQRVMIAMALLTR---PELLIADEPTTAL---DVtvqAQILTLLRELRDELNmSLLFITHNLSIVrKLAD 225
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVI-KTAD 899
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-350 |
1.83e-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: 54.25 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 5 LLSIDNLSIAFStqGETRTVVTDLSLQIQPGETLALVGESGSGKSVSalsiLRLLpSPPVSYPQGDILFHGSSLLH--AD 82
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT----FKML-TGDTTVTSGDATVAGKSILTniSD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 83 EHTlrgirgnkiAMIFQEPMVSLNPLHSLEKQLYEVLSLhRGMRKEAARGEILDCLERTGIRNAAKRLNDfphQLSGGER 162
Cdd:TIGR01257 2010 VHQ---------NMGYCPQFDAIDDLLTGREHLYLYARL-RGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNK 2076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 163 QRVMIAMALLTRPELLIADEPTTALDVTVQAQ----ILTLLRELRdelnmSLLFITHNLSIVRKLADNVAVMQNG--RCV 236
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGafQCL 2151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 237 eqNTASTLLSAPQHPYTQRLLDSEPSGDPVPlaaDSTPllrVEDL-------SVSFPIRKGILRRIVDQNPVLKNIRFSL 309
Cdd:TIGR01257 2152 --GTIQHLKSKFGDGYIVTMKIKSPKDDLLP---DLNP---VEQFfqgnfpgSVQRERHYNMLQFQVSSSSLARIFQLLI 2223
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 658548496 310 RPGESLgLVGESGSGKSTTGLALLRLIASQGEIFfdDMPLH 350
Cdd:TIGR01257 2224 SHKDSL-LIEEYSVTQTTLDQVFVNFAKQQTETY--DLPLH 2261
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
300-477 |
2.09e-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: 54.15 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL-RLIASQGEIFFDDM----PLHRWnrrqMLPVRPRMQVVFQDPNSS 374
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRisfsPQTSW----IMPGTIKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 LNPRlSVLQiieeglrvhqpglsAQQREQEVMrVMAE----VGLDAGTrhrypaEFSGGQRQRIAIARALILKPELIILD 450
Cdd:TIGR01271 516 YRYT-SVIK--------------ACQLEEDIA-LFPEkdktVLGEGGI------TLSGGQRARISLARAVYKDADLYLLD 573
|
170 180
....*....|....*....|....*....
gi 658548496 451 EPTSSLDRTVQAQIL--ALLKGLQEKHRL 477
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFesCLCKLMSNKTRI 602
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
254-518 |
2.49e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 254 QRLLDSEPSGDPvplaadSTPLLRVEDLSVSFPIRKgilrrivdQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL 333
Cdd:PLN03232 599 ERILAQNPPLQP------GAPAISIKNGYFSWDSKT--------SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 334 rliasqGEIffDDMPLHRWNRRQMLPVRPRMQVVFqdpNSSLNPRLSVLQIIEEGLRVHQPGLSAQQREQEVM--RVMAE 411
Cdd:PLN03232 665 ------GEL--SHAETSSVVIRGSVAYVPQVSWIF---NATVRENILFGSDFESERYWRAIDVTALQHDLDLLpgRDLTE 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 412 VGlDAGTrhrypaEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL--ALLKGLQEKHRlayIFISHDLQVV 489
Cdd:PLN03232 734 IG-ERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdsCMKDELKGKTR---VLVTNQLHFL 803
|
250 260
....*....|....*....|....*....
gi 658548496 490 rALCHQVIVLRQGEVVEQGECQRVFSAPT 518
Cdd:PLN03232 804 -PLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
284-511 |
3.99e-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: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 284 SFPIRKGILRRIVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLR-------LIASQGEIFFddMPLHRWNRRQ 356
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemdkvegHVHMKGSVAY--VPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 MLpvrpRMQVVFQDPnssLNPR-----------LSVLQIIEEGLRVHqpglsaqqreqevmrvMAEVGLDagtrhrypae 425
Cdd:TIGR00957 714 SL----RENILFGKA---LNEKyyqqvleacalLPDLEILPSGDRTE----------------IGEKGVN---------- 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 426 FSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKG----LQEKHRlayIFISHDLQVVRALcHQVIVLRQ 501
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHGISYLPQV-DVIIVMSG 836
|
250
....*....|
gi 658548496 502 GEVVEQGECQ 511
Cdd:TIGR00957 837 GKISEMGSYQ 846
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-219 |
4.24e-07 |
|
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: 52.83 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypqGDI--LFHGssllhadehTLRGIRGNKIAMIFQEP 101
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKS----SLFRIL---------GELwpVYGG---------RLTKPAKGKLFYVPQRP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 102 MVSLNPLHslEKQLYEVLSLH---RGMRkEAARGEILD------CLERTGIRNAakrLNDFPHQLSGGERQRVMIAMALL 172
Cdd:TIGR00954 525 YMTLGTLR--DQIIYPDSSEDmkrRGLS-DKDLEQILDnvqlthILEREGGWSA---VQDWMDVLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658548496 173 TRPELLIADEPTTALDVTVQAQILTLLRelrdELNMSLLFITHNLSI 219
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSL 641
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
307-484 |
4.47e-07 |
|
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: 52.44 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 307 FSLRPGESLGLVGESGSGKSTtglaLLRLIASQGEIFFDDMPLHRWNRRQMLPVRPRM-------QVVFQDpnsslnprl 379
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSS----LFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMtlgtlrdQIIYPD--------- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 380 SVLQIIEEGLR--VHQPGLSAQQREQEVMRvmaEVGLDAgtRHRYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:TIGR00954 540 SSEDMKRRGLSdkDLEQILDNVQLTHILER---EGGWSA--VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*..
gi 658548496 458 RTVQAQILALLKglqeKHRLAYIFISH 484
Cdd:TIGR00954 615 VDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
427-503 |
4.72e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.30 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQ------RIAIARALILKPELIILDEPTSSLDR-TVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 658548496 500 RQGE 503
Cdd:cd03240 197 KDGR 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-225 |
4.82e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 4.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548496 157 LSGGERQRVMIA--MALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNmSLLFITHNLSIVrKLAD 225
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVL-SSAD 156
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
164-505 |
5.16e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 164 RVMIAMALLTRPELLIADEPTTALDvtvqaqILTLlRELRDELNM---SLLFITHNLSIVRKLADNVAVMQNG--RCVEQ 238
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD------INTI-RWLEDVLNErnsTMIIISHDRHFLNSVCTHMADLDYGelRVYPG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 239 N-----TAST-----LLS-------------------------APQHPYTQRLLDsEPSGDPVPLAADSTPLLR------ 277
Cdd:PRK15064 236 NydeymTAATqarerLLAdnakkkaqiaelqsfvsrfsanaskAKQATSRAKQID-KIKLEEVKPSSRQNPFIRfeqdkk 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 278 -------VEDLSVSFpirkgilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAS-----QGEIffd 345
Cdd:PRK15064 315 lhrnaleVENLTKGF-----------DNGPLFKNLNLLLEAGERLAIIGENGVGKTT----LLRTLVGelepdSGTV--- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 346 dmplhRWNRRQMLPVRPrmqvvfQDPNSSLNPRLSVLQIIEEglrVHQPGlsaqQREQEVMRVMAEVGLDAGTRHRYPAE 425
Cdd:PRK15064 377 -----KWSENANIGYYA------QDHAYDFENDLTLFDWMSQ---WRQEG----DDEQAVRGTLGRLLFSQDDIKKSVKV 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 426 FSGGQRQRIAIARALILKPELIILDEPTSSLD-RTVQAQILALlkglqEKHRLAYIFISHDLQVVRALCHQVIVLRQGEV 504
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDmESIESLNMAL-----EKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
.
gi 658548496 505 V 505
Cdd:PRK15064 514 V 514
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-233 |
5.66e-07 |
|
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: 50.41 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 15 FSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPpvsypQGDILFHGSSLLHADEHTLRGIRGNKI 94
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL-----EGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 95 AMIFQEPMVsLNPL--------HSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIrnAAKRLNdfphqLSGGERQRVM 166
Cdd:cd03290 82 AYAAQKPWL-LNATveenitfgSPFNKQRYKAVTDACSLQPDI---DLLPFGDQTEI--GERGIN-----LSGGQRQRIC 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 167 IAMALLTRPELLIADEPTTALDV-----TVQAQILTLLRELRdelnMSLLFITHNLSIVRKlADNVAVMQNG 233
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDK----RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
157-225 |
5.82e-07 |
|
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: 51.08 E-value: 5.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658548496 157 LSGGERQRVMIAMALL---TRPELLIADEPTTALDVTVQAQILTLLRELRDELNmSLLFITHNLSIVrKLAD 225
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVI-KCAD 239
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-231 |
5.96e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 5.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAVMQ 231
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-249 |
6.96e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSILRLlpsppVSYPQGDILFHGSSLlhaDEHTLRGIRgNKIAMIFQEPM- 102
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-----VEVCGGEIRVNGREI---GAYGLRELR-RQFSMIPQDPVl 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 ----VSLNPLHSLEKQLYEV---LSLhRGMRKEAARgeildclERTGIRNaakRLNDFPHQLSGGERQRVMIAMALLTRP 175
Cdd:PTZ00243 1396 fdgtVRQNVDPFLEASSAEVwaaLEL-VGLRERVAS-------ESEGIDS---RVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 176 ELLI-ADEPTT----ALDVTVQAQILTLLRelrdelNMSLLFITHNLSIVRKLaDNVAVMQNGRCVEQNTASTLLSAPQ 249
Cdd:PTZ00243 1465 SGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
280-471 |
7.48e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 280 DLSVSFPIRKGILRrivdqnpVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ---GEIFFDDMplhrwnrrq 356
Cdd:TIGR00956 764 NLTYEVKIKKEKRV-------ILNNVDGWVKPGTLTALMGASGAGKTT----LLNVLAERvttGVITGGDR--------- 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 MLPVRPRmQVVF---------QDPNSslnPRLSVLQIIEEGLRVHQPG-LSAQQREQEVMRVMAEVGL----DA--GTrh 420
Cdd:TIGR00956 824 LVNGRPL-DSSFqrsigyvqqQDLHL---PTSTVRESLRFSAYLRQPKsVSKSEKMEYVEEVIKLLEMesyaDAvvGV-- 897
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658548496 421 ryPAE-FSGGQRQRIAIARALILKPELII-LDEPTSSLDRTVQAQILALLKGL 471
Cdd:TIGR00956 898 --PGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
148-229 |
8.71e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 148 KRLNDfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNV 227
Cdd:PRK13409 449 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
..
gi 658548496 228 AV 229
Cdd:PRK13409 525 MV 526
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-225 |
8.74e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 8.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVtvqAQILTLLRELRDELNmSLLFITHNLSIVrKLAD 225
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVI-KTAD 896
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
308-509 |
9.17e-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: 50.10 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 308 SLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEIFFDDMPlhrwnrrqmlPVRPRMQVVFQDPNSSLNPRLSVLQIIEE 387
Cdd:cd03237 21 SISESEVIGILGPNGIGKTT----FIKMLA--GVLKPDEGD----------IEIELDTVSYKPQYIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 388 GLRVHqpgLSAQQREQEVMRVMaevGLDAGTRHRYPaEFSGGQRQRIAIARALILKPELIILDEPTSSLDrtVQAQILA- 466
Cdd:cd03237 85 ITKDF---YTHPYFKTEIAKPL---QIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMAs 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 658548496 467 -LLKGLQEKHRLAYIFISHDLQVVRALCHQVIVLrQGEVVEQGE 509
Cdd:cd03237 156 kVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
284-506 |
1.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 284 SFPIRKGIlrRIVdqnpvLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEIFFDDMPLHRW-NRRQMLPV 360
Cdd:PRK10636 6 SLQIRRGV--RVL-----LDNATATINPGQKVGLVGKNGCGKSTL-LALLKneISADGGSYTFPGNWQLAWvNQETPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 361 RPRMQVV-------------FQDPN--------SSLNPRLSVLQIIEEGLR----VHQPGLSAQQREQEVmrvmaevgld 415
Cdd:PRK10636 78 QPALEYVidgdreyrqleaqLHDANerndghaiATIHGKLDAIDAWTIRSRaaslLHGLGFSNEQLERPV---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 416 agtrhrypAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEkhrlAYIFISHDLQVVRALCHQ 495
Cdd:PRK10636 148 --------SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDK 215
|
250
....*....|.
gi 658548496 496 VIVLRQGEVVE 506
Cdd:PRK10636 216 IIHIEQQSLFE 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
300-508 |
1.35e-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: 51.55 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 300 PVLKNIRFSLRPGESLGLVGESGSGKSTTgLALLR--LIASQGEIFF--DDMPLHRWNRRQMLPVRPRMQVVFQDpnssl 375
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTglLPPTSGTVLVggKDIETNLDAVRQSLGMCPQHNILFHH----- 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 nprlsvLQIIEEGLRVHQPGLSAQQREQEVMRVMAEvglDAGTRHRYPAE---FSGGQRQRIAIARALILKPELIILDEP 452
Cdd:TIGR01257 1018 ------LTVAEHILFYAQLKGRSWEEAQLEMEAMLE---DTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 658548496 453 TSSLDRTVQAQILALLkgLQEKHRLAYIFISHDLQVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-509 |
1.47e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 275 LLRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALL---RLIASQGEIFFDDmplhr 351
Cdd:PRK09580 1 MLSIKDLHVS-----------VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgreDYEVTGGTVEFKG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 352 wnrRQMLPVRPRMQ------VVFQDP------------NSSLNP-----------RLSVLQIIEEGLRVhqpglsaQQRE 402
Cdd:PRK09580 65 ---KDLLELSPEDRagegifMAFQYPveipgvsnqfflQTALNAvrsyrgqepldRFDFQDLMEEKIAL-------LKMP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 403 QEVMRVMAEVGldagtrhrypaeFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFI 482
Cdd:PRK09580 135 EDLLTRSVNVG------------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIV 201
|
250 260
....*....|....*....|....*...
gi 658548496 483 SHDLQVVRALCHQ-VIVLRQGEVVEQGE 509
Cdd:PRK09580 202 THYQRILDYIKPDyVHVLYQGRIVKSGD 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
310-488 |
1.91e-06 |
|
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: 49.29 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 310 RPGESLGLVGESGSGKSTTglalLRLIASQ-----GEifFDDMP-------------LHRWNRR----QMLPVRpRMQVV 367
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTA----LKILAGKlkpnlGK--FDDPPdwdeildefrgseLQNYFTKllegDVKVIV-KPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 368 FQDPNSSlnpRLSVLQIIEeglRVHQPGlsaqqREQEVMRVMaevGLDaGTRHRYPAEFSGGQRQRIAIARALILKPELI 447
Cdd:cd03236 97 DLIPKAV---KGKVGELLK---KKDERG-----KLDELVDQL---ELR-HVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 658548496 448 ILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQV 488
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAV 201
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
157-225 |
1.97e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.84 E-value: 1.97e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 157 LSGGERQRVMIAMALLTRP---ELLIADEPTTAL---DVtvqAQILTLLRELRDELNmSLLFITHNLSIVrKLAD 225
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDI---RKLLEVLHRLVDKGN-TVVVIEHNLDVI-KTAD 900
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
255-370 |
2.49e-06 |
|
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: 50.18 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 255 RLLDSEPSGDPVPLAADSTPL------LRVEDLSVSFPIRKGilrrivDQNPVLKNIRFSLRPGESLGLVGESGSGKSTt 328
Cdd:COG4615 301 ELELALAAAEPAAADAAAPPApadfqtLELRGVTYRYPGEDG------DEGFTLGPIDLTIRRGELVFIVGGNGSGKST- 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 658548496 329 glaLLRLI-----ASQGEIFFDDMPLHRWNR---RQMlpvrprMQVVFQD 370
Cdd:COG4615 374 ---LAKLLtglyrPESGEILLDGQPVTADNReayRQL------FSAVFSD 414
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
421-509 |
2.72e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 421 RYPAEFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLR 500
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVID 218
|
....*....
gi 658548496 501 QGEVVEQGE 509
Cdd:NF000106 219 RGRVIADGK 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
272-457 |
3.43e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 272 STPLLRVEDLSVSfpirkgilrriVDQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIA-----SQGEIFFDD 346
Cdd:PRK13543 8 APPLLAAHALAFS-----------RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTT----LLRVLAgllhvESGQIQIDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 347 MPLHRWNRRQMLPVRPRMqvvfqdpnSSLNPRLSVLQIIEeglrvHQPGLSAQQREQEVMRVMAEVGLdAGTRHRYPAEF 426
Cdd:PRK13543 73 KTATRGDRSRFMAYLGHL--------PGLKADLSTLENLH-----FLCGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQL 138
|
170 180 190
....*....|....*....|....*....|.
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLD 457
Cdd:PRK13543 139 SAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
302-513 |
3.90e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIAsqGEIFFDDMPLHRWNRRQMLPVrprmqvvfqdpNSSLNPRLSV 381
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKST----LSNIIG--GSLSPTVGKVDRNGEVSVIAI-----------SAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 382 LQIIEEGLrvhqpgLSAQQREQEVMRVMAEV--GLDAGTRHRYPAE-FSGGQRQRIAIARALILKPELIILDEPTSSLDR 458
Cdd:PRK13546 103 IENIEFKM------LCMGFKRKEIKAMTPKIieFSELGEFIYQPVKkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 459 TVQAQILALLKGLQEKHRLAYiFISHDLQVVRALCHQVIVLRQGEVVEQGECQRV 513
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIF-FVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-192 |
4.84e-06 |
|
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: 48.31 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFSTQGETrtVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLpsppvsYPQGDILFHGSSLLHADEHT 85
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LR---GIRGNKIaMIFQEPM-VSLNPLHSLEKQlyevlslhrgmrkeaargEILDCLERTGIRNAakrLNDFPHQ----- 156
Cdd:cd03289 75 WRkafGVIPQKV-FIFSGTFrKNLDPYGKWSDE------------------EIWKVAEEVGLKSV---IEQFPGQldfvl 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 658548496 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALD-VTVQ 192
Cdd:cd03289 133 vdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
302-508 |
6.58e-06 |
|
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: 47.25 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 302 LKNIRFSLRPGESLGLVGESGSGKSTtgLAL--------LRLIASQGEIFfddmplhrwnrRQMLPVRPRMQVVF----- 368
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSS--LAFdtiyaegqRRYVESLSAYA-----------RQFLGQMDKPDVDSiegls 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 369 -----QDPNSSLNPRLSVLQIIE--EGLRVhqpgLSAQQREQEVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARAL- 440
Cdd:cd03270 78 paiaiDQKTTSRNPRSTVGTVTEiyDYLRL----LFARVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIg 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548496 441 -ILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVRALCHQVIV-----LRQGEVVEQG 508
Cdd:cd03270 154 sGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
157-247 |
7.67e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDElNMSLLFITHNLSIVRKLADNVAVMQNGRCV 236
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
90
....*....|....*.
gi 658548496 237 -----EQNTASTLLSA 247
Cdd:PRK11288 476 gelarEQATERQALSL 491
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-265 |
8.54e-06 |
|
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: 43.54 E-value: 8.54e-06
10 20 30
....*....|....*....|....*....|
gi 658548496 236 VEQNTASTLLSAPQHPYTQRLLDSEPSGDP 265
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-224 |
8.58e-06 |
|
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: 45.83 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 34 PGETLALVGESGSGKSVSALSILRLLPSPpvsypqgdilfHGSSLLHADEHTlrgirgnkiamifqepmvslnplhslek 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-----------GGGVIYIDGEDI---------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 114 qlyevlslhrgmrkeaargeildcLERTGIRNAAKRLNDFPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQA 193
Cdd:smart00382 42 ------------------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190
....*....|....*....|....*....|....*.
gi 658548496 194 QIL-----TLLRELRDELNMSLLFITHNLSIVRKLA 224
Cdd:smart00382 98 LLLlleelRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-501 |
9.03e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.81 E-value: 9.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 427 SGGQRQRIAIARALIL---KPE-LIILDEPTSSLDRTVQAQILALLKGLQeKHRLAYIFISHDLQVVRALCHQVIVLRQ 501
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
427-508 |
9.23e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQIL-ALLKG-LQEKHRLAYIFISHDLQVVralcHQVIVLRQGEV 504
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDeLRGKTRVLVTNQLHFLSQV----DRIILVHEGMI 817
|
....
gi 658548496 505 VEQG 508
Cdd:PLN03130 818 KEEG 821
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
157-229 |
9.79e-06 |
|
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: 47.02 E-value: 9.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITHNLSIVRKLADNVAV 229
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-327 |
1.17e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLT---RPELLIADEPTTALDVTVQAQILTLLRELRDeLNMSLLFITHNLSIVrKLADNVAVMQNg 233
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVV-KVADYVLELGP- 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 234 rcvEQNTASTLLSAPQHPYTQRLLDSEPSGDPVPLAADSTPLLRVEDLSVSFPIRKGILRRIVDQNPvLKNIRFSLrPGE 313
Cdd:PRK00635 887 ---EGGNLGGYLLASCSPEELIHLHTPTAKALRPYLSSPQELPYLPDPSPKPPVPADITIKNAYQHN-LKHIDLSL-PRN 961
|
170
....*....|....*
gi 658548496 314 SLGLV-GESGSGKST 327
Cdd:PRK00635 962 ALTAVtGPSASGKHS 976
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-295 |
1.71e-05 |
|
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: 47.63 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 28 LSLQIQPGETLALVGESGSGKSvSALSILRllpsPPVSYPQGDILFHGSSLLHADEHTLRG--IRGNkiaMIFQEPmvsL 105
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKS-SLLSALL----AEMDKVEGHVHMKGSVAYVPQQAWIQNdsLREN---ILFGKA---L 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 106 NPLHSleKQLYEVLSLHRGMrkeaargEILDCLERTGIrnAAKRLNdfphqLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:TIGR00957 726 NEKYY--QQVLEACALLPDL-------EILPSGDRTEI--GEKGVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 186 ALDVTVQAQILTLLRELRDEL-NMSLLFITHNLSIVRKLaDNVAVMQNGRCVEQNTASTLLSAP--------QHPYTQRL 256
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDgafaeflrTYAPDEQQ 868
|
250 260 270
....*....|....*....|....*....|....*....
gi 658548496 257 LDSEPSGDPVPLAADSTPLLRVEDLSVSFPIRKGILRRI 295
Cdd:TIGR00957 869 GHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQL 907
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-258 |
2.03e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 3 QPLLSIDNLSIAFSTQGEtRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPSPP---------VSY-PQGDIL 72
Cdd:PLN03130 612 LPAISIKNGYFSWDSKAE-RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirgtVAYvPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 73 FHGSsllhadehtlrgIRGNkiaMIFQEPmvslnplhsLEKQLYE----VLSLHRGMrkeaargEILDCLERTGIrnAAK 148
Cdd:PLN03130 691 FNAT------------VRDN---ILFGSP---------FDPERYEraidVTALQHDL-------DLLPGGDLTEI--GER 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 149 RLNdfphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTllRELRDEL-NMSLLFIT---HNLSIVrkla 224
Cdd:PLN03130 738 GVN-----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTnqlHFLSQV---- 806
|
250 260 270
....*....|....*....|....*....|....
gi 658548496 225 DNVAVMQNGRCVEQNTASTLLSapQHPYTQRLLD 258
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSN--NGPLFQKLME 838
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-237 |
2.78e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 18 QGETRTVVTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPspPVSypqGDILFHGSSLLHADEHTLRGirgnkiami 97
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS--PTV---GKVDRNGEVSVIAISAGLSG--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 98 fqepmvslnPLHSLEKQLYEVLSLhrGM-RKE--AARGEILDCLErtgirnaakrLNDFPHQ----LSGGERQRVMIAMA 170
Cdd:PRK13546 99 ---------QLTGIENIEFKMLCM--GFkRKEikAMTPKIIEFSE----------LGEFIYQpvkkYSSGMRAKLGFSIN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 171 LLTRPELLIADEPTTALDVTVQAQILTLLRELRdELNMSLLFITHNLSIVRKLADNVAVMQNGRCVE 237
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-244 |
2.80e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 4 PLLSIDNLSIAFSTQGETRTVvTDLSLQIQPGETLALVGESGSGKSVSALSILRLLPsppvsypqgdilfhgssllHAdE 83
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSKPTL-SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-------------------HA-E 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 84 HTLRGIRGNkIAMIFQEPMVSLNPLHS--LEKQLYEVLSLHRGMRKEAARGEiLDCLERTGIRNAAKR-LNdfphqLSGG 160
Cdd:PLN03232 672 TSSVVIRGS-VAYVPQVSWIFNATVREniLFGSDFESERYWRAIDVTALQHD-LDLLPGRDLTEIGERgVN-----ISGG 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 161 ERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLreLRDELN-MSLLFITHNLSIVrKLADNVAVMQNGRCVEQN 239
Cdd:PLN03232 745 QKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC--MKDELKgKTRVLVTNQLHFL-PLMDRIILVSEGMIKEEG 821
|
....*
gi 658548496 240 TASTL 244
Cdd:PLN03232 822 TFAEL 826
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-224 |
3.75e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 6 LSIDNLSIAFstqgETRTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLpsppvsypQGDilfhgsslLHADEHT 85
Cdd:PRK15064 320 LEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKT----TLLRTL--------VGE--------LEPDSGT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 86 LRGIRGNKIAMIFQEPmvslnplhslEKQLYEVLSLHRGMRKEAARGEildclERTGIRNAAKRL----NDFPHQ---LS 158
Cdd:PRK15064 376 VKWSENANIGYYAQDH----------AYDFENDLTLFDWMSQWRQEGD-----DEQAVRGTLGRLlfsqDDIKKSvkvLS 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVtvqaqiltllrELRDELNM-------SLLFITHNLSIVRKLA 224
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM-----------ESIESLNMalekyegTLIFVSHDREFVSSLA 502
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
425-499 |
4.75e-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: 4.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAYIFISHDLQVVRALCHQVIVL 499
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-227 |
6.51e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 6.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548496 156 QLSGGERQ------RVMIAMALLTRPELLIADEPTTALDV-TVQAQILTLLRELRDELNMSLLFITHNLSIVRkLADNV 227
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVD-AADHI 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-260 |
8.10e-05 |
|
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: 45.67 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSIL-RLLPSppvsypQGDILFHGssllhadehtlrgirgnKIAMIFQEP- 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPS------EGKIKHSG-----------------RISFSPQTSw 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 102 ----MVSLNPLHSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRnaakrLNDFPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:TIGR01271 498 impgTIKDNIIFGLSYDEYRYTSVIKACQLEE---DIALFPEKDKTV-----LGEGGITLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 178 LIADEPTTALDVTVQAQIL-TLLRELRdeLNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTlLSAPQHPYTQRL 256
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFeSCLCKLM--SNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSE-LQAKRPDFSSLL 645
|
....
gi 658548496 257 LDSE 260
Cdd:TIGR01271 646 LGLE 649
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-246 |
1.02e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.08 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 24 VVTDLSLQIQPGETLALVGESGSGKSVSALSIL-RLLPSppvsypQGDIlfhgssllhadEHTLRGIRGNKIAMIFqEPM 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPS------EGKI-----------KHSGRISFSSQFSWIM-PGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 103 VSLNPLHSLEKQLYEVLSLHRGMRKEAargEILDCLERTGIRNAAKRLNdfphqLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVVKACQLEE---DITKFPEKDNTVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548496 183 PTTALDVTVQAQIL-TLLRELRdeLNMSLLFITHNLSIVRKlADNVAVMQNGRCVEQNTASTLLS 246
Cdd:cd03291 186 PFGYLDVFTEKEIFeSCVCKLM--ANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQS 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
425-499 |
1.04e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQilaLLKGLQEKHRlAYIFISHDLQVVRALCHQVIVL 499
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVAR---LIRELAEEGK-YVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-215 |
1.54e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 22 RTVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSppvSYPQG-------------------DILFH-G--SSLL 79
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKS----TLLSLITG---DHPQGysndltlfgrrrgsgetiwDIKKHiGyvSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 80 HADEHTLRGIRGNKIAMIFQepmvSLNplhslekqLYEVLSlhrgmrkEAARGEILDCLERTGIrnaAKRLNDFP-HQLS 158
Cdd:PRK10938 346 HLDYRVSTSVRNVILSGFFD----SIG--------IYQAVS-------DRQQKLAQQWLDILGI---DKRTADAPfHSLS 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658548496 159 GGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQILTLLRELRDELNMSLLFITH 215
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
425-499 |
2.41e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548496 425 EFSGGQRQRIAIARALILKPELIILDEPTSSLD---RTVQAQilaLLKGLQEKHrlAYIFISHDLQVVRALCHQVIVL 499
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqRLNVAR---LIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
301-509 |
3.47e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 301 VLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQGEIFFDDMplhrWNRRQM--LPVRP-------RMQVVFQDP 371
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKST----LLQSLLSQFEISEGRV----WAERSIayVPQQAwimnatvRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 372 NSSlnPRLSvlqiieEGLRVHQPGLSAQQREQEVMRVMAEVGLDagtrhrypaeFSGGQRQRIAIARALILKPELIILDE 451
Cdd:PTZ00243 747 EDA--ARLA------DAVRVSQLEADLAQLGGGLETEIGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548496 452 PTSSLD-----RTVQAQILALLKGlqeKHRlayIFISHDLQVVrALCHQVIVLRQGEVVEQGE 509
Cdd:PTZ00243 809 PLSALDahvgeRVVEECFLGALAG---KTR---VLATHQVHVV-PRADYVVALGDGRVEFSGS 864
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
404-508 |
4.68e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.22 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 404 EVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALiLKPE----LIILDEPTSSLDRTVQAQILALLKGLQEKHRLAy 479
Cdd:cd03271 148 RKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTV- 225
|
90 100 110
....*....|....*....|....*....|....*
gi 658548496 480 IFISHDLQVVRAlCHQVIVL------RQGEVVEQG 508
Cdd:cd03271 226 VVIEHNLDVIKC-ADWIIDLgpeggdGGGQVVASG 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-204 |
6.15e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 10 NLSIAFSTQGETRTVVTDLSLQIQPGETLALVGESGSGKSvSALSIL--RLlpspPVSYPQGDIlfhgssllhadehtlR 87
Cdd:TIGR00956 764 NLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKT-TLLNVLaeRV----TTGVITGGD---------------R 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 88 GIRGNKIAMIFQEPM--VSLNPLHSLEKQLYEVLSLHRGMR--KEAARGE-------ILDCLERTGIRNAakrLNDFPHQ 156
Cdd:TIGR00956 824 LVNGRPLDSSFQRSIgyVQQQDLHLPTSTVRESLRFSAYLRqpKSVSKSEkmeyveeVIKLLEMESYADA---VVGVPGE 900
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 -LSGGERQRVMIAMALLTRPELLI-ADEPTTALDVTVQAQILTLLRELRD 204
Cdd:TIGR00956 901 gLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD 950
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
297-485 |
6.53e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTTGLALLRL-IASQGEIFFDDMPLHRWNRRQMlpvRPRMQVVFQDPNssL 375
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTAEQPEDY---RKLFSAVFTDFH--L 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 376 NPRLsvlqIIEEGLRVhQPGLSAQQREQEVMR--VMAEVGLDAGTRhrypaeFSGGQRQRIAIARALILKPELIILDEPT 453
Cdd:PRK10522 409 FDQL----LGPEGKPA-NPALVEKWLERLKMAhkLELEDGRISNLK------LSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190
....*....|....*....|....*....|....*.
gi 658548496 454 SSLD---RTVQAQIlaLLKGLQEKHRLayIF-ISHD 485
Cdd:PRK10522 478 ADQDphfRREFYQV--LLPLLQEMGKT--IFaISHD 509
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
297-457 |
7.54e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 297 DQNPVLKNIRFSLRPGESLGLVGESGSGKSTtglaLLRLIASQ--GEIFFDDMPLHRWNRRQMLPVRPRMQVVFQDPNSs 374
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTT----LMDVLAGRktGGYIEGDIRISGFPKKQETFARISGYCEQNDIHS- 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 375 lnPRLSVLQ--IIEEGLRvhqpgLSAQQREQEVMR----VM----------AEVGLDAGTrhrypaEFSGGQRQRIAIAR 438
Cdd:PLN03140 966 --PQVTVREslIYSAFLR-----LPKEVSKEEKMMfvdeVMelveldnlkdAIVGLPGVT------GLSTEQRKRLTIAV 1032
|
170
....*....|....*....
gi 658548496 439 ALILKPELIILDEPTSSLD 457
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLD 1051
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-499 |
1.15e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALltRPELL----IADEPTTALDVTVQAQILTLLRELRDELNmSLLFITHNLSIVrKLADnvavmqn 232
Cdd:PRK00635 477 LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLAD------- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 233 grcveqntastllsapqhpytqRLLDSEP-----------SGDPVPLAADSTPL----LRVEdLSVSFPIRKG------I 291
Cdd:PRK00635 546 ----------------------RIIDIGPgagifggevlfNGSPREFLAKSDSLtakyLRQE-LTIPIPEKRTnslgtlT 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 292 LRRIVDQNpvLKNIRFSLRPGESLGLVGESGSGKST------------------------TGLALLRLI--------ASQ 339
Cdd:PRK00635 603 LSKATKHN--LKDLTISLPLGRLTVVTGVSGSGKSSlindtlvpaveefieqgfcsnlsiQWGAISRLVhitrdlpgRSQ 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 340 GEI------FFDDMplhrwnrRQMLPVRPRMQ---------------------------VVFQDPNSSLNPRLSVLQIIE 386
Cdd:PRK00635 681 RSIpltyikAFDDL-------RELFAEQPRSKrlgltkshfsfntplgacaecqglgsiTTTDNRTSIPCPSCLGKRFLP 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 387 EGLRVHQPG--------LSAQQREQ---------EVMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAIARALIL---KPEL 446
Cdd:PRK00635 754 QVLEVRYKGkniadileMTAYEAEKffldepsihEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTL 833
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 658548496 447 IILDEPTSSL-DRTVQAQILALLKGLQEKHRLayIFISHDLQVVRaLCHQVIVL 499
Cdd:PRK00635 834 YVLDEPTTGLhTHDIKALIYVLQSLTHQGHTV--VIIEHNMHVVK-VADYVLEL 884
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
282-529 |
1.76e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 282 SVSFPIRKGILRRIVDQnpvlknIRFSLRPGESL--GLVGESGSGKSTTGLALLRLIAS-QGEIF--FDDMPLHRWnrrq 356
Cdd:PRK00635 363 TLTHKVWRGVLNEIGEK------VRYSNKPSRYLpkGTSATSCPRCQGTGLGDYANAATwHGKTFaeFQQMSLQEL---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 357 mlpvrprmqVVFqdpNSSLNPRLSVLQIIEEGLRvhqpglsaqQReqevMRVMAEVGLDAGTRHRYPAEFSGGQRQRIAI 436
Cdd:PRK00635 433 ---------FIF---LSQLPSKSLSIEEVLQGLK---------SR----LSILIDLGLPYLTPERALATLSGGEQERTAL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 437 ARAliLKPELI----ILDEPTSSLDRTVQAQILALLKGLQEKHRlAYIFISHDLQVVrALCHQVIVLRQ------GEVVE 506
Cdd:PRK00635 488 AKH--LGAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRIIDIGPgagifgGEVLF 563
|
250 260
....*....|....*....|....*.
gi 658548496 507 QGECQRVF---SAPTQRYTRQLLSAD 529
Cdd:PRK00635 564 NGSPREFLaksDSLTAKYLRQELTIP 589
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-188 |
2.82e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 1 MTQPLLSIDNL----SIAFSTQGETrtVVTDLSLQIQPGETLALVGESGSGKSvsalSILRLLPSppvsypqgdILFHGS 76
Cdd:PRK13543 1 MIEPLHTAPPLlaahALAFSRNEEP--VFGPLDFHVDAGEALLVQGDNGAGKT----TLLRVLAG---------LLHVES 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 77 SLLHAD-EHTLRGIRGNKIAMIFQEPmvSLNPLHSLEKQLYEVLSLHrGMRKEAARGEILDCLERTGIRNAAKRlndfph 155
Cdd:PRK13543 66 GQIQIDgKTATRGDRSRFMAYLGHLP--GLKADLSTLENLHFLCGLH-GRRAKQMPGSALAIVGLAGYEDTLVR------ 136
|
170 180 190
....*....|....*....|....*....|...
gi 658548496 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
Cdd:PRK13543 137 QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
427-508 |
5.67e-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: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 427 SGGQRQRIAIARALILK---PELIILDEPTSSLDRTVQAQILALLKGLQEKHRLAyIFISHDLQVVRALCHqVIVL---- 499
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVIEHNLDVIKTADY-IIDLgpeg 908
|
90
....*....|.
gi 658548496 500 --RQGEVVEQG 508
Cdd:TIGR00630 909 gdGGGTVVASG 919
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
157-234 |
7.15e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548496 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVTVQAQIL--TLLRELRDElnmSLLFITHNLSIVrKLADNVAVMQNGR 234
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeeCFLGALAGK---TRVLATHQVHVV-PRADYVVALGDGR 858
|
|
| |
